UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
|
|---|---|---|
P46643 | MALAMMIRNAASKRGMTPISGHFGGLRSMSSWWKSVEPAPKDPILGVTEAFLADPSPEKVNVGVGAYRDDNGKPVVLECVREAEKRLAGSTFMEYLPMGGSAKMVDLTLKLAYGDNSEFIKDKRIAAVQTLSGTGACRLFADFQKRFSPGSQIYIPVPTWSNHHNIWKDAQVPQKTYHYYHPETKGLDFSALMDDVKNAPEGSFFLLHACAHNPTGVDPTEEQWREISQLFKAKKHFAFFDMAYQGFASGDPARDAKSIRIFLEDGHHIGISQSYAKNMGLYGQRVGCLSVLCEDPKQAVAVKSQLQQLARPMYSNPPLHGAQLVSTILEDPELKSLWLKEVKVMADRIIGMRTTLRESLEKLGSPLSWEHVTKQIGMFCYSGLTPEQVDRLTSEYHIYMTRNGRISMAGVTTGNVGYLANAIHEVTKSS | Amino acid aminotransferase important for the metabolism of amino acids and Krebs-cycle related organic acids. No activity with D-Asp or D-Ala as amino donors. In plants, it is involved in nitrogen metabolism and in aspects of carbon and energy metabolism. 2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate kcat is 205 sec(-1) for the forward reaction. kcat is 319 sec(-1) for the reverse reaction. Homodimer. In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. |
P53001 | MKLAKRVSALTPSTTLAITAKAKELKAAGHDVIGLGAGEPDFNTPQHIIDAAVRSMNEGHTKYTPSGGLAELKNSIAEKFKRDQNIEYKPSQIIVCTGAKHALYTLFQVILDEEDEVIIPTPYWVSYPEQVKLAGGKPVYVEGLEENHFKISPEQLKNAITEKTKAIVINSPSNPTGVMYTEEELSALGEVCLEHDILIVSDEIYEKLTYGGKKHVSIAQLSDRLKEQTVIINGVSKSHSMTGWRIGYAAGSEDIIKAMTNLASHSTSNPTSIAQYGAIAAYNGPSEPLEEMREAFEHRLNTIYAKLIEIPGFSCVKPEGAFYLFPNAKEAAQSCGFKDVDEFVKALLEEEKVAIVPGSGFGSPENVRLSYATSLDLLEEAIERIKRFVEKHS | 2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate Homodimer. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. |
Q40324 | MASQNITPSPTASSDSVFAHLVRAPEDPILGVTVAYNKDPSPIKLNLGVGAYRTEEGKPLVLDVVRRVERQLLNDMSRNKEYIPIVGLADFNKLSAKLIFGADSPAIQENRVTTVQGLSGTGSLRVGGEFLAKHYHQRIIYLPTPTWGNHTKVFNLAGLTVKTYRYYAPATRGLDFQGLLEDLGSAPSGSVVLLHACAHNPTGVDPTLEQWEQIRQLIRSKSLLPFFDSAYQGFASGSLDADAQPVRLFVADGGELLVAQSYAKNMGLYGERVGALSIVSKSADVSSRVESQLKLVIRPMYSSPPIHGASIVAAILKDRDLYNDWTIELKAMADRIINMRQQLFDALRARGTPGDWSHIIKQIGMFTFTGLNPEQVSILTKEYHIYLTSDGRISMAGLSSKTVPHLAHAIHAVVTRVA | Important for the metabolism of amino acids and Krebs-cycle related organic acids. In plants, it is involved in nitrogen metabolism and in aspects of carbon and energy metabolism. 2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate Homodimer. Nodules, roots, stems and leaves, in decreasing order of aspartate aminotransferase 1 concentration. Is the predominant aspartate aminotransferase isoenzyme in roots. In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. |
P85906 | LNLGVGAYREYLPIEGLAAFNKVATVQGLSGTGSLRQALYDSISSK | Important for the metabolism of amino acids and Krebs-cycle related organic acids. In plants, it is involved in nitrogen metabolism and in aspects of carbon and energy metabolism (By similarity). 2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate Homodimer. In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. |
Q7FLL4 | MATLYSQVPSVSAVFSLYTSFSAITMLFRTILNEIVPKRIREYIAMKAVDFFSSYFQSDFTFVIEQRWEFVENQTFRAAEVYLPTCLAGLSTGKLLVGSSNLKNPAAEPKLGIPVNTKIIDNFEGIHLEWTLHSVETKKYLPEKRYFHLTCKKEFREKIMTDYFTYLAKSAEKIMSHRENLKIYTYNQDRSKWESAIFEHHTTFETLAVEPDLKKTLIDDLDAFSKGKDFFKSVGRAWKRGYLLYGPPGTGKSSMVAAIANHMKYHIYDLQIQSVRDDGELREILTSTKNRSILLIEDIDCGADASRRRQSKKKEEDGGEDDGEPQKRKKKFEVGISLSGLLNFVDGLWSSCGEEKIIIFTTNHKEKLDPALLRPGRMDVHILMDNCTPFVFKKLVALYLKTDEHVLFDPIEKLILEVSSTPAEVTQQLMASKNADIALKGLAEFLENKKLKKGEDSSVEEEGEIEDAETKEAET | ATP + H2O = ADP + H(+) + phosphate Expressed in developing shoots. Accumulates in shoots and roots upon potassium-starvation. Belongs to the AAA ATPase family. BCS1 subfamily. |
Q9SI12 | MFPSSDFSFSPSSLFSAYASLTGFLMLFRSMLHDFVPEKLRSYFSSLLDRFFTPKSKYLTVIIDENFGLNRNQVFDAAEMYLRSKIGPETERLRVGKIPKQKHFTISIERGEEILDTFEESEVKWSYVQSENEKGDKVKRYYELTFEKKLRDKVLNSYLTHVVAESEEIKRNLRVVKLYSRDVYASDDDDGMAGGNWGCINLEHPSTFDTLAMDPNAKKKIIDDLERFLKRKEFYKRVGKAWKRGYLLYGPPGTGKSSLIAAMANYLKFDVFDLELSSIYDNGELKRVLLSTTNRSILVIEDIDCNAEVRDREAENQEDEQIKGKVTLSGILNFIDGLWSSFGDERIIVFTTNHKERLDPALLRPGRMDVHINMSYCTGLGFRTLVSNYLGLDGLNHPLCEEIEALVDSTEVTPAELAEELMQDDDTDVVLRGVISFVEKRKVERSKTKKEVSICKATDDDEKQNGSLGCVKKKKKGGKQKGKGKGKGKAKTYLI | ATP + H2O = ADP + H(+) + phosphate Belongs to the AAA ATPase family. BCS1 subfamily. The predicted gene At2g18190 has been split into 2 genes: At2g18190 and At2g18193. |
Q9ZPX7 | MGILWDSFLLLLVSTFALFLVRILLFKTGLIYMVKLWRRKIIDWFHVYQFYKVPEFNDNVQENHLYQKVYMYLNSLSSIENSDFTNLFTGKKSNEIILRLDRNQVVGDEFLGARVCWINGEDEDGARNFVLKIRKADKRRILGSYLQHIHTVSDELEQRNTELKLFINVGIDDHLNKKKKKNGRWRSIPFDHPCTFDNIAMETDLKNKVKSDLESFLKGKQYYNRLGRVWKRSYLLYGPSGTGKSSFVAAMANFLDYDVYDIDLSKVVDDSDLKMLLLQTRGKSVIVIEDLDRHLSTKSTAVNLSGILNFTDSILSSCTADERIMVFTMTGKEQIDPAMLRPGRVDVHIHFPLCDFTAFKTLANNYLGVKEHKLFSQVEGIFQNGASLSPAEIGELMIANRNSPTRALKHVINALQTDGDRRGTGRRLLLENGSRKSTSEDVSDDMSGSLCGGGGGSSPAVKEFRKLYGLLRIKSSRKSGSFDVAREMRDG | ATP + H2O = ADP + H(+) + phosphate Belongs to the AAA ATPase family. BCS1 subfamily. Truncated N-terminus. |
Q9LH84 | MLETGAIWGITGTTVTSFMFFWAIYKQYVPAHFRAYVERYFHKMIGWISYYVDIKFTEYTDEGLKRSQAYDSIRNYLASKSTALAKRLKANETKNSKSLVFSMDDHEEIEDEFEGVKVKWYSNVKVIQPQSNYGQRSSEERRHFTLSFHRRHRGMIIETYLDHVLREGKAIGLMNRERKLYTNNSSQEWYPWRSGKWSNVPFHHPATFETLAMDPEKKEGIKKDLIKFSKGKDYYKKVGKPWKRGYLLFGPPGTGKSTMIAAIANFLDYDVYDLELTTVKDNSELKKLLLDTTSKSIIVIEDIDCSLDLTGQRKKKKEEDEEEDGEEKKEGEKKPKVDDKQSKVTLSGLLNSIDGLWSACSGEKIIVFTTNFVDKLDPALIRRGRMDNHIEMSYCKFEAFKVLAKNYLEIETHDLYGEIERKLEETDMSPADVAETLMPKSDEEDADICIKRLVKTLEEEKEKARKLAEEEEKKKAEKEAKKMKKAEEAEEKKKKTEEDEKKEKVKAKEENGNVSQQNGNSIDLNKKSDS | ATP + H2O = ADP + H(+) + phosphate Belongs to the AAA ATPase family. BCS1 subfamily. |
F4J0B1 | MLEVGTIWGFTSTTMASIMFLWPMYKQFVPYQLREYLENTIQKYLDKLFRRDSNFVYIRFPEYTGEGLSKSRAYDEIGNYLSSISTARAKRLKAKESENSKSLVLCLDDDEAVVVVFQGVNVVWSSTVVDKEDKHNSKEGRYLTLTFENHHRDIITNTYIDHVLREGKEIALKNRERKLYTNNDSSSYSSWWEGLWSNVPFNHHASFETLGMDLDKKEEIKKDLIKFTKGKDYYRKVAKPWKRGYLLFGPPGTGKSTMISAIANFLEYDVYDLELTTVKDNAELKKLMLDTKGKSIVVIEDIDCSLELTEHRKKKKEEDEDKEEKKEAENLKRVSGNNESNVTLSGLLNAIDGLWSACSDEKIIIFTTNFVDNLDPALIRRGRMDYHIEMSYCRFEAFKVLAKNYLENESHDLYGEIGRLLEEVDVSPADVAENLMPKSDEDDADICFRRLVKSLEEEKKKKIEKEARKNKKKAEDNVKQEKQNKVKGMVTK | ATP + H2O = ADP + H(+) + phosphate Belongs to the AAA ATPase family. BCS1 subfamily. Truncated N-terminus. |
Q2V3R7 | MFEAGGLFGFTGTTMASLMFFWSVYRQFVPYQIRDYLEKCFYKMFGLVSNSVHIKFTEYTEDKGLKKSQAYDLIRNYLSSKSTARAQRLKANESKNSKSLVLSLDNHEAVEDVFQGVKVVWSLSVWKSNDQADSSEKRYLTLSFHNRYREMITTTYLDHVLREGKEIGLKNRERKLYTNNSSQDYSAWREGRWSNVPFDHPATFETLAMDLEKKEGMKKDLIKFTKGKDYYRKVGKPWKRGYLLFGPPGTGKSTMISAMANFLEYDVYDLELTTVKDNSELKKLMLDTKGKSIVVIEDIDCSLDLTGQRKKKKEEDEDEEEEEKKKEAEKLLKRERGERESKVTLSGLLNAIDGLWSACSGEKIIVFTTNYLDKLDPALIRRGRMDNHIEMSYCRFEAFKVLAKNYLEIESHDLFGEIKRLVEETDMSPADVAENLMPKSDEDDADICLTRLVKSLEEEKEKAKKLAEEEKMKKAARDARRIKKKAEEEHKKKNKVEENGDVSHDNGNHI | ATP + H2O = ADP + H(+) + phosphate Belongs to the AAA ATPase family. BCS1 subfamily. |
Q9LJJ8 | MFAENLTRIGSNVAGLFFVWSTLKRYFPRQIQQLLFNAIQRIPIFKRLSDKILEFFSPYAYIRFREIEGYRYNYAFAAVKTYLGAKVNSEVKNLKGNQVKENMSLDLKRDDVKIEEEYEGVKMWWEIFRCVKGKKICRLTFHRSNWDVVTGSYLRYVVEEGKSIKARKKKVMVLMNNPSLNWKTSMKGLWTCTEFEHPATFDTLAMDIDKKDEIFRDLVAFRDGKEYYDRIGKAWKRGYLLYGPPGTGKSTMIAAMANLMKYNIYDLELTSIGNNWELKKLLIATTNKSIIVIEDIDCSLDLTGEREVKDLKGDKEGKKSNAVTLSGLLNFIDGIWSACGQERILVFTTNHVGKLDQALIRRGRMDMHIELSYCTFGAFKILAKNYLNIDSHHLFGEIESLLKETKITPADVAEHMMAKEVDGSLKGLIRALERIKWSQNVKVEEQLQQGD | ATP + H2O = ADP + H(+) + phosphate Belongs to the AAA ATPase family. BCS1 subfamily. Extended N-terminus. |
Q9LJJ7 | MAMMGQLWTNTGSALATLMFVYTIFKQFFPLFGPQLEPFLYRLFGRFYPYIQITFHEYSGEHFKRSEAYLGIQSYLSKDSSARAKKLKANTTKGSKSIVLSMDDKEEITDDFEGIRVWWQSKKEGATRQSFSFYPEANEKRYYMLRFHRRDREVIIERYLEHVMREGKTIEQKNRERKLYSNTPGQSHGNNSKWSHVTFEHPATFDTLAMEENKKEEIKSDLIKFSKSKDYYKKIGKAWKRGYLLFGPPGTGKSTMIAAMANFLEYDVYDLELTTVKDNTHLRRLLIETSAKSIIVIEDIDCSLNLTGQRKKKEEEEEDGDDKNTIEKKMMMKNEGENKESKVTLSGLLNFIDGLWSACGGERIIVFTTNFVDKLDPALIRKGRMDKHIEMSYCCFEAFKVLAKNYLDVEESEMFEEIKRLLEVEEIKMTPADVGENLLPKSEKEGGETCLKRLIEALKEEKEEAKKKVEEEEEEKQRKKEKVKEIEAEKEKKKKIEEEN | ATP + H2O = ADP + H(+) + phosphate By singlet oxygen (1)O(2). Belongs to the AAA ATPase family. BCS1 subfamily. |
Q9LJJ6 | MMMGNTFGSSLASLFFLWATIQQIFPNHLRIAIKEFLISTIQQLSFVQRFSDRFINFFSPYVEISFSQYEDYQFNHAFAAIETYLGAKATDKAKHLRASQVKESKGLVLKRDETKVRDEYEGGTVWWEMETDSTGYRTFKLTFHRRSRDIVTDSYIKYVFEEGKSIQAKSKQMKLFTNNPSSHWGTSKKSFWRYIDFEHPASFHTLAMDTKKKEEILNDLAAFSNGKEYYKKIGKAWKRGYLLHGPPGTGKSTMIAAMANHLNYSIYDLELTAIRNNSELRKLLTATSSKSIIVIEDIDCSLDLTGKRKKEKNLMTSREDGEQGTEEDKSFVTLSGLLNFIDGIWSACGQERIIIFTTNHFEKLDPALIRRGRMDMHIELSYCSFEAFKILAKNYLDLDTHPLFKKIESLLKETKIAPADVAENLMKKNTEIDADGSLKDLIQALEGKKKIHGAQVDEPKDKYTKKFYKAFCMSSKA | ATP + H2O = ADP + H(+) + phosphate Induced in roots by salt stress. Belongs to the AAA ATPase family. BCS1 subfamily. Truncated N-terminus. |
Q9LJJ5 | MMGNMFGSSLASLFFLWATIQQIFPNHLKIAIKEFFLSTIQQISFAKRFSDKFINFFSPYVQINFSEYEDYRVNHAFDPIETYLGAKATDKAKHLRASQVRESKGLVLKRDETKVRDEYEGIRVWWEMETDSAGYKTLKLTFHRRSRDIVTNSYIKYVVEEGKSIDAKNKKMKLFTNNPSSHWGSSKTSFWRYIDFEHPATFETLAMDPKKKEQILNDLAAFNNGKDYYKKIGKAWKRGYLLYGPPGTGKSTMIAAMANLLNYSIYDLELTAIQNNSELRKILTATSNKSIIVIEDIDCSLDLTGKRKKKESNLMIWRKDGDQDNEENKSFVTLSGLLNFIDGIWSACGQERIIVFTTNHLAKLDPALIRRGRMDMHIELSYCTFEAFKTLAKNYLDLDSHPLFSKIESLMKETNIAPADVAENLMKKNRETDADGSLNDLIESLERKKKVQIAQVDEHKEYSNKIVEAFRKLF | ATP + H2O = ADP + H(+) + phosphate Induced in roots by salt stress. Belongs to the AAA ATPase family. BCS1 subfamily. |
Q9SVK5 | MSSSSESHLATAKTALTAVASVAAAAILARSVVQDYMPNEVHEYISHGFRRFFSYFSYQMTAVIEEFGGFEHNQVFEAAEAYLSTKISNSTRRIKVNKLEKQSNYSVTVERDEEVVDIFDGVKLSWILVCRHVDKKDFRNPRDLNSTLKSEVRSYELSFRKKFKNMVLESYLPFVVEQAASIKQKFKTLKIFTVDSYSVEWTSVTLDHPSTFRTLALDPEVKKNLVEDLDRFVQRKGFYGRVGKAWKRGYLLYGPPGTGKSSLIAAIANHLNFDIYDLDLTSLNNNAELRRLLMSTANRSILVVEDIDCSIELKDRSTDQENNDPLHKTVTLSGLLNFVDGLWSSCGNERIIVFTTNYREKLDPALLRPGRMDMHIHMSYCTPAAFKVLASNYLEIQDHILFEQIEEFIREIEVTPAEVAEQLMRSDSVDKVLQGLVEFLKAKKQIDNSKA | ATP + H2O = ADP + H(+) + phosphate Induced in roots by salt stress. Belongs to the AAA ATPase family. BCS1 subfamily. |
Q56WV1 | MKEYWTSLASLLGVLAFCQSLMNSVFPPELRFAISKLFNKFFKLFSTFCYFDITEIDGVNTNELYNAVQLYLSSSVSIAGNRLSLTRAVNSSSVTFGLSNNDSIVDTFNSVTVVWEHIVTQRQTQTFAWRPMPEEKRGFTLRIKKKDKNLILDSYLDYIMEKANEIRRLNQDRLLYTNSRGGSLDSRGLPWESVPFKHPSTFDTLAMDPVKKQQIMEDLKDFAECQSFYERTGRAWKRGYLLYGPPGTGKSSMIAAMANYLRYDIYDLELTEVKSNSELRKLLMKTSSKSIIVIEDIDCSINLTNRNKKQSTGSYNEPEMLTGSGLGDDLGDGNTITLSGLLNFTDGLWSCCGSERIFVFTTNHIEKLDPALLRSGRMDMHIHMSYCTFSSVKILLRNYLGFEEGDLNDVVLKELAEVVDRAEITPADVSEALIKNRRDKERAVRELLVDLRSRVERNEKNGKSRVQNVSLEEQENRAFDSLYAEENGGEEEEIEDNICKSSDDCS | ATP + H2O = ADP + H(+) + phosphate Belongs to the AAA ATPase family. BCS1 subfamily. Truncated N-terminus. |
Q9SUL9 | MSDYWTTMASLLGMLAFCQTIVQLVFPPELRLAFLHFLTRIRHVFSSHIYFDITEIDGVNTNELYNAVQLYLSSSVTVNDAVSSSNNNTRLSLTRVPNSSSVTFGLSNNDRITDVFNGVTILWEHVVVQRQVQSFSWRPMPEEKRGFTLQINKRDKALVLDSYLDYIVGKSEEIRRRNEERLLYTNSRGVSLDARSHPWDSVRFKHPSTFDTLAMDPEKKKRIMEDLREFANGQGFYQKTGRAWKRGYLLYGPPGTGKSSLIAAMANYLGYDIYDLELTEVQNNSELRKLLMKTSSKSIIVIEDIDCSISLTKRGKNKKKNGSYEYDPGLTNGSGLEEPGSSVTLSGLLNFTDGLWSCCGSEKIFVFTTNHIEKLDSALMRSGRMDMHVHMGFCKFPALKILLKNYLRLEEEDMDSVVLKEMEECVEEAEITPADVSEVLIRNRSDAEKAVREIVSVLKERVVKRRKSVGLKKKKQEGQEEEEEAEEEQEKRALDSPNRRNREVCGFREEEEEEDEKEK | ATP + H2O = ADP + H(+) + phosphate Belongs to the AAA ATPase family. BCS1 subfamily. Truncated N-terminus. Truncated N-terminus. |
Q9FN78 | MFSLRNLPSLAPFVSAYASLTGYVMMIKPFLEMTIPPPLQNYMISYLNSFLHSTPSTLTLIIDDHIKNGMYNELYGAAQVYISTKVNHNAERLRISRDRSEKNVNIHFSVGEVVSDIYQGIEVKWRFCVDSNKSNMVHYFGEHFKLNPDRECVELSFEKKHTELVLNSYIPYVESKAKVINNERKILKMYSYCCMYLKWQSVNLEHPSTFDTMAMNEELKRSVMGDLDRFIRRKDFYKRVGKPWKRGYLLYGPPGTGKTSLVAAIANYLKFDIYDLQLASVREDADLRRLLLGTTNSSILLVEDIDCAVDLHTRLQPKTQDDTKGSSMLTLSGLLTCIDGLWSSCGDERIVIFTTTHKERLDPALLRPGRMDMHIHMGHCCFDVFKTLASNYLGLSHDDPHHLYPEIERLIKGEVLTPAQVAEELMKNEDPDVALEGLVKVLKRKRLELEKYDGETGRGGLRKPELQFFL | ATP + H2O = ADP + H(+) + phosphate Belongs to the AAA ATPase family. BCS1 subfamily. |
Q9FN77 | MVFSRDIPSPASMFSTYASMMGYVMIIKPMINTIIPRPVQNFVFSYLKSFAGSRSSTLTLTIDQMSSMYIPDELYAAAQAYLSTKISPNSVRLIMARDPAEKKVKLYLSDGEVVSDVYNGIKLKWRFLARNKNNTMVEEYGQSYQGNIQRESLELSFDKKHRDLVVNSYIPYVESKAKEVNNKRRILKMHCYSHMAQTWQSVNFKHPSTFDTMAMNDDLKRSMIEDLDRFVGRKDFYKRVGKAWKRGYLLYGPPGTGKSSLVAAMANYLKFDIYDLQLASVQGDAHLRSLLLATNNSSILLIEDIDCSVDLPTRLQPPTETSQPLGAVQVSKPLTLSGLLNCIDGLWSSCGNERIIIFTTNNKEKLDPALLRPGRMDMHIYMGHCSFQGFKTLASNYLGLSDENDDTHPLCPDIKHLIDGHVLTPAQVAEELMKDEDADAALEGLVKVLKRKRLEPKKCDDESKMKKLKEGEEAIADAELAVLTPAQVEDKEELVASEYANVMPEWLPRSRLVMVLPGFHRARGIRRGLGDEM | ATP + H2O = ADP + H(+) + phosphate Belongs to the AAA ATPase family. BCS1 subfamily. |
Q9FN76 | MVFSKDLPSPATMFSTYASLAGYIMMIKPMIHTIIPRPIQNFVFSYIKSFVGSPQAYLSSKISPDASKLRMTRDPNNKNVNLHLSQGEVVSDVYKGIELKWRYLEGRNKKTTVVGEETEEAIVNWQCFELSFDKKHKDLVVKSYIAYVERKAKVIKEERRIIKMHSYSSYTLRWQSVKFEHPSTFHTMAMTPKLKSSVMEDLDRFIKRKDYYKRVGKAWKRSYFLYGPPGTGKSSLVAAMANYLKFDIYDLQLANVQGDAQLRSLLLATNNSSILLVEDIDCSVDLPTRLQPATTTLGAPKGSTPLTLSGLLNCIDGLWSSCGDERIVIFTTNNKEVLDPALLRPGCMDMHIYLGHCSFEGFKILASNYLGMPHDSDDPHRLYPDIKRLIDG | ATP + H2O = ADP + H(+) + phosphate Belongs to the AAA ATPase family. BCS1 subfamily. |
Q3E9G3 | MFFSKDLPSPTSVFTAYASMAGYMMMIRSMAHELIPAPLQDFIYRTLRSLFFRSSSSTLTLTIDDDNMGMNNEIYRAAQTYLSTKISPDAVRLRISKGHKDKHVNLYLSDGEIVNDVYEDVQLVWRFVTDGGDKKGGGGGVGGRGGGGGRRGGMDDDGKSEYFELSFDKKHKDLILNSYVPYIESKAKEIRDERRILMLHSLNSLRWESVILEHPSTFETMAMEDDLKRDVIEDLDRFIRRKEFYKRVGKAWKRGYLLYGPPGTGKSSLVAAMANYLKFDVYDLQLASVMRDSDLRRLLLATRNRSILVIEDIDCAVDLPNRIEQPVEGKNRGESQGPLTLSGLLNFIDGLWSSCGDERIIIFTTNHKDRLDPALLRPGRMDMHIYMGHCSFQGFKTLASNYLGLSDAAMPHRLFPEIERLIDGEVMTPAQVAEELMKSEDADVALEGLVNVLEKMRLKSKESNPVMMKQKESRLEMEEMRLKSDTEGSPRKNSKRFKKLVLFWT | ATP + H2O = ADP + H(+) + phosphate Belongs to the AAA ATPase family. BCS1 subfamily. |
Q9FLD6 | MMMMGDSFGSIGSSMASLFFLWATIQQIFPDHLKITIKEFLLSSFQQLCFAQRVSDHFTNLFSPYVEIHFPESDEYSFNQAFSAIDTYLDSKATDKTKHLRGSQVKESKGLVLKRNEAKVRDEYKGANVWWERVVDNDGNRYYKLTFHNRARTLITNSYIKYVVEEGKSIIVKNKQTRLFTNNLSTQWVFGQNMWRSIEFEHPASFQTLAMDPKKKEEIVNDLIAFSNGKEYYKKIGKAWKRGYLLYGPPGTGKSTMISAMANLLNYNIYDLELTAVKNNSELKKLLTATSSKSIIVIEDIDCSADFTSNRIKKESNSRERYGKEDKDENSVTLSGLLNFIDGIWSACGQERIVVFTTNHLEKLDPALIRRGRMDMHIELSYCTYEAFKILAKNYLDLDGDDAHPLFSEIKALLEETKISPADVAENLMARNQQIDVDKSLNLLISALEEENQYQRSQQEKKKSKFKIFG | ATP + H2O = ADP + H(+) + phosphate Belongs to the AAA ATPase family. BCS1 subfamily. Truncated N-terminus. |
Q9FKM3 | MKEYWTSLASLLGVLAFCQSLMQSIFPPELRFAFLKFFNRIFHVFSSYCYFDITEIDGVNTNELYNAVQLYLSSSVSIAGNRLSLTRAVNSSSITFGLSNNDSIVDTFNGVTVLWEHVVTQRQTQTFAWRPLPEEKRGFTLRIKKKDKTLILNSYLDYIMERANEIRRKNQDRLLYTNSRGGSLDSRGHPWESVPFKHPSTFETLAMDPRKKQQIMDDLKDFAEGQVFYQKTGRAWKRGYLLYGPPGTGKSSMIAAMANYLGYDIYDLELTEVHSNSELRKLLMKTSSKSIIVIEDIDCSINLTNRKKNSSNVSSQRSYYDAETRNGSGSGSGGSGEEGGNGNTITLSGLLNFTDGLWSCCGSERIFVFTTNHIEKLDPALLRSGRMDMHIYMSFCNFPSLKILLKNYLGYGVEDINGDVLKEMEMVVEKAEMTPADVSEALIKNRRDKEKAIRELLEDLKSRGERNVKDGKLRGGSGNLTELEVVEEQEKRAIDSQNEDEDHDEEEIELEDNICKTRED | ATP + H2O = ADP + H(+) + phosphate Belongs to the AAA ATPase family. BCS1 subfamily. |
F4J869 | MIENYWTSFCGNHHTSSNCTVRFLQICFGITLSFLTLCICLFHKEPPKRIHQFFCLRLVSALFNGIIGSLDLVLGIWVLRENHSKPLILWLVILIQGFTWLFINLIICVRGTRIRKSSLRLLSIFSFFYGLVSSCLSVNNAVFGDELAVRTILDVLLLPGSVLLLLSAYKGYRFDESGESSLYEPLNAGDSNGFSEKADFDNRVSQFAKAGLFSTLSFWWLNSLIKRGNVKDLEEEDIPELRKEERAETCYSLFEENLIEQKRRLGSSCQPSILKVTVLCVWRELLTSGFFAFMKIVAVSAGPLLLNAFILVAEGNASFRYEGLVLAVLLFFSKMIESLSQRQWYFRCRIVGLRVRSLLTAAINKKQLRLNNSSRLIHSGSEIMNYATVDAYRIGEFPYWFHQLWTTSFQLLIALGILFHSVGVATFSALAVIILTVLCNAPIAKLQNKFQSELMTSQDERLKACNESLVNMKVLKLYAWESHFKKVIEKLRNIELKSLKAVQMRKAYNAVLFWSSPVFVSAATFATCYFLDIPLRASNVFTFVATLRLVQDPVRMIPDVIGVTIQAKVAFSRIATFLEAPELQGGERRRKQRSEGNQNAIIIKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTIAYVSQTAWIQTGTIRDNILFGGVMDEHRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRDFQDLVNAHRETAGSERVVAVENPTKPVKEINRVISSQSKVLKPSRLIKQEEREKGDTGLRPYIQYMNQNKGYIFFFIASLAQVTFAVGQILQNSWMAANVDNPQVSTLKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQVLFVSVPMVYLAFRLQKYYFQTAKELMRINGTTRSYVANHLAESVAGAITIRAFDEEERFFKKSLTLIDTNASPFFHSFAANEWLIQRLETVSAIVLASTAFCMILLPTGTFSSGFIGMALSYGLSLNMGLVYSVQNQCYLANWIISVERLNQYTHLTPEAPEVIEETRPPVNWPVTGRVEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNLDPLCQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMKDENSLFGKLVKEYWSHYNSADSR | Pump for glutathione S-conjugates. ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2. Ubiquitous. Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily. |
Q9MAH4 | MELPVKAPIPGGREISYRLETKNLSYRIGGNTPKFSNLCGLLSEKEEKVILKDVSCDARSAEITAIAGPSGAGKTTLLEILAGKVSHGKVSGQVLVNGRPMDGPEYRRVSGFVPQEDALFPFLTVQETLTYSALLRLKTKRKDAAAKVKRLIQELGLEHVADSRIGQGSRSGISGGERRRVSIGVELVHDPNVILIDEPTSGLDSASALQVVTLLKDMTIKQGKTIVLTIHQPGFRILEQIDRIVLLSNGMVVQNGSVYSLHQKIKFSGHQIPRRVNVLEYAIDIAGSLEPIRTQSCREISCYGHSKTWKSCYISAGGELHQSDSHSNSVLEEVQILGQRSCKNIFRTKQLFTTRALQASIAGLILGSIYLNVGNQKKEAKVLRTGFFAFILTFLLSSTTEGLPIFLQDRRILMRETSRRAYRVLSYVLADTLIFIPFLLIISMLFATPVYWLVGLRRELDGFLYFSLVIWIVLLMSNSFVACFSALVPNFIMGTSVISGLMGSFFLFSGYFIAKDRIPVYWEFMHYLSLFKYPFECLMINEYRGDVFLKQQDLKESQKWSNLGIMASFIVGYRVLGFFILWYRCYRTRS | Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. |
Q9SZC3 | MNGHCLFAASPPRLFPLRSISSSVSPSGSYRIKFSDNVAVECRNLCFSVSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHQVVMPTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGDAATISDFIKAKQSSYIDQIGS | Belongs to the ABC transporter superfamily. ABCI family. |
F4K3L3 | MILQEGLPLLYQQFTALFGKNLLLSWRNKRATCLQIFSSFFFILLIFCIEEAMKASDASSSAYKNITDPTLLVSPPILPCEDKFFVKLPCYDFVWSGNNSRRVTDIVSAIMANNPGRPIPTNKVQSFKEPDEVDTWLLSHPLQVPGALHFVERNASVISYGVQTNSSSESKRGQTEDPTFKFLVPLQVAAEREIARSLLGDPNFGWGLGFKEFARPAIITETTSALSVMGPVFFLAFSMFGFVLQLGALVTEKELKLRQAMTMMGVYDSAYWLSWLTWEGILTLVSSLFLVLFGMIFRFDFFLKNSFVLVFLLFLLFQFNMIGLAFALSSIISKSSSATTVGFLVFLIGFITQFVSATGFPYSSSYAVSRRVMWSLFPPNTFSAGLKLLLDATSTPKSSGISWSNRAVCEGGQATCVISINIIYQWLLGTFLFWFVLAIYFDNIIPNASGVRKPIFYFLAPGYWTGKGGNKVEEGSIFSCVGSVPLVEHNTPNDKDVLEEETEVKQQAMDGIADPNIAVQIHGLAKTYPGTTKLGCCKCTKTSPFHAVKGLWMNIAKDQLFCLLGPNGAGKTTTISCLTGINPVTGGDALIYGDSIRSSVGISNIRKMIGVCPQFDILWDALSSEQHLHLFASIKGLPPASIKSTAEKLLADVKLTGAAKVRAGSYSGGMKRRLSVAVALIGDPKLVFLDEPTTGMDPITRRHVWDIIQESKKGRAIILTTHSMEEADILSDRIGIMAKGRLRCIGTSIRLKSRFGTGFVATVSFIENKNDNNIGVGASHEPLKKFFKEHLKVEPTEENKAFMTFVIPHDKENLLTGFFEELQNRESEFGISDIQLGLATLEEVFLNIARQAELESATAEGNMVTLELASGISLEIPVGARFVGIPDTENAENPSGVMVEVYWQQDGSGSMCISGHSSEMRVPQNVPVTRPPSPNALGHKSLRQGVRGIVIDL | Belongs to the ABC transporter superfamily. ABCA family. CPR flippase (TC 3.A.1.211) subfamily. |
Q9FWX7 | MNGDGAREGDSVSHEPSTSKSPKEGEETKKEEKSEEKANTVPFYKLFAFADSSDVLLMICGSIGAIGNGMSLPFMTLLFGDLIDSFGKNQNNKDIVDVVSKVCLKFVYLGLGTLGAAFLQVACWMITGERQAARIRSTYLKTILRQDIGFFDVETNTGEVVGRMSGDTVLIQDAMGEKVGKFIQLVSTFVGGFVLAFIKGWLLTLVMLTSIPLLAMAGAAMALIVTRASSRGQAAYAKAATVVEQTIGSIRTVASFTGEKQAINSYKKFITSAYKSSIQQGFSTGLGLGVMFFVFFSSYALAIWFGGKMILEKGYTGGAVINVIIIVVAGSMSLGQTSPCVTAFAAGQAAAYKMFETIKRKPLIDAYDVNGKVLEDIRGDIELKDVHFSYPARPDEEIFDGFSLFIPSGATAALVGESGSGKSTVISLIERFYDPKSGAVLIDGVNLKEFQLKWIRSKIGLVSQEPVLFSSSIMENIAYGKENATVEEIKAATELANAAKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAIARAILKDPRILLLDEATSALDAESERVVQEALDRVMVNRTTVIVAHRLSTVRNADMIAVIHRGKMVEKGSHSELLKDSEGAYSQLIRLQEINKDVKTSELSSGSSFRNSNLKKSMEGTSSVGNSSRHHSLNVLGLTTGLDLGSHSQRAGQDETGTASQEPLPKVSLTRIAALNKPEIPVLLLGTVAAAINGAIFPLFGILISRVIEAFFKPAHELKRDSRFWAIIFVALGVTSLIVSPTQMYLFAVAGGKLIRRIRSMCFEKAVHMEVAWFDEPQNSSGTMGARLSADATLIRALVGDALSLAVQNVASAASGLIIAFTASWELALIILVMLPLIGINGFVQVKFMKGFSADAKSKYEEASQVANDAVGSIRTVASFCAEEKVMQMYKKQCEGPIKDGIKQGFISGLGFGFSFFILFCVYATSFYAGARLVEDGKTTFNNVFQVFFALTMAAIGISQSSTFAPDSSKAKVAAASIFAIIDRKSKIDSSDETGTVLENVKGDIELRHLSFTYPARPDIQIFRDLCLTIRAGKTVALVGESGSGKSTVISLLQRFYDPDSGHITLDGVELKKLQLKWLRQQMGLVGQEPVLFNDTIRANIAYGKGSEEAATESEIIAAAELANAHKFISSIQQGYDTVVGERGIQLSGGQKQRVAIARAIVKEPKILLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIAEKGTHETLIKIEGGVYASLVQLHMTASN | Belongs to the ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily. |
Q9S9R0 | MGFEALNWYCKPIAEGFWEKTPDGAFGAYTPCAIDSLVMIVSNSVLLGLCFYRIWITLYNAKAQIYVLRKMYYHCVLWILACCCVVEPVLRLVMGISLFDMGDETDLPPFEVASLMVEAFAWFAMLVLIGLETKQYVKEFRWYVRFGVVYVLVADAVLLDLVLPLKNSINRTALYLCISSRCCQALFGILLLVYIPELDLYPDYHILNNESLDNVEYDALPGGVNICPERYASIFSGIYFSWMTPLMQLGYRKPITERDVWQLDQWDQTETLIKRFQRCWTEESRRPKPWLLRALNNSLGRRFWLGGIFKVGHDLSQFVGPVILSHILQSMIEGDPAWVGYVYAFLIFFGVTFGVLCQSQYFQHVGRVGFRLRSTLVAAIFHKSLRLTNKARKNFASGKVTNMITTDANALQLIAEQLHGLWSAPFRIIVSMVLLYQQLGVASIFGSLILFLLIPFQTLIVRKMRKLTKEGLQWTDKRVGIIYEILASMDIVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSTPVVVTLVSFGVYVLLGGDLTPARAFTSLSLFAVLRSPLSTLPNLISQAVNANVSLQRIEELLLSEERILAQNPPLQPGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVDIRGSVAYVPQVSWIFNATLRENILFGSDFESERYWRAIDVTALQHDLDLFPGRDRTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPFSALDAHVAHQVFDSCVKHELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGNFAELSKSGTLFKKLMENAGKMDATQEVNTNDENISKLGPTVTIDVSERSLGSIQQGKWGRSMLVKQEERETGIISWDVVMRYNKAVGGLWVVMILLVCYLTTEVLRVLSSTWLSIWTDQSTPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFETNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGIVSTISLWAIMPLLILFYATYIYYQSTSREVRRLDSVTRSPIYALFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLASTSSNRWLTIRSESLGGVMIWLTATFAVLRYGNAENQAVFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIQFEDVHLRYRPGLPPVLHGLSFFVYPSEKVGVVGRTGAGKSSMLNALYRIVELEKGRILIDDYDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILFLDEATASVDVRTDSLIQRTIREEFKSCTMLIIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFKMVHSTGPENGQYLSNLVFERRGNGMSQGG | Pump for glutathione S-conjugates. ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2. Ubiquitous. Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily. |
Q9LMU4 | MEIEASRQQTTVPVSVGGGNFPVGGLSPLSEAIWREKAPTEFVGDVSARLTWQDLTVMVTMGDGETQNVLEGLTGYAEPGSLTALMGPSGSGKSTMLDALASRLAANAFLSGTVLLNGRKTKLSFGTAAYVTQDDNLIGTLTVRETIWYSARVRLPDKMLRSEKRALVERTIIEMGLQDCADTVIGNWHLRGISGGEKRRVSIALEILMRPRLLFLDEPTSGLDSASAFFVTQTLRALSRDGRTVIASIHQPSSEVFELFDRLYLLSGGKTVYFGQASDAYEFFAQAGFPCPALRNPSDHFLRCINSDFDKVRATLKGSMKLRFEASDDPLEKITTAEAIRLLVDYYHTSDYYYTAKAKVEEISQFKGTILDSGGSQASFLLQTYTLTKRSFINMSRDFGYYWLRLLIYILVTVCIGTIYLNVGTSYSAILARGSCASFVFGFVTFMSIGGFPSFVEDMKVFQRERLNGHYGVAAFVIANTLSATPFLIMITFISGTICYFMVGLHPGFTHYLFFVLCLYASVTVVESLMMAIASIVPNFLMGIIIGAGIQGIFMLVSGFFRLPNDIPKPFWRYPMSYISFHFWALQGQYQNDLRGLTFDSQGSAFKIPGEYVLENVFQIDLHRSKWINLSVILSMIIIYRIIFFIMIKTNEDVTPWVRGYIARRRMKQKNGTQNTTVAPDGLTQSPSLRNYIATRTDGARRW | Required for the cuticle, root suberin and pollen coat development by controlling cutin and maybe wax transport to the extracellular matrix (PubMed:24112720, PubMed:20035035). Involved in developmental plasticity and stress responses. Together with ABCG9 and ABCG14, required for vascular development by regulating lipid/sterol homeostasis (PubMed:24112720). May be a transporter of lignin precursors during tracheary element differentiation (PubMed:28921082). Homodimer (PubMed:24112720, PubMed:20870961). Forms heterodimers with ABCG9, ABCG12 and ABCG14 in epidermal cells (PubMed:24112720, PubMed:20870961). Localized in a polar manner in the epidermis side facing the extracellular matrix (cuticle) and in the endosperm tissue of the developing seed (PubMed:20035035). Trafficking to the plasma membrane is independent of ABCG12 (PubMed:20870961). Expressed in seedlings, roots, stems, leaves, flowers, and siliques, mostly in epidermis, trichomes, vasculatures and developing tissues (PubMed:14730060, PubMed:17727615, PubMed:17951461, PubMed:17989085, PubMed:24112720, PubMed:20035035). Follows an uniparental maternal expression in the seed, thus being the product of a maternally expressed imprinted gene (PubMed:21838868). Accumulates in the phloem (PubMed:24112720). Transcripts seem to be transported from shoots to roots (PubMed:27247031). First observed in seed coat and the endosperm (PubMed:20035035). Displays a polar localization in the embryo protoderm (PubMed:20035035). During embryo development, expressed in the radical tip. In seedlings, localized in the cotyledons, root tip, and young leaves. As secondary root tips emerge, expressed in the pericycle during the initial cell divisions. In leaves, mostly detected in the expanding basal portion, trichomes and stomatal cells. Present in rosette leaves vascular system and epidermis (PubMed:24112720). In roots of mature plants, mainly expressed in lateral root primordia and developing lateral roots (PubMed:24112720). Accumulates in buds and open flowers, mainly in the petal epidermis and the vasculature (PubMed:20035035). In the inflorescence, found in all floral organs, predominantly in the anthers, styles, and young siliques, particularly in young seeds (PubMed:20035035). Upon anthesis and later, progressively restricted to the carpel. Also observed in phloem cells of the flower stem, and in the cortical cells and interfascicular fibers (PubMed:24112720). Accumulates during tracheary element differentiation (PubMed:28921082). By light, NaCl, abscisic acid (ABA), wounding, and glucose stresses. Repressed by H(2)O(2) and cytokinin. Bushy phenotype (PubMed:24112720). Abnormal cuticle and pollen grain shapes, reduced levels of wax and cutin monomers, unusual lipidic cytoplasmatic inclusions in epidermal cells, inter-organ postgenital fusions, and altered morphology of trichomes and pavement cells (PubMed:24112720, PubMed:20035035). Altered petal and silique morphology, fusion of seeds, and changes in levels of cutin monomers in flowers and siliques associated with the suppression of the expression of a large number of cuticle-associated genes (PubMed:20035035). Altered root suberin composition, as well as root expression of suberin biosynthetic genes (PubMed:20035035). Highly susceptibility to salt and reduced root branching. Excess in sterol (e.g. campesterol) composition (PubMed:24112720). Vascular patterning defects in cotyledons and the floral stem, with a stronger phenotype in plant missing also ABCG9 and ABCG14 (PubMed:24112720). Both single and double mutants abcg11 abcg12 exhibit ABCG12-containing membrane inclusions protruded into the vacuole and contiguous with the endoplasmic reticulum (PubMed:20870961). Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. |
Q9FMU0 | MAVSTFSSPTPVFGIAEPPASFSSTAIGWKQPLRFRRTKKPRVISCDYSCIEVRDVCYRPPGTQLNILNGVNFSLREKSFGLIFGKSGSGKTTLLQLLAGLNKPTSGSICIQGYGDDGQPKADPDLLPTEKVGIVFQFPERFFVADNVLDEITFGWPRQKGSLQLKEQLTSNLQRAFNWVGLDSIPLDKDPQLLSGGYKRRLALAIQLVQTPDLLILDEPLAGLDWKARADVAKLLKHLKKELTLLVVSHDLRELAALVDQSWRMETGGVLVAERPPL | Belongs to the ABC transporter superfamily. ABCI family. |
F4K3L4 | MVNPSPASFWTQANALLRKNLTYQRKHIWTNVRLILVPLFLCLILLAIQQVLDALMKGVSDMSNCGGNVTLPGGICPIPNPPSLPPMLQIPQHELRSVKTDFFSYKDLPDKLCRETGSCPVTILFTGDKLPLGKALSANIFSTSFVVNSSDLLPTLANNVLGSTEAAGEDNYEDPGIASDLPIYSIQPSCSANSTWPLSLGQIQTAVKCVQGLCLWRNNSVEVNDELFKGSWRGNPAGMPNEIVAAYDLMSTDRKNFNVTIWYNSTYNDEFATGQALKLVRVPRSINLISNAYLKFLKGPGTRILFEFLKEVPKEETKMNQDIASLLGPLFFTWVVLLLFPVILTSLVYEKQERLRIIMKMHGLGDGPYWMISYAYFLTISMLYVISLVGFGSAIGLKYFRRNDYSIQFVFYFIYSNLQISLAFLVSSIFSKVKTVTVIAYILVYGTGLLGSFLFQKMIETQSFPEEWILAMELYPGFSLYRGLYEFSQYASRGNGMKWQDLSDSGMGEVFCIMSVEWFLALIVAYYIDQVFTSGKHPFFFLVNLFKSPSSLPRRPTVQRLDSKRVFIDMDKHDVTQERESVQKLRNEGSTGHAILCDNLKKVYPGRDGNPPKMAVRGLYLSVSSGECFGMLGPNGAGKTSFISMMTGLLKPSSGTALVQGLDICKDMNKVYTSMGVCPQHDLLWETLTGREHLLFYGRLKNIKGSDLTQAVEESLKSVSLYDGGVGDKPAGNYSGGMKRRLSVAISLIGNPKVVYLDEPSTGLDPASRKNLWNVIKRAKQNTAIILTTHSMEEAEFLCDRLGIFVDGGLQCIGNSKELKSRYGGSYVFTMTTSSKHEEEVERLVESVSPNAKKIYHLAGTQKFELPKQEVRIAEVFRAVEKAKANFTVFAWGLADTTLEDVFIKVARTAQAFISLS | Belongs to the ABC transporter superfamily. ABCA family. CPR flippase (TC 3.A.1.211) subfamily. |
Q9FWX8 | MNRDGAGEGDSVSHEHSTSKTDEKAKTVPLYKLFAFADSFDVFLMICGSLGAIGNGVCLPLMTLLFGDLIDSFGKNQNNKDIVDVVSKVCLKFVYLGLGRLGAAFLQVACWMITGERQAAKIRSNYLKTILRQDIGFFDVETNTGEVVGRMSGDTVHIQDAMGEKVGKFIQLVSTFVGGFALAFAKGWLLTLVMLTSIPFLAMAGAAMALLVTRASSRGQAAYAKAATVVEQTIGSIRTVASFTGEKQAINSYKKYITSAYKSSIQQGFSTGLGLGVMIYVFFSSYALAIWFGGKMILEKGYTGGSVINVIIIVVAGSMSLGQTSPCVTAFAAGQAAAYKMFETIKRKPLIDAYDVNGKVLGDIRGDIELKDVHFSYPARPDEEIFDGFSLFIPSGATAALVGESGSGKSTVINLIERFYDPKAGEVLIDGINLKEFQLKWIRSKIGLVCQEPVLFSSSIMENIAYGKENATLQEIKVATELANAAKFINNLPQGLDTKVGEHGTQLSGGQKQRIAIARAILKDPRVLLLDEATSALDTESERVVQEALDRVMVNRTTVVVAHRLSTVRNADMIAVIHSGKMVEKGSHSELLKDSVGAYSQLIRCQEINKGHDAKPSDMASGSSFRNSNLNISREGSVISGGTSSFGNSSRHHSLNVLGLFAGLDLGSGSQRVGQEETGTTSQEPLRKVSLTRIAALNKPEIPVLLLGTVVAAINGAIFPLFGILISRVIEAFFKPADQLKKDSRFWAIIFVALGVTSLIVSPSQMYLFAVAGGKLIRRIQSMCFEKAVHMEVSWFDEPENSSGTMGARLSTDAALIRALVGDALSLAVQNAASAASGLIIAFTASWELALIILVMLPLIGINGFLQVKFMKGFSADAKSKYEEASQVANDAVGSIRTVASFCAEEKVMQMYNKQCEGPIKDGVKQGFISGLGFGFSFFILFCVYATSFYAAARLVEDGKTTFIDVFQVFFALTMAAIGISQSSTFAPDSSKAKVAAASIFAIIDRKSKIDSSDETGTVLENVKGDIELRHLSFTYPARPGIQIFRDLCLTIRAGKTVALVGESGSGKSTVISLLQRFYDPDSGQITLDGVELKKLQLKWLRQQMGLVGQEPVLFNDTIRANIAYGKGSEEAATESEIIAAAELANAHKFISSIQQGYDTVVGEKGIQLSGGQKQRVAIARAIVKEPKILLLDEATSALDAESERLVQDALDRVIVNRTTVVVAHRLSTIKNADVIAIVKNGVIAENGTHETLIKIDGGVYASLVQLHMTASN | Belongs to the ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily. |
Q8N4D2 | MDAQDCQAAASPEPPGPPARSCVAAWWDMVDRNLRYFPHSCSMLGRKIAALYDSFTSKSLKEHVFLPLIDMLIYFNFFKAPFLVDLKKPELKIPHTVNFYLRVEPGVMLGIWHTVPSCRGEDAKGKDCCWYEAALRDGNPIIVYLHGSAEHRAASHRLKLVKVLSDGGFHVLSVDYRGFGDSTGKPTEEGLTTDAICVYEWTKARSGITPVCLWGHSLGTGVATNAAKVLEEKGCPVDAIVLEAPFTNMWVASINYPLLKIYRNIPGFLRTLMDALRKDKIIFPNDENVKFLSSPLLILHGEDDRTVPLEYGKKLYEIARNAYRNKERVKMVIFPPGFQHNLLCKSPTLLITVRDFLSKQWS | May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the serine esterase family. Truncated N-terminus. Wrong choice of CDS. Wrong choice of CDS. |
F4I4U8 | MGFEALNWYCKPVADGFWEKAVDGAFGAYTPCAIDSLVMLVSHFVLLGLCFYRIWIIFHNTKAQIYVLRKKYYNCVLGLLACYCVVEPVLRLVMGISLFDMDEETDFPPFEVASLMVEAFAWFSMLVLIGLETKQYVKEFRWYVRFGVLYVLVADAVLLDLVLPLKNSINRTALYLFISSRCSQALFGILLLIYIPELDPYPGYHIVNNEPLDNVEYDALRGGEHICPERHASIFSRIYFGWITPLMQLGYRKPITEKDVWQLDKWDQTETLIKRFQRCWTEESRRPKPWLLRALNNSLGGRFWLAGIFKIGNDLSQFVGPVILSHLLRSMQEGDPAWVGYVYAFIIFVGVTLGVLCEAQYFQNVWRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQISQQLHGLWSAPFRIIVSMILLYQQLGVASLFGSLILFLLIPLQTLIISKMRKLTKEGLQWTDKRVGITNEILSSMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTVVSFGVFVLLGGDLTPARAFTSLSLFAVLRFPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGTPAISIKNGYFSWDSKTTKPTLSDINLEIPVGTLVAIVGGTGEGKTSLISAMLGELSHAETTSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDATALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVAHQVFDSCMKDELRGKTRVLVTNQLHFLPLMDKIILVSEGMIKEEGTFVELSKSGILFKKLMENAGKMDATQEVNTNDENILKLGPTVTVDVSERNLGSTKQGKRRRSVLIKQEERETGIISWNVLMRYKEAVGGLWVVMILLACYLATEVLRVSSSTWLSIWTDQSTSKNYSPGFYIVVYALLGFGQVAVTFTNSFWLITSSLHAARRLHDAMLSSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLQNGNTNNQAGFASTMGLLLSYTLNITSLLSGVLRQASRAENSLNSVERVGNYIDLPSEATDIIENNRPVCGWPSGGSIKFEDVHLRYRPGLPPVLHGLTFFVSPSEKVGVVGRTGAGKSSMLNALFRIVEVEKGRIMIDDCDVAKFGLTDVRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDAGLWEALHRAHIKDVISRNPFGLDAEVCEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPANAQYLSNLVFERRENGMSVGG | Pump for glutathione S-conjugates. ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2. Ubiquitous. Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily. |
Q9C8K2 | MELESTSNGRRPPPPAEIGRGAYLAWEDLTVVIPNFSGGPTRRLLDGLNGHAEPGRIMAIMGPSGSGKSTLLDSLAGRLARNVIMTGNLLLNGKKARLDYGLVAYVTQEDILMGTLTVRETITYSAHLRLSSDLTKEEVNDIVEGTIIELGLQDCADRVIGNWHSRGVSGGERKRVSVALEILTRPQILFLDEPTSGLDSASAFFVIQALRNIARDGGRTVVSSIHQPSSEVFALFDDLFLLSSGETVYFGESKFAVEFFAEAGFPCPKKRNPSDHFLRCINSDFDTVTATLKGSQRIRETPATSDPLMNLATSEIKARLVENYRRSVYAKSAKSRIRELASIEGHHGMEVRKGSEATWFKQLRTLTKRSFVNMCRDIGYYWSRIVIYIVVSFCVGTIFYDVGHSYTSILARVSCGGFITGFMTFMSIGGFPSFIEEMKVFYKERLSGYYGVSVYIISNYVSSFPFLVAIALITGSITYNMVKFRPGVSHWAFFCLNIFFSVSVIESLMMVVASLVPNFLMGLITGAGIIGIIMMTSGFFRLLPDLPKVFWRYPISFMSYGSWAIQGAYKNDFLGLEFDPMFAGEPKMTGEQVINKIFGVQVTHSKWWDLSAIVLILVCYRILFFIVLKLKERAEPALKAIQAKRTMKSLKKRPSFKKVPSLSSLSSRRHQPLHSLSSQEGLTSPIN | Involved in the secretion of cuticular wax from epidermal cells to the cuticle, especially in the transport of aldehydes, alcohols and acids. (Microbial infection) Required for the polarization of reflected light on both adaxial and abaxial leaves surfaces upon viral infection by Turnip vein clearing virus (TVCV), probably by regulating cuticular wax compounds deposition, thus influencing visual attractiveness of infected plants for insect vectors. Forms heterodimers with ABCG11 in epidermal cells. Trafficking to the plasma membrane is dependent of ABCG11. Exclusively and constitutively expressed in epidermal cells. By NaCl and abscisic acid (ABA). Abnormal cuticle and unusual lipidic cytoplasmatic inclusions in epidermal cells associated with a reduced secretion of aldehydes, alcohols and acids (PubMed:17951461, PubMed:26965486). The double mutant abcg11 abcg12 exhibits ABCG12-containing membrane inclusions protruded into the vacuole and contiguous with the endoplasmic reticulum (PubMed:20870961). Reduced polarizing on the adaxial and abaxial leaves surfaces, and impaired impact of viral infection by Turnip vein clearing virus (TVCV) on the polarization of reflected light leading to high light reflections; this phenotype is not visible upon viral infection by Cucumber mosaic virus (CMV) (PubMed:28346494). Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. |
Q9LVE8 | MNHSNLANPTVSLTVTLIPKHPIRHLTSPIPNRNFTNPKLLFPLRLNETPSSSLAAKRVFIVRATVDGDGKTGNWVNRLPIPGLGAENVFRLISSATGSPIGQFISSPVTFLHSVDPRIKLVWLLTLVVLPARANLVVRLGLVLCTALLSILVLPRQVWIDQLARVSLLSGILFITLGLGSDGAPPMLQSRTPPSSITSLPNLPMSLSGYSYMLLKLGPLQFTRKGLSVGSTAACLTFIIFQSASICLATTTPEQLALALRWFLFPLTYIGVPVSEIILTLLLSLRFINLVFDEVRSVSLGIVSRRVNWQQLTVLETLDIFASFIRRIFKNIFRHAEQISQAMIVRGFRGESSSHKIYFFSGSSNKFADFASVLCLIGVISTALLSEYFLV | Was originally thought to belong to the ABC transporter family (PubMed:18299247). Lacks the conserved ABC domain, which is one of the features of the ABC transporter family. |
Q9C7F8 | MDNTERSSNGNIQAETEAKEEKKNIKKESVSLMGLFSAADKLDYFLMLLGGLGACIHGATLPLFFVFFGKMLDSLGNLSTDPKAISSRVSQNALYLVYLGLVNFVSAWIGVSCWMQTGERQTARLRINYLKSILAKDITFFDTEARDSNLIFHISSDAILVQDAIGDKTDHVLRYLSQFIAGFVIGFLSVWQLTLLTLGVVPLIAIAGGGYAIVMSTISEKSETAYADAGKVAEEVMSQVRTVYAFVGEEKAVKSYSNSLKKALKLGKRSGLAKGLGVGLTYSLLFCAWALLLWYASLLVRHGKTNGAKAFTTILNVIFSGFALGQAAPSLSAIAKGRVAAANIFRMIGNNNSESSQRLDEGTTLQNVAGRIEFQKVSFAYPSRPNMVFENLSFTIRSGKTFAFVGPSGSGKSTIISMVQRFYEPNSGEILLDGNDIKSLKLKWFREQLGLVSQEPALFATTIASNILLGKENANMDQIIEAAKAANADSFIKSLPNGYNTQVGEGGTQLSGGQKQRIAIARAVLRNPKILLLDEATSALDAESEKIVQQALDNVMEKRTTIVVAHRLSTIRNVDKIVVLRDGQVRETGSHSELMLRGGDYATLVNCQETEPQENSRSIMSETCKSQAGSSSSRRVSSSRRTSSFRVDQEKTKNDDSKKDFSSSSMIWELIKLNSPEWPYALLGSIGAVLAGAQTPLFSMGIAYVLTAFYSPFPNVIKRDVEKVAIIFAGAGIVTAPIYLLQHYFYTLMGERLTSRVRLSLFSAILSNEIGWFDLDENNTGSLTSILAADATLVRSALADRLSTIVQNLSLTVTALALAFFYSWRVAAVVTACFPLLIAASLTEQLFLKGFGGDYTRAYSRATSVAREAIANIRTVAAYGAEKQISEQFTCELSKPTKNAFVRGHISGFGYGLSQFLAFCSYALGLWYVSVLINHKETNFGDSIKSFMVLIVTAFSVSETLALTPDIVKGTQALGSVFRVLHRETKISPDQPNSRMVSQVKGDIEFRNVSFVYPTRPEIDIFKNLNLRVSAGKSLAVVGPSGSGKSTVIGLIMRFYDPSNGNLCIDGQDIKTLNLRSLRKKLALVQQEPALFSTTIYENIKYGNENASEAEIMEAAKAANAHEFIIKMEEGYKTHAGDKGVQLSGGQKQRVAIARAVLKDPSVLLLDEATSALDTSSEKLVQEALDKLMKGRTTVLVAHRLSTIRKADTVAVLHKGRVVEKGSHRELVSIPNGFYKQLTSLQEVL | Belongs to the ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily. |
F4INF8 | MAITLTNFTFLYMDANLKRLGDIVLGFGANVVTLLLILILTITRRNGRCNRRKSYIEKCLLYVTPALGACLSCVDLVLLVRTNRRREVILCFVPLSGFVMWIAVILSLKFACCACHVFTSQILCFWWIFRFLTDALHLNMIFTLQRVQEICLIMLDIAFGISINVLRIKQAHPKIIPLEDPLIEDDDDQKRIVRRLFLEKNGSWWDLFTFGYIGSIMKHGSVKQLELENLLTLPPEMDPFTCCENLLRCWQLQECNNYSTPSLIWSIYGVYGWPYFRLGLLKVFNDCIGFAGPLLLNRLIKSFLDTQYTFRLSKLKLKLRSSIMSVIYRKCLWVNTANRSGFSEGEIQTFMSVDADRIVNLCNSLHDLWSLPLQIGIALYLLYTQVKFAFLSGLAITILLIPVNKWISVLIASATEKMMKLKDERIRKTGELLTNIRTLKMYGWDNWFADWLKETRATEVTHLATRKYLDAWCVFFWATTPTLFSLCTFGLFALMGHQLDAATVFTCLALFNSLISPLNSFPWVINGLIDAFISTRRVSKFLCCLEHSRDFSIDSGFTSEDLAVCVEDASCTWSSNVEEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSVAYVPQVPWLLSGTVRENILFGKPFDSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCWILQRALLGPLLNKKTRVMCTHNIQAISCADMIVVMDKGKVNWSGSVTDMPKSISPTFSLTNEFDMSSPNHLTKRKETLSIKEDGVDEISEAAADIVKLEERKEGRVEMMVYRNYAVFSGWFITIVILVSAVLMQGSRNGNDLWLSYWVDKTGKGVSHYSTSFYLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILLANFVGLLGIIVVLSYVQVLFLLLLLPFWYIYSKLQVFYRSTSRELRRLDSVSRSPIYASFTETLDGSSTIRAFKSEEHFVGRFIEHLTLYQRTSYSEIIASLWLSLRLQLLGSMIVLFVAVMAVLGSGGNFPISFGTPGLVGLALSYAAPLVSLLGSLLTSFTETEKEMVSVERVLQYMDVPQEEVSGPQSLSDKWPVHGLVEFHNVTMRYISTLPPALTQISFTIQGGMHVGVIGRTGAGKSSILNALFRLTPVCSGEILVDGKNISHLPIRELRSCLAVVPQSPFLFQGSLRDNLDPLGLSEDWRIWEILDKCKVKAAVESVGGLDSYVKESGCSFSVGQRQLLCLARALLKSSKILCLDECTANIDVHTASLLHNTISSECKGVTVITIAHRISTVVDLDSILILDRGILVEQGKPQHLLQDDSSTFSSFVRASQ | Pump for glutathione S-conjugates. ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2. Ubiquitous. Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily. |
A2XCD4 | MPHFPNLPLPEAAAAAAHAALLALALLLLLLRSARALASRCASCLKTAPRRAAAVDGGLAAASSVGAWYRAALACCGYALLAQVAALSYEVAVAGSHVAVEALLLPAVQALAWAALLALAMQARAVGWGRFPVLVRVWWVVSFVLCVGIAYDDTRHLMGDDDDDEVDYAHMVANFASAPALGFLCLVGVMGSTGVELEFTDDDSSVHEPLLLGGQRRDADEEPGCLRVTPYGDAGIVSLATLSWLSPLLSVGAQRPLELADIPLMAHKDRAKSCYKAMSSHYERQRMERPGSEPSLAWAILKSFWREAAINGAFAAVNTIVSYVGPYLISYFVDYLSGKIEFPHEGYILASVFFVAKLLETLTARQWYLGVDVMGIHVKSGLTAMVYRKGLRLSNSSRQSHTSGEIVNYMAVDVQRVGDYAWYFHDIWMLPLQIILALAILYKNVGIAMVSTLVATVLSIAASVPVAKLQEHYQDKLMASKDERMRKTSECLKNMRILKLQAWEDRYRLKLEEMRNVECKWLRWALYSQAAVTFVFWSSPIFVAVITFGTCILLGGELTAGGVLSALATFRILQEPLRNFPDLISMIAQTRVSLDRLSHFLQQEELPDDATITVPHGSTDKAININDATFSWNPSSPTPTLSGINLSVVRGMRVAVCGVIGSGKSSLLSSILGEIPKLCGQVRISGSAAYVPQTAWIQSGNIEENILFGSPMDKQRYKRVIEACSLKKDLQLLQYGDQTIIGDRGINLSGGQKQRVQLARALYQDADIYLLDDPFSAVDAHTGSELFREYILTALASKTVIYVTHQIEFLPAADLILVLKDGHITQAGKYDDLLQAGTDFNALVCAHKEAIETMEFSEDSDEDTVSSVPIKRLTPSVSNIDNLKNKVSNNEKPSSTRGIKEKKKKPEERKKKRSVQEEERERGRVSLQVYLSYMGEAYKGTLIPLIILAQTMFQVLQIASNWWMAWANPQTEGDAPKTDSVVLLVVYMSLAFGSSLFVFVRSLLVATFGLATAQKLFVKMLRCVFRAPMSFFDTTPSGRILNRVSVDQSVVDLDIAFRLGGFASTTIQLLGIVAVMSKVTWQVLILIVPMAVACMWMQRYYIASSRELTRILSVQKSPVIHLFSESIAGAATIRGFGQEKRFMKRNLYLLDCFARPLFSSLAAIEWLCLRMELLSTFVFAFCMAILVSFPPGTIEPSMAGLAVTYGLNLNARMSRWILSFCKLENRIISVERIYQYCKLPSEAPLIIENSRPSSSWPENGNIELVDLKVRYKDDLPLVLHGISCIFPGGKKIGIVGRTGSGKSTLIQALFRLIEPTGGKVIIDDVDISRIGLHDLRSRLSIIPQDPTLFEGTIRMNLDPLEECTDQEIWEALEKCQLGEVIRSKDEKLDSPVLENGDNWSVGQRQLIALGRALLKQAKILVLDEATASVDTATDNLIQKIIRSEFKDCTVCTIAHRIPTVIDSDLVLVLSDGKIAEFDTPQRLLEDKSSMFMQLVSEYSTRSSCI | ABC transporter that may affect phytic acid transport and compartmentalization. May function directly or indirectly in removing phytic acid from the cytosol or in vesicle trafficking. Required for phytic acid accumulation in developing seeds. Phytic acid is the primary storage form of phosphorus in cereal grains and other plant seeds. Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily. |
A0A0P0VSW0 | MPHFPNLPLPEAAAAAAHAALLALALLLLLLRSARALASRCASCLKTAPRRAAAVDGGLAAASSVGAWYRAALACCGYALLAQVAALSYEVAVAGSHVAVEALLLPAVQALAWAALLALAMQARAVGWGRFPVLVRVWWVVSFVLCVGIAYDDTRHLMGDDDDDEVDYAHMVANFASAPALGFLCLVGVMGSTGVELEFTDDDSSVHEPLLLGGQRRDADEEPGCLRVTPYGDAGIVSLATLSWLSPLLSVGAQRPLELADIPLMAHKDRAKSCYKAMSSHYERQRMERPGSEPSLAWAILKSFWREAAINGAFAAVNTIVSYVGPYLISYFVDYLSGKIEFPHEGYILASVFFVAKLLETLTARQWYLGVDVMGIHVKSGLTAMVYRKGLRLSNSSRQSHTSGEIVNYMAVDVQRVGDYAWYFHDIWMLPLQIILALAILYKNVGIAMVSTLVATVLSIAASVPVAKLQEHYQDKLMASKDERMRKTSECLKNMRILKLQAWEDRYRLKLEEMRNVECKWLRWALYSQAAVTFVFWSSPIFVAVITFGTCILLGGELTAGGVLSALATFRILQEPLRNFPDLISMIAQTRVSLDRLSHFLQQEELPDDATITVPHGSTDKAININDATFSWNPSSPTPTLSGINLSVVRGMRVAVCGVIGSGKSSLLSSILGEIPKLCGQVRISGSAAYVPQTAWIQSGNIEENILFGSPMDKQRYKRVIEACSLKKDLQLLQYGDQTIIGDRGINLSGGQKQRVQLARALYQDADIYLLDDPFSAVDAHTGSELFREYILTALASKTVIYVTHQIEFLPAADLILVLKDGHITQAGKYDDLLQAGTDFNALVCAHKEAIETMEFSEDSDEDTVSSVPIKRLTPSVSNIDNLKNKVSNNEKPSSTRGIKEKKKKPEERKKKRSVQEEERERGRVSLQVYLSYMGEAYKGTLIPLIILAQTMFQVLQIASNWWMAWANPQTEGDAPKTDSVVLLVVYMSLAFGSSLFVFVRSLLVATFGLATAQKLFVKMLRCVFRAPMSFFDTTPSGRILNRVSVDQSVVDLDIAFRLGGFASTTIQLLGIVAVMSKVTWQVLILIVPMAVACMWMQRYYIASSRELTRILSVQKSPVIHLFSESIAGAATIRGFGQEKRFMKRNLYLLDCFARPLFSSLAAIEWLCLRMELLSTFVFAFCMAILVSFPPGTIEPSMAGLAVTYGLNLNARMSRWILSFCKLENRIISVERIYQYCKLPSEAPLIIENSRPSSSWPENGNIELVDLKVRYKDDLPLVLHGISCIFPGGKKIGIVGRTGSGKSTLIQALFRLIEPTGGKVIIDDVDISRIGLHDLRSRLSIIPQDPTLFEGTIRMNLDPLEECTDQEIWEALEKCQLGEVIRSKDEKLDSPVLENGDNWSVGQRQLIALGRALLKQAKILVLDEATASVDTATDNLIQKIIRSEFKDCTVCTIAHRIPTVIDSDLVLVLSDGKIAEFDTPQRLLEDKSSMFMQLVSEYSTRSSCI | ABC transporter that may affect phytic acid transport and compartmentalization. May function directly or indirectly in removing phytic acid from the cytosol or in vesicle trafficking. Required for phytic acid accumulation in developing seeds. Phytic acid is the primary storage form of phosphorus in cereal grains and other plant seeds. Expressed in roots, leaf sheaths, leaf blades and developing seeds. Strong reduction in seed phytic acid, and strong increase of inorganic phosphate and myo-inositol levels in seeds. Seedling lethality when homozygous. Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily. |
Q8GX48 | MTTPEGAMYVAWEDLTVVIPNFGEGATKRLLNGVNGCGEPNRILAIMGPSGSGKSTLLDALAGRLAGNVVMSGKVLVNGKKRRLDFGAAAYVTQEDVLLGTLTVRESISYSAHLRLPSKLTREEISDIVEATITDMGLEECSDRTIGNWHLRGISGGEKKRLSIALEVLTKPSLLFLDEPTSGLDSASAFFVVQILRNIASSGKTVVSSIHQPSGEVFALFDDLLLLSGGETVYFGEAESATKFFGEAGFPCPSRRNPSDHFLRCVNSDFDNVTAALVESRRINDSSFSLHQLHETTNTLDPLDDIPTAEIRTTLVRKFKCSLYAAASRARIQEIASIVGIVTERKKGSQTNWWKQLRILTQRSFINMSRDLGYYWMRIAVYIVLSICVGSIFFNVGRNHTNVMSTAACGGFMAGFMTFMSIGGFQSFIEEMKVFSRERLNGHYGVAVYTVSNLLSSLPFIILMCLSTSSITIYMVRFQSGGSHFFYNCLDLICAITTVESCMMMIASVVPNFLMGVMLGAGYIGIMVLSAGFFRFFPDLPMVFWRYPVSYINYGAWALQGAYKNEMIGVEYDSPLPLVPKMKGELILQTVLGINPESSKWLDLAVVMMILIGYRIAFFAILKFREKVFPVIHMLYTKRTLSHIQKRPSFRRMTPFPSRRYPVHHALSSQEGLNSPLH | By NaCl. Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. |
Q08644 | MGVADLIKKFESISKEEGDATVDTNSSSKPLKSNDETKELHQQESTAVPQEVDVNEEFENEPETINSSRTAEKPLETNLPKPETNEEDEEEGSMSENKIYSKGENADINVNDFQEYKEMENTGAEVLASSVEESDAIQEGVAEETEGIATPKQKENEKNDESEEESANNASEPAEEYSQSEEDADIEQSNGKETENAENASQQANDGSTSTTTSKNKKKKNKKKNKKKRNGNVNTNANVDDSTKTGENDDTTGDTTSSTTSAIQEVNDLEVVDDSCLGIDQQHNREHLKALTQDVKEETLENIAHEGRGDNTGDQNAVEKSDFEKSDTEGSRIGRDLPFEFGKRNLTEESDVWDHNAWDNVEWGEEQVQQAEEKIKEQFKHPVPEFDKKLYNENPARYWDIFYKNNKENFFKDRKWLQIEFPILYASTRKDAEPVTIFEIGCGAGNTFFPILKDNENENLRIIAADFAPRAVELVKNSEQFNPKYGHATVWDLANPDGNLPDGVEPHSVDIAVMIFVFSALAPNQWDQAMDNLHKILKPGGKIIFRDYGAYDLTQVRFKKNRILEENFYVRGDGTRVYFFSEEKLREIFTKKYFLENKIGTDRRLLVNRKRQLKMYRCWVQAVFDVPQ | S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Thr) and tRNA(Ser) (PubMed:21518804, PubMed:21518805, PubMed:28003514). N(3)-methylcytidine methylation of tRNA(Thr) requires the N6-threonylcarbamoylation of tRNA (t6A37) by the EKC/KEOPS complex as prerequisite (PubMed:28003514). N(3)-methylcytidine methylation of tRNA(Ser) requires the formation of N(6)-dimethylallyladenosine(37) (i6A37) by MOD5 as prerequisite (PubMed:28003514). Methylation of tRNA(Ser) is also stimulated by SES1 (PubMed:28003514). Binds F-actin and shows weak F-actin cross-linking activity (PubMed:9467951). cytidine(32) in tRNA(Thr) + S-adenosyl-L-methionine = H(+) + N(3)-methylcytidine(32) in tRNA(Thr) + S-adenosyl-L-homocysteine cytidine(32) in tRNA(Ser) + S-adenosyl-L-methionine = H(+) + N(3)-methylcytidine(32) in tRNA(Ser) + S-adenosyl-L-homocysteine Interacts with SES1. Cytoplasmic and cortical cytoskeleton. N- and C-terminal domains are encoded in separate ORFs that are translated into one protein via a +1 frameshift (PubMed:9467951). ABP140 mRNA translation follows a cotranslational transport: mRNA is transported to the distal pole of the mother cell, independently of the SHE machinery, and follows a translational coupling, in which ABP140 mRNA is tethered to actin cables via its nascent protein product and is transported to the distal pole by actin retrograde flow (PubMed:21792172). Produced by ribosomal frameshifting between codon Leu-277 and Gly-278. Belongs to the methyltransferase superfamily. METL family. |
Q9FZH4 | MGFSSFISQPLSSSLSVMKRNVSAKRSELCLDSSKIRLDHRWSFIGGSRISVQSNSYTVVHKKFSGVRASWLTTTQIASSVFAVGTTAVLPFYTLMVVAPKAEITKKCMESSVPYIILGVLYVYLLYISWTPETLKYMFSSKYMLPELSGIAKMFSSEMTLASAWIHLLVVDLFAARQVYNDGLENQIETRHSVSLCLLFCPVGIVSHFVTKAIINNQYK | Required for neoxanthin biosynthesis, an intermediary step in abscisic acid (ABA) biosynthesis. Probably not involved directly in the enzymatic conversion of violaxanthin to neoxanthin. Cannot convert violaxanthin to neoxanthin in vitro. Required for ABA biosynthesis in response to drought stress (PubMed:17470058). Required for neoxanthin biosynthesis which is involved in photoprotection of photosystem II (PSII). Neoxanthin acts as an antioxidant within the photosystem PSII supercomplex (PubMed:17351115). Expressed in root vasculature, root hairs, leaves, trichomes, sepals, stamens, stigma, pedicels, siliques and embryo. Induced by heat stress. No visible phenotype under normal growth conditions, but mutant plants accumulate violaxanthin and completely lack neoxanthin. Plants over-expressing ABA4 have increased levels of trans-neoxanthin. |
A0A384JQF5 | MSSQPFTNKVIALTGSASGIGLETAKLLASRGARLSLADIQEDKLKELQAQLESEYYVDVITTKVDVRKFGEVEAWINKTIDNFGKLDGSANLAGVAPESIGLKGIVEQDLDEWEFVLGVNLTGTMNSLKAQLKVMANNGSIVNASSIRGLTGAAKNASYSSAKHGIIGLTRTAAKEVGGKGIRVNAICPGRISTPMLKTAENSIGLHLQPGSANYPPIALGRDGEAKEVAQLVAFLLSDESTYISGADISIDGGWRC | Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses (PubMed:15240257, PubMed:16820452). The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase aba3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene (PubMed:30226766). The cytochrome P450 monooxygenase aba1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (Probable). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase aba2 and the short-chain dehydrogenase/reductase aba4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (Probable). Aba2 is responsible for the hydroxylation of carbon atom C-1' and aba4 might be involved in the oxidation of the C-4' carbon atom (PubMed:16820452). Hormone biosynthesis. Constitutively expressed at a low level. Reduces the production of abscisic acid (ABA) and accumulates a compound that corresponds probably to 1',4'-trans-diol-ABA. Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
Q14RS1 | MSSQPFTNKVIALTGSASGIGLETAKLLASRGARLSLADIQEDKLKELQAXXESEYHVDVITTKVDVRKFGEVEAWINKTIDNFGKLDGSANLAGVAPESIGLKGIVEQDLDEWEFVLGVNLTGTMNSLKAQLKVMANNGSIVNASSIRGLTGAAKNASYSSAKHGIIGLTRTAAKEVGGKGIRVNAICPGRISTPMLKTAENSIGLHLQPGSANYPPIALGRDGEAKEVAQLVAFLLSDESTYISGADISIDGGWRC | Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses (PubMed:15240257, PubMed:16820452). The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase aba3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene (PubMed:30226766). The cytochrome P450 monooxygenase aba1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (Probable). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase aba2 and the short-chain dehydrogenase/reductase aba4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (Probable). Aba2 is responsible for the hydroxylation of carbon atom C-1' and aba4 might be involved in the oxidation of the C-4' carbon atom (PubMed:16820452). Hormone biosynthesis. Constitutively expressed at a low level. Reduces the production of abscisic acid (ABA) and accumulates a compound that corresponds probably to 1',4'-trans-diol-ABA. Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
G4N1P8 | MGSIENPEIMASTMLHILPLAGKVYGITGGASGIGLATAQILSRRGATVCIADVDPKAMASAEVYFSGQSGAKYSITKVDISKRSEVNAWVDGIISQFGRLDGAANVAGVIGKIHGAVPVSEMDDDEWDKIVAVNLTGTMYCMRAQLRNIVDGGSIVNVASIHGLKGFANHAAYDASKHGVIGLTKAAAQENGAREIRVNAVAPGAIYTPLMQKNWDITGRPKDAPFDDPSAFRRQGTAMETGNVIAFLLGPDSTFVSGSVYSVDGAWI | Short-chain dehydrogenase/reductase involved in the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses (PubMed:26648962). During pathogen-host interaction, ABA plays a dual role in disease severity by increasing plant susceptibility and accelerating pathogenesis in the fungus itself (PubMed:26648962). The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase ABA3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene (By similarity). The cytochrome P450 monooxygenase ABA1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (By similarity). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase ABA2 and the short-chain dehydrogenase/reductase ABA4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (By similarity). ABA2 is responsible for the hydroxylation of carbon atom C-1' and ABA4 might be involved in the oxidation of the C-4' carbon atom (By similarity). Hormone biosynthesis. Expression is up-regulated in spores. Leads to slower vegetative growth and dark pigmentation of the mycelia (PubMed:26648962). Leads also to the secretion of a very dark pigment (PubMed:26648962). Affects sporulation and appressoria formation (PubMed:26648962). Shows hyper-branching of the germ tubes, as well as unusual bulges along the hyphae with less melainized appressoria (PubMed:26648962). Significantly reduces the production of abscisic acid (ABA) (PubMed:26648962). Highly reduces virulence (PubMed:26648962). Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
L7I518 | MGSIENPEIMASTMLHILPLAGKVYGITGGASGIGLATAQILSRRGATVCIADVDPKAMASAEVYFSGQSGAKYSITKVDISKRSEVNAWVDGIISQFGRLDGAANVAGVIGKIHGAVPVSEMDDDEWDKIVAVNLTGTMYCMRAQLRNIVDGGSIVNVASIHGLKGFANHAAYDASKHGVIGLTKAAAQENGAREIRVNAVAPGAIYTPLMQKNWDITGRPKDAPFDDPSAFRRQGTAMETGNVIAFLLGPDSTFVSGSVYSVDGAWI | Short-chain dehydrogenase/reductase involved in the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses (PubMed:26648962). During pathogen-host interaction, ABA plays a dual role in disease severity by increasing plant susceptibility and accelerating pathogenesis in the fungus itself (PubMed:26648962). The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase ABA3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene (By similarity). The cytochrome P450 monooxygenase ABA1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (By similarity). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase ABA2 and the short-chain dehydrogenase/reductase ABA4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (By similarity). ABA2 is responsible for the hydroxylation of carbon atom C-1' and ABA4 might be involved in the oxidation of the C-4' carbon atom (By similarity). Hormone biosynthesis. Expression is up-regulated in spores. Leads to slower vegetative growth and dark pigmentation of the mycelia (PubMed:26648962). Leads also to the secretion of a very dark pigment (PubMed:26648962). Affects sporulation and appressoria formation (PubMed:26648962). Shows hyper-branching of the germ tubes, as well as unusual bulges along the hyphae with less melainized appressoria (PubMed:26648962). Significantly reduces the production of abscisic acid (ABA) (PubMed:26648962). Highly reduces virulence (PubMed:26648962). Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
A0A0A7HMS2 | MSSSSSQSSLYQPRPVLSSQRFSPAPDYIDTRRSFHGDSRLPLRESTGNVQQQHHHQEPSSAHSSFNGGSLVGCYQTPVTLSPSMQSSIPPPAPIVPSQSFDCLRSLQATTSRQHHHVPPPLPQVPTRYHQRGKPRNSINPLYFWPAFRQYRNRQAHKDTQKDKGGVWRRPELEDAFVDSVLLMPHMGRRKFSMGGKLHGRNMLISEYIFVICVALLGSKEIFRIDNSNDSIEQMGRKQVSSHMQVVKKFFEDLRCFHFLFPSEEKKEPGTTNSDDFYEEEEQESFKSNPVLTALAEGRVPDVRPNYEYFSQLLALQSSITVRPKTVEIFVSSADVKIRDEVAYDANDNPLDPASFPHLGKYMNSSGDDKPNVLGKDVLLHEYTRSLDRSTSACVKTVTRRWQRDAPAMYDSLDLPDRDEDCLLLEMCSTVDLHEHAKFPSGSELTGYVEVSVTQPALQGHRWKCVTRLTRPPELQTDEGRPEMYSNESGIHRRGCADTRHEDCGCHLRPRQDIHVPFPAVEWASILSMAVQYPDVEHQRKKEKRSCGKKPDLERSASSSKRKRSEDEGDAAAWTRREPTGSDLICKVAMYQELWSCAPDSTRWTRQAIIFWRFSTTNQWYKYNPVFRPAGTTWRWLTVNDPMSRYHQQRALVYPSAGGNNMPRDAVMSPTPSVSQHLTATMSENFSQAWDSSGSNVTTHTQVHVAGGGGGGGSNMTTLFDSFPSGLATPPPTASLHGSYSASGSFDAGNGVGGCYMPPTCGGGADGPHGGLPAPSQSYFDAAGQTVNTTFGDVKPLLSGSATNPYLPGAAGGGGTGSLDLSGQFAYDDGQQHQHQHQHQQHQQQNHNGGSNGGLPGWDMGPALDSWTAGSSAGGAPAATPTGPDWGPTAPVPRMTEHHPGMWDPVHWSNHGTPGRGGEGSPRQMKRRRTEVLVDGVPVTAGW | BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (By similarity). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity). Binds to the sequence 5'-CATTCY-3', where Y is a pyrimidine, making both major- and minor-groove contacts (By similarity). localizes to the nuclei of phialides and terminal cells of mature conidia (By similarity). Expression is positively regulated by stuA through direct binding of stuA to the abaA promoter region (PubMed:26283234). Belongs to the TEC1 family. |
E9RD40 | MATDWQPECIAPQHQSGLENIGHHTDRALQNTSGNVQSYSDAILHGGMSGRDDHLQHLAYKYSHAPVHPQPMQTATTLHPHHILNARVQAKKLRRVQSLGPNHAGARRGRSYLKSQKYLEYRARPRRDTGKDGEPVWSDELEDAFQQALEANPPMGRRKWSERGKSYGRNELIAEYIYKVTGKKRTRKQVSSHLQVLDSFLKGDPDWERLVREQPADRSGNQHQPVGPKWRTSLDHPLPSHYGGHMHATYHDHLSPVQPYVGELPPPHYTLGSNMHERSTDTIHGFNFDMWVSAPQQANQGDKAFHVYTCLQGDQYHPVAPPMPLENVRDWRTTFPHLNSVMEELDGPLDCEIILLEASLKLMNDFPPPGSKLGIQLDIDFAPPGMTDATVLSQMDNWTCSTYIYEDGNRLSKADHNLARPLSTKVKPPFESSWWAKLFTELTQDKQMAEKSGRHQNADDHIRQFFRSLSAVQEIRAISQNSRRVSQGSGHPGDCSKRMAILLWKFRQTLPDEVGLTTWRKLIPPPDRTMMNSPKPATGIDLPPLSLDSILLKPQPPNVYQNPQGHDLLHQNGTSQPHWPLYPPPHESMSNMYHSTGSFDFLNSVSKAEDGLPDRTAVTSILDSFPAMPPQETSQPSSLNVSSGGPVMLNVHDMSLSHHNLAGYALSHDNHYVPSQQHGVSVHDSSNVLNNIFGPGSQPMDEIGNSQSAWGPPIPSTTIPSDVGSNHYTHLPYHHHDHQTSASRESHPPNGFEGLMGPDDLMDKIVGSMPDDPGMNGAGPDHASAAYADTNATEAVQ | BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (By similarity). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity). Binds to the sequence 5'-CATTCY-3', where Y is a pyrimidine, making both major- and minor-groove contacts (By similarity). Essential for differentiation and functionality of phialides as conidiogenous cells (PubMed:20966095). Regulates autolysis and cell death (PubMed:20966095). Positively regulates expression of the gliotoxin biosynthetic gene cluster in actively growing vegetative cells, and likely bridges morphological and chemical development during the life-cycle (PubMed:26032501). Negatively regulates expression of the melanin biosynthetic gene cluster (PubMed:24123270). localizes to the nuclei of phialides and terminal cells of mature conidia (By similarity). Highly expressed during conidiation (PubMed:20966095). Expression is positively regulated by hsp90 (PubMed:22822234). Expression is decreased by 2',4'-Dihydroxychalcone (2',4'-DHC) (PubMed:26190922). Results in the formation of aberrant conidiophores exhibiting reiterated cylinder-like terminal cells lacking spores and causes delayed autolysis and cell death (PubMed:20966095). Reduces significantly expression of the gliotoxin biosynthetic gene cluster including gliM, gliP, gliT, and gliZ (PubMed:26032501). Belongs to the TEC1 family. |
Q5H7P4 | MAEWQTECMLPPTQPGFEGVGPHPGRVLQNTSGNIQSYSDTLAHTDPTGRDDHFSHYGFKYPHQPPVPTHPMPTTTGLHPQQVINNRFHTKKLRRLQSLGPNLIGPRRTRSYLKSQKYIEYRARPRRDTGKDGEPVWSDELEDAFQQALEANPPMGRRKWSERGKSYGRNELIAEYIYKTTGKRRSRKQVSSHLQVLDSFLKGDPDWERLVREQPADRSNGQPPSAGPRWRNSLELPFSSHYNSHNYPSYHDSLRPVQSYSGELPPPHVVFHPNLHAEATNINKIYGLSFDMWVSAPNQPGGIESAFHLYTRLQGDQRHPAPPKRLENIPNWRTSFPHLNSVMADVNNPLNCDIILLEANLRLMDDFPPSGSKLGIQLELDFTQPPNGDALTNQMENWSCSTYIYEEGQNIYRARQDLPKQQSNKVKPPFESTWWAKRFTELTEIAKDRQLNELADRQTRDYFRTLTAVQEIRATPSSRRVSNQYPDNSQDDSKRMAILLWQFRQTRSNEVGTTTWRRVTSPSSDRNTIPSPKPVTGIDLPPLSFYANSLARPAPSIYQAPQSHDLVHHNGTSQPQWSMYQPPQDSIFNANGGFDLLNSITKPEGGLHDKTAVTSVLDTYPNLQPEVSQPTSLNGSNGGPGMLSIPDMSLSHTNLNAYNLSGHDNHYGTPQHPGVSVPDNSHVLNNGIFGSSTQSIDDMSQTHAPWPTPTSSITDVGSSNYSHLQFSDHHVPSVSRESHQPNHFEVLLGPDDLIVGSMPGDPGINGAAHGHMNHTYTENNAVEAA | BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (PubMed:19850144). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity). Binds to the sequence 5'-CATTCY-3', where Y is a pyrimidine, making both major- and minor-groove contacts (By similarity). Controls expression of wetA (PubMed:19850144). localizes to the nuclei of phialides and terminal cells of mature conidia (By similarity). Expression is controlled by brlA (PubMed:19850144). Forms aberrant phialides (PubMed:19850144). Belongs to the TEC1 family. The predicted 2 genes AO090003000856 and AO090003000857 have been merged. The predicted 2 genes AO090003000856 and AO090003000857 have been merged. |
Q5BGA8 | MATDWQPECMVSQNQAALESIGAHSDRALQNTSGNVQAYSDSLAHHDTTGRDDPLQHYTLKYPHPPVPVPSHPLPTATANLYHPQLLSHRYQVKKLRRLQSNGSSYAGSRRGRSYLKSQKYLEYRARPRRDTGKDGEPVWSDELEDAFQQALEANPPMGRRKWSERGKSYGRNELIAEYIYKLTGKRRTRKQVSSHLQVLDSFLKGDPDWERLVREQSDRSTAQTQPVGPRWRTSMDHLPSSHYGTHATSSYPEPMRLMPPYSADLQLPQYSPTSTQQDTNNNTIQGLSFDMWVSAPNKPDRIDDAYHLYTRLQGDQRQPPMPLEDLKNWRVSFPHLSSSLSDVNDPLNCEIILLETNLELMDDFPPMGSRLGIHLELDIANPMSGTAPTVNQMENWTCSTYIYEDGRRTMEAYHNLTKPHTTKVKPPFESSWWAKTFTKLTQDKREAESTGHHHAADERTRRYFHSLTAVQEIRATVPPSLRRLQNHYPGSPAEESKRMAIILWKFRQTRPNEVGTTTWRKLITSPDRALTNSPRPSTAIDLPPLSLDSILLSKPTSNLYQAPPQHHDLLHQNAPSQQSWSLYQPSHDHVNSLYHSAGAFDFLNSITKPEEGLSDKTAPTSVLDPFPNLTQQTTSQTAGINVSSGTPVMLQIPDLSLSSNLGTYGLGHESHYVPSHHNAANLHDHSSTTGLGHYFAPSTQSLDEISHSHAPWSAPNTTISGDTSGGNYHHLPFTTSDHSVTVSRESHQNHSFEGLLPSDDLVGIVGGLSGDPNMNGAGPEHTSSAYAEHTAVEAV | BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (PubMed:2655931, PubMed:2196567). They act individually and together to regulate their own expression and that of numerous other sporulation-specific gene (PubMed:2655931, PubMed:2823119). Controls temporal and spatial specificity in Aspergillus development (PubMed:2655931, PubMed:7704830). Directs the differentiation of phialides and is continuously required for maintenance of their function (PubMed:2152124). Expression of abaA leads to activation of brlA and wetA, cessation of vegetative growth, and accentuated cellular vacuolization (PubMed:2655931). Binds to the sequence 5'-CATTCY-3', where Y is a pyrimidine, making both major- and minor-groove contacts (PubMed:8139553). Multiple abaA binding sites are present in the cis-acting regulatory regions of several developmentally controlled structural genes as well as those of the upstream regulatory gene brlA, the downstream regulatory gene wetA, and abaA itself (PubMed:8139553). localizes to the nuclei of phialides and terminal cells of mature conidia (By similarity). Expression is induced during conidiation, after conidiophore vesicles, metullae, and phialides had formed (PubMed:2823119). Negatively regulated by velC (PubMed:24587098). In the promoter, a 45-base-pair region encompassing the major and minor abaA transcription initiation sites contains directly repeated sequences related to the mammalian initiator (Inr) element and is sufficient for correct transcription initiation and for developmental induction (PubMed:2117702). Prevents the formation of normal conidiophores (PubMed:2823119, PubMed:2152124). Fails to form any viable conidia, even though it does produce morphologically normal phialides(PubMed:2655931). Belongs to the TEC1 family. |
S5FRT9 | MSSSLYHPRPVLSSQRYTPSPDYLQDARRTYHDNSRLPLRETASNAQSHNFNSMVPCYSSQVGISPSVPASLPAPMIPSQSFECLYRVPTPRNQPRFQQRRPRNEVNPLYFWPAFRQYRNRQAHKDTQKDKGGVWRRPELEDAFVDSVLLMPHMGRRKFSMGGKLHGRNMLISEYIFTICVAILGSKEIFRIDNSNDSIEQMGRKQVSSHMQVVKKFFEDLRCFHFLFPAEEKKEPGSTNSDDYYDEEEQESFKSNPVLTALAEGRVPDVKPNYEYFSQLLALQSLISVRPKTAEVYVSSSEVKFRDEIAYDAQDAPLDTESFPHLNKYNNCDDSPSVLGKDVLLHEYTRSLDRTTSACVKTVTRRWQKDAPEIYETLELPTRDEECLLLEMCATLELHEHARFPSGSELTGFVEVAITNPNLQSHRWKCVTRLTRPSELHSDDKKSSVYTNETGIHRRGCSDSKPDCDCHSRPRQDIHVPFPAVEWASILSMAVQYPDVEHQRKKEKRTKGDDRKNLDRAGSKRKRSEDDGDAASWARRDLTGSDLICKVAMYQELWSCAPDSNRWVRQGIVFWRFNTTNQWYKYNPVFKPAGTSWRWLTVNDPMSRYHQQKALVYPSASMSLDSIMSPTPSINQHMTAAMNETFSSAWDPSVSLAQVPNATATNNGLTLFESFSGGLATPPPTAGLQGSYSGSFDHGMPPSTGVGFIPSTCSTAGESHPGTGHGHSHSAAYYDAQTTLADLKPVMSTVNPYQSPTTSSGLDLSSSLVYDNAECDTGLQGWDMPALDGWSTGAGSGSEWGSHHKVEPSSDQTALWTQSQWAQMAGDRDGSPRPMKRRRGDGIDSHIPPTMTAAAGGW | AbaA and wetA are pivotal regulators of conidiophore development and conidium maturation (By similarity). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity). Binds to the sequence 5'-CATTCY-3', where Y is a pyrimidine, making both major- and minor-groove contacts (By similarity). Plays a pivotal role in conidiation by regulating cell cycle pathways and other conidiation-related genes (PubMed:24039821). localizes to the nuclei of phialides and terminal cells of mature conidia (PubMed:24039821). Expression is positively regulated by flbD (PubMed:25277408). Leads to abnormally shaped phialides and abolishes production of conidia (PubMed:24039821). Belongs to the TEC1 family. Extended N-terminus. |
E9EMI7 | MSSLFQPRPVLSSQRYSQSPDYVDTRRSIHNGRLPLRESTGNAQSHSFNGLVSCYQNQVALAPSMQTTIPAPMVPSQSLDCLYRVPTPRQQARFQRRPKTSVNPLYFWPAFRQYRNRQAHKDTQKDKGGVWRRPELEDAFVDSVLLMPHMGRRKFSMGGKLHGRNMLISEYIFVICIALLGSKEIFRIDNSNESIEQMGRKQVSSHMQVVKKFFEDLRCFHFLFPSEEKKEPGSTNSDDCYDEEEQESFKSNPVLTALAEGRVPDVKPNYEYFSQLLALQSSICTRPKTCEIFVSSSDIKIRDDVAYDVHDTPLDQASFPHLNKYTNCDDSPNVLGKDVLLHEYTRSLDRTTSACAKSVTRRWQHDAPAMYETLELPSRDEECLLLEMCATLELHEHAKFPSGSELTGFVEVAITQPALQNHRWKCITRLTRPAELHSDEGKHGVYTNDSGIHRRGCSDSKAECECHTRPRQDIHVPFPAVEWASILSMAVQYPDVEHQRLKEKRRKYADGDGKKELERAGSKRKRSEDEGDAASWTRREPTGSDLICKVAMYQELWSCAPDSTQWTRQAIIFWRFNTTNQWHKYNPVFKPAGTTWRWLTINDPMSRYHQQKALVYPTANVSRDALMSPTPTIHQHLTAAMNETFNSWDQGSSAPHVPHVPPLQTPNNSIGLFDSFSNGLATPPPTATLPPAYPTGNFDSRSGSFDARSASFDTRSGSFDGNLGPNNGVAFLPTTGPPPQHERQPTALGNNNQPFFDGQQSFSEVKPINTAVNSYMTASTSLELPNQLVYDNSGVDTSNMQGWDMSALDGWSAAASAPGSATAEWGPNTKVESHAGDHHGAMWAPPHWPLSAGAAPSSHERGASPRPLKRRRETMDVHVPVTAGW | BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation. They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (PubMed:29958281). BrlA, abaA and wetA act together to positively regulate the expression of the Pks1 gene cluster that mediates the biosynthesis of an anthraquinone derivative pigment that contributes to conidial pigmentation that provides protection from UV radiation, heat and cold stress (PubMed:29958281). Expression increases significantly during initiation of conidiation and remains elevated until colourisation is stabilized (PubMed:29958281). Expression is positively regulated by BrlA (PubMed:29958281). Produces phialides on which short deformed hypha are formed. Belongs to the TEC1 family. |
K9GDC6 | MATGWQPECLVTQNQSSLGPVEAHSDRALQNTTGNVQSYSDHLTHADIAAREDQLHQLGFKYPHAPHHPQPLSASGLDQQHVAARLHQRKLRRLHSVGPNSQSRRARSSYLKSQKYLEYRRRPRRDTGKDGEPVWSDELEDAFQQALEANPPMGRRKWSERGKSYGRNELIAEYIFKLTGKRRTRKQVSSHLQVLDSFLKGDPDWERLVREASPERSSSVHGSAPAPKWRTAVEHTSASSHYGSHTHGSYHDHMRSMQPYAGDLPPPHYTLGSNMQEAAASTIHGFNFDMWVTAPQQANRIGKALHTYTRLQGDLHHSAASSMPLEHVNGWRSSFPQLASMVDDINNPMDCDIILLEVNLELMTDFPPARSQLGIQLDLDFGHPSAGDVFGVSQMDNWTCSTHIYEDGQKLIESHDDLPKTQSTKVKPLFESSWWAKMFTKVTQDKRMAEDSGNPQVAREADDNTRNFFRSLSAVQELRATSPSSHRLSNQYQGHHGDESKRMAVLVWKFRQTRPGQVGTTTWRRLIPAPDRTSNNSPLAVSGIDLPPLSLDSILLNKASHQGMYQTPQPHDLIPHPSQSHSQWSLYHPPHDNVANLFNPSGHLDFLASISKAEDTINDKIAVTSVLDSFSTSLAPESIPSTSLHGPSGAPVMLNVHDLPLSHPGIGYAMGHEASHYVPSHQHSVNMHDSNGVLHSFFGSNMQPLDDLSHSHASWGAHSTSIPGDVGAGSYHLSYHPEHHGHGPVSRESQQPHHFDSLLPSEDLMDKIVGRMSNGASMHGAGPDAAGYDNSTVDSV | BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (By similarity). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity). Binds to the sequence 5'-CATTCY-3', where Y is a pyrimidine, making both major- and minor-groove contacts (By similarity). Plays an essential role in the differentiation and functionality of phialides (PubMed:25530311). localizes to the nuclei of phialides and terminal cells of mature conidia (By similarity). completely abolishes conidia formation and leads to the formation of compact white colonies (PubMed:25530311). Produces extremely elongated and immature phialides with defective morphology (PubMed:25530311). Belongs to the TEC1 family. |
W6PQG8 | MATDWQPECLVAQNQPSLDPVGAHSDRALQNTTGNVQSYSDQLAHAGVTARDDQFHQYSFKYPHGPHPQPLSAPGLHQQHVAARLHQRKLRRLHSVGPNSQSRRAQSSYLKSQKYMEYRRRPRRDTGKDGEPVWSDELEDAFQQALEANPPMGRRKWSERGKSYGRNELIAEYIFKLTGKRRTRKQVSSHLQVLDSFLKGDPDWERLVREPALERSSSVHGSAPAPKWRTAVEHPSGSSHYGSHTHPSYHDHMRSMQPYAGDLPPPHYTLGSNMQETAASTIHGFSFDMWVSAPQQANRIDKALHAYTRLQGDLHHPVAPPMPLEHVNGWRSSFPQLASMVDDVNNPLDCDIILLEVNLELMTDFPPTGSRLGIQLDLDYGHPSAGDVLGVSQMDNWTCSTHIYQDSQKLLETYHDLPKTQSTKVKPLFESSWWAKLFTQLTQEKRIAEDSGNPQAARDADDHARQFFRSLSAVQEIRATSPSSCRLSNQYQGHHGDESKRMAVLAWKFRQTRPGEVGTTTWRRLIPAPDRTTTNSPRPASAVDRVPLSLDSILLNKPSHQGIYQAPHPHDLIHHPSQSQSQWPMYQSPHDNVSNLYNPSGHLDFMSSISKAEDGLNDKIAVTSVLDSFSASLAPESISSTSLHGSSGAPVMLNVHDLPLTHPGMGYTMGHETSHYVPSQHHSVNMHDSNSVLHGFFGSHTQPLDDLSHGHGSWGTHSTSIPGDVGAGSYHIPYQAEHHGPVSRESQQPHQFDGLLPSEDLMDKIVGRMSNGSGMHGAGPDAGYDNATVDAV | BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (By similarity). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity). Binds to the sequence 5'-CATTCY-3', where Y is a pyrimidine, making both major- and minor-groove contacts (By similarity). localizes to the nuclei of phialides and terminal cells of mature conidia (By similarity). Expression is positively regulated by pcz1 (PubMed:25811807). Belongs to the TEC1 family. |
B6H7F3 | MATDWQPECLVTQNQTSLDPVGAHSDRALQNTTGNVQSYSDQLAHADITAREDQLHQLGFKYPHAPHHPQPLSAPGLHQQHVAARLHQRKLRRLHSVGPNSQSRRARSSYLKSQKYLEYRARPRRDTGKDGEPVWSDELEDAFQQALEANPPMGRRKWSERGKSYGRNELIAEYIFKLTGKRRTRKQVSSHLQVLDSFLKGDPDWERLVREASPERSSSVHGSAPAPKWRTAMEHPSASSHYGSHTHPSYHDHMRSMQPYAGDLPPPHYPLGSNMQEAAASAIHGFSFDMWVSAPQQANRLDKALHAYTRLQGDLHHPVAPPMPLEHVSGWRSSFPQLASMVDDINNPLDCDIILLEVNLELMTDFPPAGSRLGIQLDLDYGHPTAGDVLGVSQMDNWTCSTHIYEDSQKILETYHDLPKTQSTKVKPLFESSWWAKLFTQLTQEKRMAEDSGNPQAARDADDHARHFFRSLSAVQELRATPPSSRRLSTQYQGHHGDESKRMAILAWKFRQTRPGEVGTTTWRRLIPAPDRTTTNSPRPVSGVDRPPLSLDSILLNKPSHQGVYQTPQPHDLIHHPSQSHSQWPMYQSPHDNVANLFNTPGHLDFMTSISKAEDGLNDKTAVTSVLDSFSTSLAPESIPSTSLHGPSGAPVMLNVHDLPLSHPGMGYTMGHEASHYVPSQQHSVNMHDSNSVLHGFFGSNTQPLDDLSHGQASWGAHSTSIPGDVGAGSYQLPYQPEHHVPVSRESQQPHHFDGLLPSEDLMDKIVGRMSNGPSIHGAGPDASAGYDNATVDAV | BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (By similarity). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity). Binds to the sequence 5'-CATTCY-3', where Y is a pyrimidine, making both major- and minor-groove contacts (By similarity). localizes to the nuclei of phialides and terminal cells of mature conidia (By similarity). Expression is also positively regulated by stuA (PubMed:21148688). Belongs to the TEC1 family. |
Q5H7P3 | MATERQPECIMSQTQHCLESLGAQSCQEPPNASGDTQQYSNNPAHNDTAGPDDHLQQITCKDRHSPVPNHSQLSIHRYQVKKLRRLQSNGSRLAGPQRGRSYLKLQSFLDYRVQQRRGTCKDGEPVWSDELEDAFHQALEANPPMGRRNWSARGESYGRNELIADYIYRLTGKRRTRTQVSSHLQVLDSFLKGDPDWERLVREQPADHSNSQTQLVGPTRRSPINCLSSSHYSKDSLVCAVQCLGFGMWVSAPNMPDRIDDAFHVYTRLRRGQPQAPMPLEELTNWRTFFPHLNSLLLEVNDPLSCEIILLEARLQLMDVHPPTGSRLEIGLELDITNPTLGAAPMSNQRENWTCYNYIYEEGQKTMETYHNIPKPHTTRIRLPFESSWWAERFTMLTEDKQVAEASGHQHAAKERNQQFFRTLTAVQEIRASEPASLRRLHNQYAGSPSDGSKRMAIILWQFRQTLPIEVGTTICRKLIAAPGRTNEIYLPTPDLDSVRLTPLSSDPIPPSRSTPSMYQSPRTHELLQQHWPLYQPSHHHVTSVFNSAGAFDFTNSITKPEESLSDKTNSASMLDPFPNLQQQTTSQPTSLDVSSGAPRMLQIPDLPLPHTGLGAYGLGHESHLIGPDEPVGSTVGMSGDAGMNGARLETLLEDDLRVTATSQGTVLQDWQQGGSKNSGKKNPRAGDDAHTLEFTQTRAFTDSGYASTKLDNYGHIQSTRDIPTEPPAGPGYASGEQPEVPQTQNFVHVDAARTVYSDTSSVTSLQREGYISELAGDLFTKVSSWQPDSMTMERISEVLPELLRAFALKVGHNAPSQMHRDVMVFIHKNRE | Probable regulator of conidiophore development and conidium maturation (By similarity). Belongs to the TEC1 family. |
P52659 | MDLALLRTFVTVHRAGSFTRAAALLGLSQPAVTSQIRTLERQLGRPLFLRQARGVTPTTIGDELAHRAAPHLDALVEIAESGLDDDSSSRTLYLAGPPEFTTERVLPALTGLTGDDGQGLTLRVSFGTAEETLEGLSCGRHDLAISTTRPRGALLSATPLCDEEHVLVAAPRWAERIGADTVRLKGAPALDDLPVVEVHESLPFVSRYWASVFDCAPAATGTVIVPDLRAVLSCASAGAGLAVLPRYLCARALEQGAVVTLLDPVVPPLRTYFLVVRTGTLALPHVARAHEWLRHAATAWC | Putative regulator that may be involved in stimulating antibiotic production in S.antibioticus. Belongs to the LysR transcriptional regulatory family. |
P15450 | MKVVIFIFALLATICAAFAYVPLPNVPQPGRRPFPTFPGQGPFNPKIKWPQGY | This peptide has bactericidal activity. |
P81463 | FVPYNPPRPGQSKPFPSFPGHGPFNPKIQWPYPLPNPGH | Antibacterial peptide against Gram-positive and Gram-negative bacteria. By bacterial infection. |
P0DPR5 | MTTTLKKVVAASMVGSVAEWYEFFLYGTASALVFGELFFQQTGNAIDGILAAFALYAVGFLARPLGGLVFGHYGDKIGRKKLLQISLIIVGITTFLMGCIPTFHQIGYWAPTLLVILRLIQGFAFGGEWGGAVILVSEHSPDDRRGYWASWPQTGVPLGNLVATLVLLLLSKNLSPEQFLDWGWRCAFWFSAVVVLIGLWIRKNVDDAEVFKEAQAKQQLLEKQQLGIIEVLKYHKKSVIAGIGARFAENILYYMVVTFSISYLKLVVHKDTSQILLLMFGAHLIHFFIIPFMGHLSDIFGRKPIYLIGAVLTAFWGFVGFPLMDTGNDWLIMLAIVLGLFIESMTYSPYSALMTELFPTHIRYTALSFCYQVAPIMAGSLAPLIALTLLKEFNSSIPISLYLVAASLISIVSILLVKETKGRSLAFKD | Efflux pump that mediates resistance to fosfomycin (PubMed:27650185). Probably also involved in the secretion of biofilm matrix that contributes to the pathogenicity (PubMed:27650185). Inhibited by the efflux inhibitor and energy decoupler carbonyl cyanide m-chlorophenylhydrazone (CCCP). Expression is up-regulated on exposure to fosfomycin. Disruption of the gene increases susceptibility to fosfomycin. Disruption also results in impaired biofilm formation and decreased virulence. Belongs to the major facilitator superfamily. |
O65624 | MDISALFLTLFAGSLFLYFLRCLISQRRFGSSKLPLPPGTMGWPYVGETFQLYSQDPNVFFQSKQKRYGSVFKTHVLGCPCVMISSPEAAKFVLVTKSHLFKPTFPASKERMLGKQAIFFHQGDYHAKLRKLVLRAFMPESIRNMVPDIESIAQDSLRSWEGTMINTYQEMKTYTFNVALLSIFGKDEVLYREDLKRCYYILEKGYNSMPVNLPGTLFHKSMKARKELSQILARILSERRQNGSSHNDLLGSFMGDKEELTDEQIADNIIGVIFAARDTTASVMSWILKYLAENPNVLEAVTEEQMAIRKDKEEGESLTWGDTKKMPLTSRVIQETLRVASILSFTFREAVEDVEYEGYLIPKGWKVLPLFRNIHHSADIFSNPGKFDPSRFEVAPKPNTFMPFGNGTHSCPGNELAKLEMSIMIHHLTTKYSWSIVGASDGIQYGPFALPQNGLPIVLARKPEIEV | Involved in the oxidative degradation of abscisic acid. Plays an important role in determining abscisic acid levels in dry seeds and in the control of postgermination growth. 2-cis-(+)-abscisate + O2 + reduced [NADPH--hemoprotein reductase] = (+)-8'-hydroxyabscisate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] Plant hormone degradation; abscisic acid degradation. A number of isoforms are produced. According to EST sequences. Mainly expressed in flowers, siliques, roots and stems. Lower expression in rosette leaves and dry seeds. Expressed in vascular tissues of embryo during the seed development. Expressed predominantly during mid-maturation of seed and down-regulated during late maturation. Up-regulated 12 hours after seed imbibition. By abscisic acid treatment, salt or osmotic stresses, and by dehydration and rehydration. Expression regulated by phytochrome B. Plants show a reduced germination. Belongs to the cytochrome P450 family. |
Q5R9Z5 | MATCAEILRSEFPEIDGQVFDYVTGVLHSGSADFESVDDLVEAVGELLQEVSGDSKDDAGIRAVCQRMYNTLRLAEPQSQGNSQVLLDAPIQLSKITENYDCGTKLPGLLKREQSSTVNAKKLEKAEARLKAKQEKRSEKDTLKTSNPLVLEEASASQAGSRKESRLESSGKNKSYDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLLHVEQEVAEDDTPALQSVLESDSVREDLLRRERELSAHIAAGRVEGSEAAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIAADIIHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIDRFRYNANRASQVQSKLKMLEKLPELKPVDKESEVVMKFPDGFEKFSPPILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLARKFPGRPEEEYRHQLGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVTRVEGGFDQYRALLQEQFRREGFL | Displays an antiviral effect against flaviviruses in the presence of OAS1B. Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily. Lacks transmembrane domains and is probably not involved in transport. |
Q66H39 | MATCADILRSEFPEIDGQVFDYVTGVLHSGSADFESVDDLVEAVGELLQEVSGDSKDDAGIRAVCQRMYNTLRLAEPQNQGNNQVLLDAPIQLSKIMENYDCDTKLPGLLKREQSSTVNAKKLEKAEARLKAKQEKRSEKETLKTSSPLVLEEASASQAGSRKESRLESSGKNKSYDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLLHVEQEVAGDDTPALQSVLESDTIREDLLRQERGLSLKIAAGRAEGSEAALLAEVYTKLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIDRFRYNANRASQVQSKLKMLEKLPELKPVDKESEVVLKFPDGFEKFSPPILQLDEVDFYYDPKHIIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLAPVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLARKFPGRPEEEYRHQLGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGHALNNFRGGVVLVSHDERFIRLVCKELWVCEKGSVTRVEGGFDQYRALLQEQFRREGFL | Displays an antiviral effect against flaviviruses such as west Nile virus (WNV) in the presence of OAS1B. Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily. Lacks transmembrane domains and is probably not involved in transport. |
Q55FQ7 | MGPKGKKKGQSFDDSDEEINNKKGGNKKGQQLEDDIPQPVKKGGNKKGQRGKQDSDDEPENIPQPVAKKSNNKKGQRGKQDSDDEQDEIPQPQKKGGKPAPQPQKKGGKQQDSDDEQDEIPQPVKKGGKPAPQKKGGKQQQQQDSDDEQEEIPQPVKKGGKPAPQKKGGKQQDSDDEEDEIPQPVKKGGKPAPQKKGGKQQESEDEDEEDEVQQPVKKGGKNDKKKGVKHVEEEEEEEEEEEIEQPVKKGGKAPKPKKGGKGSKQESEDEEDDVQQPVKKGGKKDKKKGSKHVEEEEEEEEEEEIEQPVKKGSNKKDQKKGGKGKHVEEEEEEEEEEEIEQPVKKGSNKKDQKKGGKGKQQQESEDEEEEIQQPVKKGGKKDKKKGSKHVEEEEEEEEEEEEIEQPVKKGGKKDKKSSLEDSMSELSIKSKKGGKGKHVEEEEEQEQEEEEEKPKSKSNKKDKKKGKHVEEEEEEEEEEEEKPKSKSNKKDKKKGSKHIEEEEEEEEEEEEEEKEEEEEKKMTLAEIRAAKKVKKVDKKEKKKEKEKKKRDEQEEDAFELAKKKQQEEIDYDNIDIDDVPGKDAPTYVHLKSSEGLRSKIGNDIKFDNLILSVPGRILLNNASLTLAYGQKYGFVGRNGIGKSTLVKKIAMRDEITIAPHLRVLYVEQEVTGDDTTPLDCVLAADEERKWLLDEEKVLTELEKVNPSWQFDPRQKRNYSLRDIYDRLKEIDADKASIRAANILIGLGFTFEEISVKKSRDYSGGWRMRIALARALFCKPEVLLLDEPSNHLDLHACVWLEKYLNQWDRTLLVVSHEASFLNEVVDNIIYIHDQKLDQYRGNYDAFMKQKSVNLRSKEKEKDKQDRKLKKMNEFITKNKNNTQAKQAASRAKKMEKIETIELEREDASLVVDFPQPEHLTPPLLVFKDVCFGYEGRPTMFKKLDIGIDMDSKIALVGMNGVGKSTLMKLMNGDLHETTGYIERSRKMRVARFSQHFVDQLDTTMTPIEYFQSKFNNPPVQQIRNHLGRFGICNSLPLHKITTLSGGQKSRVILAELAWAEPHILLLDEPTNHLDIDAIEALAEGINAFTGGVVLISHNQHLINLIAEQIWVVKKDGTIYLYPGTFMDYKNEISREIDNMVIRS | Belongs to the ABC transporter superfamily. |
Q4WDV4 | MALNSTDNRWSTGEDTPSEAQLPDGEERLDAAPDEKVTAEDIDRRLTNLVRKISAQSRRSHHSFLFGAGENSSLNPQSPSFDARKWARAFYNARYRQDDGHPPRVVGVAFKNLNVFGYGSPVDYQMSVGNALLKVPTMVRQALGGGKQRVDILHDVEGLVLPGEQLCVLGPPGSGCSTFLRTIAGETHGLNVDAASYINYHGISPKQMSTAFRGEAIYTAEVDAHFPMLSVGDTLYFAALARAPQVIPGGLSRQEYAKHLRDVIMAMFGIGHTINTRVGNDFVRGVSGGERKRVTIAEAALGYSPLQCWDNSTRGLDSANAVEFCRTLRTQSDVFGITSCVAIYQAPQAAYDLFDKVLVLYEGWQIYFGAAHEAQAYFEQLGFQCPESQTTADFLTSMCSPAERIVKPGFEHMAPRTPEEFAQRWKESPQRQSLLHAIEKYSTEHPLDGPDLHQFALSRRAEKSHRQREKSPYTLSYRGQVKLCLWREWQRLKNDPSVTLAMLIGNFFEALIIASIFYNLTGDTSSFYYRGALLFMMVLLNAFASVLEILTLYEKRTIVEKQSRYAYYHPSAEALSSFIMSLPYKFVNSSLVNLTLYFMSNLRREPGPFFFFLLISTSMMLAMSMFFRWFASLTKTIDQALAPSSIILLALVLYTGFTIPVSYMRGWASWIRWLNPVSYGFEAVMINEFHGREFPCSSFVPSGPGYEDVSRTQRVCSTVGATSGSDVVSGDVFVRSSYGYVNSHRWRNFGIIIAMTVFLAVCHFVTTELVASKRSKGEVLVFRRGSAHIARAKQGQRDEEQPSASAVPSEKYSEAPTPVEGVETQTSIFHWEDVCYDVKIKNETRRILDHVDGWIKPGTLTALMGVSGAGKTTLLDVLASRTTVGVVTGETLVDGRQRDSSFQRKTGYVQQQDLHLATTTVREALEFSALLRQPPQYSREEKLEYVEKVIDLLHMRDYADAIVGVPGEGLNVERRKRLTIGVELAARPKLLLFLDEPTSGLDSQTSWSICNLMETLTRNGQAILCTIHQPSAMLFQRFDRLLLLAKGGKTVYFGEIGSGARTLMDYFVRNGGPPCPKGANPAEHMLEVIGAAPGAHTDIDWPAVWRNSPEYQQVRQELSRLRQLASQPSSVHSDDPSSYSEFAAPFPAQLGQVGRRVFQQYWRTPSYLYSKAILTVGSSIFIGFSFFKGDNTAQGLQNQVFGVFVFLFVVIQLIFQIIPTFVTQRTLYESRERQSKTYSWQAFVLSNIAVEFAWNTIAAVLCFLAWFYPVGLYRNAEYTDSVHSRSTLVFLIIWATFLFASSFAHLLIAGVESAELASALANIMGIMMYAFCGILAGPHALPGFWIFMYRVNPFTYLVSGLLSASLGDAPMHCAANEFLAFSPPANRTCGEYMEDYMALAGGYLLDSAARGDEQCQYCRVDNTSQYLRNFSIDFATRWRDFGLLWVYVAVNTFGAVFLYWLCRVPKGKKRL | Pleiotropic ABC efflux transporter that shows a strong substrate specificity for the azole class of drugs such as lotrimazole (CLT), fluconazole (FLC), itraconazole (ITC), ketoconazole (KTC), posaconazole (POS), econazole (ECON), metconazole (MET), miconazole (MCZ), prochloraz (PCLZ), and tebuconazole (TEBZ). ATP + fluconazole(in) + H2O = ADP + fluconazole(out) + H(+) + phosphate ATP + H2O + itraconazole(in) = ADP + H(+) + itraconazole(out) + phosphate The efflux inhibitor FK506 impairs the transport activity. Belongs to the ABC transporter superfamily. ABCG family. PDR (TC 3.A.1.205) subfamily. |
D4AYW0 | MAWLALLGLLPLLPAIQPTWQANGYEINSTADSFVTAATPFTLRSARPPECPPCFNCQLPAFKCHQFGKCNKFNGKCDCPPGFGGDDCAEPLCGSLPDGRDRTPRKGSTCQCKDGWSGINCNMCETNDACNAMMPEREGGVCYRHHNGGETVAENYQMCEVTNRKIRDMLKEKKPQVTFSCKKEDKTCNFQFWVDQLESFYCSLDTCKWNMDITENQNLTTYQCDNIKCGCVPDRMLCETTGVSLEPLFGQLTGPAKFTSTSTKGGSNKDGSAFSEPVIDKVISDLFGDKSILLDCYSSECLYKTAVPGYKPPVKVINTPLIAGVIAGCSLFIVGVILLIWYLSRRKAYNQYHALADDSDDEGSKLMADHKPASLQFENISYYINGQQILSGIRGIAKPGQVTAIMGASGAGKTTFLDILARKNKRGVVHGDIYVNGEKFNDSEYKKVVGFVDQEDTMLPTLTVHETILNSALLRLPRDMSDAAKQQRVYEVEKQLGIHHIKDQLIGSEEGKGRGISGGEKKRVSIACELVTSPSILFLDEPTSGLDAFNAFNVIECLVNLAKSYNRTVIFTIHQPRSNIVALFDQLILLGKGKTVFSGPYSSCQSYFDNIGYSCPPGFNIADYLVDLTMHASQSRSTEEPAVNVDSHDNNFRTASSSLRAVKSVASASNASIDNASAVDSAQESLLRPKDKRRSSLKQRQDRQLYTRKRGSGLESPPDPQTDNEDGHVMSLAERAQQWLPLSRQQGQVPPQILQDPDHLPPIASGFVTDLDVLVSYYANSNVANAVRDEISSSVQDALAANGQANSQQASDAVTGQMTGYARVGLIRQFIILSSRTWKNLYRNPMLMLTHYATAILLAVLSGYLFYGLTDDIKGFQNRLGLFFFLLALFGFSTLTSLTVFSSERLLFVRERANGYYSPVTYFTAKVLFDIVPLRLIPPIIMGVIVYPMVGLIPDWPEFSKFILVLVLFNLAAAGICLLIGIVFRDPGVANLIGSLVMLFSLLFAGLLLNHDAIPASALWLQTLSIFHYAFEALIVNEVTFLTLIDHKYGLDIEVPGASILSAFGFNNLALWNDVAGLGVISGVSIIMAYAAMHFLLVEKR | Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. |
Q8T691 | MDSNNNNNNENEAFSGASESSEFRKIVEENENEREFEQSNPSPPEYSNYENKDDGINLETINPNISLDNNNNNNQNNQNNQNNNNNNNNQNNNIINNLNKKNKKRSTFKNRIDFSFKDINHYVQITEKGKKKKISKQILTNINGHIESGTIFAIMGPSGAGKTTLLDILAHRLNINGSGTMYLNGNKSDFNIFKKLCGYVTQSDSLMPSLTVRETLNFYAQLKMPRDVPLKEKLQRVQDIIDEMGLNRCADTLVGTADNKIRGISGGERRRVTISIELLTGPSVILLDEPTSGLDASTSFYVMSALKKLAKSGRTIICTIHQPRSNIYDMFDNLLLLGDGNTIYYGKANKALEYFNANGYHCSEKTNPADFFLDLINTQVEDQADSDDDDYNDEEEEIGGGGGGSGGGAGGIEDIGISISPTMNGSAVDNIKNNELKQQQQQQQQQQQSTDGRARRRIKKLTKEEMVILKKEYPNSEQGLRVNETLDNISKENRTDFKYEKTRGPNFLTQFSLLLGREVTNAKRHPMAFKVNLIQAIFQGLLCGIVYYQLGLGQSSVQSRTGVVAFIIMGVSFPAVMSTIHVFPDVITIFLKDRASGVYDTLPFFLAKSFMDACIAVLLPMVTATIVYWMTNQRVDPFYSAAPFFRFVLMLVLASQTCLSLGVLISSSVPNVQVGTAVAPLIVILFFLFSGFFINLNDVPGWLVWFPYISFFRYMIEAAVINAFKDVHFTCTDSQKIGGVCPVQYGNNVIENMGYDIDHFWRNVWILVLYIIGFRVLTFLVLKLKSRNKFKQE | Belongs to the ABC transporter superfamily. ABCG family. Extended C-terminus. |
Q9BXL4 | MACLMAAFSVGTAMNASSYSAEMTEPKSVCVSVDEVVSSNMEATETDLLNGHLKKVDNNLTEAQRFSSLPRRAAVNIEFRDLSYSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGLPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRGKVCNLVPYLRDLGLNCPTYHNPADFVMEVASGEYGDQNSRLVRAVREGMCDSDHKRDLGGDAEVNPFLWHRPSEEVKQTKRLKGLRKDSSSMEGCHSFSASCLTQFCILFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNSGFLFFSMLFLMFAALMPTVLTFPLEMGVFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVILSIYGLDREDLHCDIDETCHFQKSEAILRELDVENAKLYLDFIVLGIFFISLRLIAYFVLRYKIRAER | Catalyzes the efflux of phospholipids such as sphingomyelin, cholesterol and its oxygenated derivatives like 7beta-hydroxycholesterol and this transport is coupled to hydrolysis of ATP (PubMed:17408620, PubMed:24576892). The lipid efflux is ALB-dependent (PubMed:16702602). Is an active component of the macrophage lipid export complex. Could also be involved in intracellular lipid transport processes. The role in cellular lipid homeostasis may not be limited to macrophages. Prevents cell death by transporting cytotoxic 7beta-hydroxycholesterol (PubMed:17408620). 7beta-hydroxycholesterol(in) + ATP + H2O = 7beta-hydroxycholesterol(out) + ADP + H(+) + phosphate ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) + phosphate an N-(acyl)-sphingosylphosphocholine(in) + ATP + H2O = ADP + an N-(acyl)-sphingosylphosphocholine(out) + H(+) + phosphate a sphingomyelin(in) + ATP + H2O = a sphingomyelin(out) + ADP + H(+) + phosphate The cholesterol efflux is enhanced by APOA1. Homodimer; disulfide-linked (PubMed:16702602). Homooligomer (PubMed:16702602). May form heterodimers with several heterologous partners of the ABCG subfamily. Forms heterodimers with ABCG4 (PubMed:27228027). Interacts with CAV1; this interaction regulates ABCG1-mediated cholesterol efflux (PubMed:24576892). Predominantly localized in the intracellular compartments mainly associated with the endoplasmic reticulum (ER) and Golgi membranes. Additional isoforms seem to exist. Expressed in several tissues. Expressed in macrophages; expression is increased in macrophages from patients with Tangier disease. Strongly induced in monocyte-derived macrophages during cholesterol influx. Conversely, mRNA and protein expression are suppressed by lipid efflux. Induction is mediated by the liver X receptor/retinoid X receptor (LXR/RXR) pathway. Not induced by bacterial lipopolysaccharides (LPS). Repressed by ZNF202. Palmitoylation at Cys-315 seems important for trafficking from the endoplasmic reticulum. Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Database for mutations in ABC proteins |
Q64343 | MACLMAAFSVGTAMNASSYSAAMTEPKSVCVSVDEVVSSNVDEVETDLLNGHLKKVDNNFTEAQRFSSLPRRAAVNIEFKDLSYSVPEGPWWKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGMPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFELFDQLYVLSQGQCVYRGKVSNLVPYLRDLGLNCPTYHNPADFVMEVASGEYGDQNSRLVRAVREGMCDADYKRDLGGDTDVNPFLWHRPAEEDSASMEGCHSFSASCLTQFCILFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNSGFLFFSMLFLMFAALMPTVLTFPLEMSVFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPAYLQWMSYISYVRYGFEGVILSIYGLDREDLHCDIAETCHFQKSEAILRELDVENAKLYLDFIVLGIFFISLRLIAYFVLRYKIRAER | Catalyzes the efflux of phospholipids such as sphingomyelin, cholesterol and its oxygenated derivatives like 7beta-hydroxycholesterol and this transport is coupled to hydrolysis of ATP (PubMed:14668945). The lipid efflux is ALB-dependent. Is an active component of the macrophage lipid export complex. Could also be involved in intracellular lipid transport processes. The role in cellular lipid homeostasis may not be limited to macrophages. Prevents cell death by transporting cytotoxic 7beta-hydroxycholesterol (By similarity). 7beta-hydroxycholesterol(in) + ATP + H2O = 7beta-hydroxycholesterol(out) + ADP + H(+) + phosphate ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) + phosphate an N-(acyl)-sphingosylphosphocholine(in) + ATP + H2O = ADP + an N-(acyl)-sphingosylphosphocholine(out) + H(+) + phosphate a sphingomyelin(in) + ATP + H2O = a sphingomyelin(out) + ADP + H(+) + phosphate The cholesterol efflux is enhanced by APOA1. Homodimer; disulfide-linked. Homooligomer. May form heterodimers with several heterologous partners of the ABCG subfamily. Forms heterodimers with ABCG4. Interacts with CAV1; this interaction regulates ABCG1-mediated cholesterol efflux. Predominantly localized in the intracellular compartments mainly associated with the endoplasmic reticulum (ER) and Golgi membranes. Expressed mainly in brain, thymus, lung, adrenals, spleen and placenta. Little or no expression in liver, kidney, heart, muscle or testes. Strongly induced in macrophage cell line RAW 264.7 during cholesterol influx. Induction is mediated by the liver X receptor/retinoid X receptor (LXR/RXR) pathway. Down-regulated by endotoxins or cytokines (TNF and IL1) in J-774 macrophages. Palmitoylation at Cys-315 seems important for trafficking from the endoplasmic reticulum. Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. |
H9BZ66 | MTNQLPNKVELAEVVPQNGGVFLTWEDLWVTASSVKDGSKAILKGLTGYAMPGELLAIMGPSGSGKSTLLDTIAGRLGSSTRQSGDILINGRRQTLAYGSSAYVTQDDTLLATLTIKEAVYYSAELQLPNSMSKSEKKEIADVTLKGMGLQDAMETRIGGWSGKGISGGQKRRVSICLEILTRPKLLFLDEPTSGLDSAASYYVMKAIASQCQGRTIIASIHQPSVDVFSLFHSLCLLSSGRTVYFGPASAANEFFALSGFPCPTLQNPSDHFLKTINSDFDQDIEEGSTRRKSTEEVIDILIKSYKASDKYNAVQSQVAEICQQEGEMLDKRSHASFITQSLVLTRRSFINMSRDLGYYWLRLAVYVVIAVGLGSLYYDVGFSAASVQARGSMLMFVASFITFMAIGGFPSFVEDMKVFQREKLNGHYGSGSFVIANTLSAMPYLLLVSLIPGAIAYFMTGLQNGFEHFIYFALVLFTCMMIVESLMMIVASMVPNFLMGLIAGAGIQALMLLSGGFFRLPNDLPKPFWKYPLHYVAFHKYAYEGMFKNEFEGLKIHDVNGEDILRNTWQMNMDYSKWIDLVILLGMLVLYRVLFLLVVKAGEIVKPAIRAFMSHSPNQINSAERPLDVFDS | ABC transporter controlling the release of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) (PubMed:22345641, PubMed:28663500). This scent, mostly produced in the evening and night by the petals, attracts the pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta) (PubMed:22345641). Homodimer. Restricted to the petals, with the highest expression in the limb and, to a lesser extent, in petal tubes, probably in both epidermal and mesophyll cell layers. Accumulates during flower development with highest levels in open flowers, and fades out as flowers are senescing. In fragrant cultivars (e.g. cv. Mitchell and cv. V26), increases before the onset of volatile emission at the end of the light period, peaks at night and decreases when volatile emission declines early morning; this precise regulation is tuned by ODO1 binding and activation of its promoter. Disturbed release of volatile organic compounds (VOCs) in flowers, including benzoides and phenylpropanoids, which accumulate to toxic levels in the plasma membrane. Belongs to the ABC transporter superfamily. ABCG family. |
Q4GZT4 | MSSNSYEVSIPMSKKLNGIPETTSKDLQTLTEGAVLSFHNICYRVKVKTGFLLCRKTIEKEILANINGVMKPGLNAILGPTGGGKSSLLDILAARKDPHGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLPTTMTSYEKNERINKVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIAMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFGAIGFRCEPYNNPADFFLDIINGDSSAVVLNREDIGDEANETEEPSKKDTPLIEKLAEFYVNSSFFKETKVELDKFSGDQRRKKLPSYKEVTYATSFCHQLKWISRRSFKNLLGNPQASIAQLIVTVFLGLVIGAIFYDLKNDPAGIQNRAGVLFFLTTNQCFSSVSAVELLVVEKKLFIHEYISGYYRVSSYFFGKLLSDLLPMRMLPSIIFTCITYFLLGLKPKVEAFFIMMLTLMMVAYSASSMALAIAAGQSVVSIATLLMTISFVFMMIFSGLLVNLKTVVPWLSWLQYLSIPRYGYAALQHNEFLGQNFCPGLNVTTNNTCSYAICTGEEFLTNQGIDISPWGLWKNHVALACMIVIFLTIAYLKLLFLKKFS | Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes a wide variety of physiological compounds, dietary toxins and xenobiotics from cells. Involved in porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol to extracellular space, it also functions in the cellular export of heme. Also mediates the efflux of sphingosine-1-P from cells. Acts as a urate exporter functioning in both renal and extrarenal urate excretion (By similarity). In kidney, it also functions as a physiological exporter of the uremic toxin indoxyl sulfate (By similarity). Also involved in the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates (By similarity). Mediates the secretion of the riboflavin and biotin vitamins into milk. Extrudes pheophorbide a, a phototoxic porphyrin catabolite of chlorophyll, reducing its bioavailability (By similarity). Plays an important role in the exclusion of xenobiotics from the brain. It confers to cells a resistance to multiple drugs and other xenobiotics including mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, and the anthracyclines daunorubicin and doxorubicin, through the control of their efflux (By similarity). In placenta, it limits the penetration of drugs from the maternal plasma into the fetus. May play a role in early stem cell self-renewal by blocking differentiation (By similarity). ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2. ATP + H2O + urate(in) = ADP + H(+) + phosphate + urate(out) ATP + H2O + indoxyl sulfate(in) = ADP + H(+) + indoxyl sulfate(out) + phosphate ATP + H2O + sphing-4-enine 1-phosphate(in) = ADP + H(+) + phosphate + sphing-4-enine 1-phosphate(out) ATP + estrone 3-sulfate(in) + H2O = ADP + estrone 3-sulfate(out) + H(+) + phosphate ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP + dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate 4-methylumbelliferone sulfate(in) + ATP + H2O = 4-methylumbelliferone sulfate(out) + ADP + H(+) + phosphate 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D-glucuronate(in) + ATP + H2O = 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D-glucuronate(out) + ADP + H(+) + phosphate 4-methylumbelliferone beta-D-glucuronate(in) + ATP + H2O = 4-methylumbelliferone beta-D-glucuronate(out) + ADP + H(+) + phosphate 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(in) + ATP + H2O = 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(out) + ADP + H(+) + phosphate 17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O = 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) + phosphate ATP + H2O + methotrexate(in) = ADP + H(+) + methotrexate(out) + phosphate ATP + H2O + riboflavin(in) = ADP + H(+) + phosphate + riboflavin(out) ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide a(out) + phosphate Homodimer; disulfide-linked. The minimal functional unit is a homodimer, but the major oligomeric form in plasma membrane is a homotetramer with possibility of higher order oligomerization up to homododecamers. Enriched in membrane lipid rafts. The extracellular loop 3 (ECL3) is involved in binding porphyrins and transfer them to other carriers, probably albumin. N-glycosylated. Glycosylation-deficient ABCG2 is normally expressed and functional. Phosphorylated. Phosphorylation may regulate the localization to the plasma membrane, the homooligomerization and therefore, the activity of the transporter. Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. |
Q8MXM4 | MAPPEIGNDEIPLQEFGQKSFAADNTIGGMQSISYDNSGAPMGLYKEKKGMYVTARNLSMSIGTEKKGDKRNILSDLNFFLKPGSMVLILGSPGCGKTSVMKALANQLHSETVSGSLLFNGKAANKSTHHRDVAYVVQGDHHMAPFTVRETFKFSADLQMSEGTSEEEKNARVDYILKTLDLTRQQDTVVGNEFLRGVSGGQKKRVTIGVEMVKDAGLFLMDEPSTGLDSTTTLELMKHFRELSNVNQVSSLVALLQPGVEVTKLFDFLMIMNAGHMVYFGPMSDAISYFEGLGFKLPKHHNPAEFFQEIVDEPELYFEGEGEPPLRGAEEFANAYKNSAMFQSIVNDLDNTQPDLTFCKDSSHLPKYPTPLSYQIRLASIRAFKMLISSQVAVRMRIIKSIVMGLILGSLFYGLDLNQTDGNNRSGLIFFSLLFIVFSGMGAIAILFEQREVFYIQKDGKYYKTFAFFLSLIFSEIPIALLETVVFCVLVYWMCGLQANAEKFIYFLLMNFVGDLAFQSFFKMVSAFAPNATLASVIAPAALAPFILFSGFMAPKRSIGGWWIWIYWISPIKYAFEGLMSNEHHGLIYSCDDSETIPPRNTPNFELPYPRGSGNSSICQITRGDQFLDQLGMPQNNWFKWIDLLIVFAFGALFSFGMYFFLKNVHVDHRASDPKNDKRSKKASKRSKKIKDSKVDIKENRMVKAQKEIPIGCYMQWKDLVYEVDVKKDGKNQRLRLLNEINGYVKPGMLLALMGPSGAGKSTLLDVLANRKTGGHTKGQILINGQERTKYFTRLSAYVEQFDVLPPTQTVKEAILFSAKTRLPSDMPNEEKIKFVENIIETLNLLKIQNKQIGHGEEGLSLSQRKRVNIGVELASDPQLLFLDEPTSGLDSSAALKVMNLIKKIASSGRSIICTIHQPSTSIFKQFDHLLLLKRGGETVYFGPTGDKSADLLGYFENHGLICDPLKNPADFILDVTDDVIETTLDGKPHQFHPVQQYKESQLNSDLLAKIDAGVMPVGTPVPEFHGVYSSSYQTQFVELGKRSWLAQVRRVQNIRTRLMRSLFLGVVLGTLFVRMEETQENIYNRVSILFFSLMFGGMSGMSSIPIVNMERGVFYREQASGMYSIPIYLFTFIVTDLPWVFLSAIIYTVPMYFISGLRLDPNGAPFFYHSFISFTTYFNFSMLAMVFATVLPTDEIAHALGGVALSISSLFAGFMIPPASIAKGWHWFYQLDPTTYPLAIVMINEFQDLEFHCTSSESVTIPNVLTVNGTYIDVGPICPITNGNQILQRYEMKPEDKYKFLAVIFGYSVFFFICIFIALKFIRHQTK | Required for endocytosis and endosomal pH regulation. Associated with the endosome/lysosome system. Present at low levels in vegetative cells, peaks at roughly 5 hours and decrease by 10 hours. There is another peak of production at 12.5 hours, and a slight increase beginning at 20 hours (at protein level). Cells that have a abcG2-abcG18 disruption have an endocytosis rate roughly 70% that of wild-type (or rtoA disrupted cells). Disruption on abcG2-abcG18-rtoA cells have an endocytosis rate roughly 20% that of wild-type. The exocytosis rates of abcG2-abcG18 and abcG2-abcG18-rtoA disrupted cells are roughly that of wild-type; abcG2-abcG18 endosomes have an unusually high pH, whereas abcG2-abcG18-rtoA endosomes have an almost normal pH. Belongs to the ABC transporter superfamily. ABCG family. PDR (TC 3.A.1.205) subfamily. |
Q9NUS0 | MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS | Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes a wide variety of physiological compounds, dietary toxins and xenobiotics from cells (PubMed:11306452, PubMed:12958161, PubMed:19506252, PubMed:20705604, PubMed:28554189, PubMed:30405239, PubMed:31003562). Involved in porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol to extracellular space, it also functions in the cellular export of heme (PubMed:20705604, PubMed:23189181). Also mediates the efflux of sphingosine-1-P from cells (PubMed:20110355). Acts as a urate exporter functioning in both renal and extrarenal urate excretion (PubMed:19506252, PubMed:20368174, PubMed:22132962, PubMed:31003562). In kidney, it also functions as a physiological exporter of the uremic toxin indoxyl sulfate (By similarity). Also involved in the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates (PubMed:12682043, PubMed:28554189, PubMed:30405239). Mediates the secretion of the riboflavin and biotin vitamins into milk (By similarity). Extrudes pheophorbide a, a phototoxic porphyrin catabolite of chlorophyll, reducing its bioavailability (By similarity). Plays an important role in the exclusion of xenobiotics from the brain (Probable). It confers to cells a resistance to multiple drugs and other xenobiotics including mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, and the anthracyclines daunorubicin and doxorubicin, through the control of their efflux (PubMed:11306452, PubMed:12477054, PubMed:15670731, PubMed:18056989, PubMed:31254042). In placenta, it limits the penetration of drugs from the maternal plasma into the fetus (By similarity). May play a role in early stem cell self-renewal by blocking differentiation (By similarity). ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2. ATP + H2O + urate(in) = ADP + H(+) + phosphate + urate(out) ATP + H2O + indoxyl sulfate(in) = ADP + H(+) + indoxyl sulfate(out) + phosphate ATP + H2O + sphing-4-enine 1-phosphate(in) = ADP + H(+) + phosphate + sphing-4-enine 1-phosphate(out) ATP + estrone 3-sulfate(in) + H2O = ADP + estrone 3-sulfate(out) + H(+) + phosphate ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP + dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate 4-methylumbelliferone sulfate(in) + ATP + H2O = 4-methylumbelliferone sulfate(out) + ADP + H(+) + phosphate 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D-glucuronate(in) + ATP + H2O = 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D-glucuronate(out) + ADP + H(+) + phosphate 4-methylumbelliferone beta-D-glucuronate(in) + ATP + H2O = 4-methylumbelliferone beta-D-glucuronate(out) + ADP + H(+) + phosphate 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(in) + ATP + H2O = 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(out) + ADP + H(+) + phosphate 17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O = 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) + phosphate ATP + H2O + methotrexate(in) = ADP + H(+) + methotrexate(out) + phosphate ATP + H2O + riboflavin(in) = ADP + H(+) + phosphate + riboflavin(out) ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide a(out) + phosphate Specifically inhibited by the fungal toxin fumitremorgin C and Ko143. Homodimer; disulfide-linked (PubMed:15001581, PubMed:17686774, PubMed:18056989, PubMed:28554189). The minimal functional unit is a homodimer, but the major oligomeric form in plasma membrane is a homotetramer with possibility of higher order oligomerization up to homododecamers (PubMed:15001581). Enriched in membrane lipid rafts. Highly expressed in placenta (PubMed:9850061). Low expression in small intestine, liver and colon (PubMed:9861027). Expressed in brain (at protein level) (PubMed:12958161). The extracellular loop 3 (ECL3) is involved in binding porphyrins and transfer them to other carriers, probably albumin. N-glycosylated (PubMed:15807535, PubMed:23189181). Glycosylation-deficient ABCG2 is normally expressed and functional. Phosphorylated. Phosphorylation at Thr-362 by PIM1 is induced by drugs like mitoxantrone and is associated with cells increased drug resistance. It regulates the localization to the plasma membrane, the homooligomerization and therefore, the activity of the transporter. Genetic variations in ABCG2 define the blood group Junior system (JR) [MIM:614490]. Individuals with Jr(a-) blood group lack the Jr(a) antigen on their red blood cells. These individuals may have anti-Jr(a) antibodies in their serum, which can cause transfusion reactions or hemolytic disease of the fetus or newborn. Although the clinical significance of the Jr(a-) blood group has been controversial, severe fatal hemolytic disease of the newborn has been reported. The Jr(a-) phenotype has a higher frequency in individuals of Asian descent, compared to those of European descent. The Jr(a-) phenotype is inherited as an autosomal recessive trait. Genetic variations in ABCG2 influence the variance in serum uric acid concentrations and define the serum uric acid concentration quantitative trait locus 1 (UAQTL1) [MIM:138900]. Excess serum accumulation of uric acid can lead to the development of gout, a common disorder characterized by tissue deposition of monosodium urate crystals as a consequence of hyperuricemia (PubMed:18834626, PubMed:19506252, PubMed:20368174). Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. Was originally proposed to function as a glutathione transporter (PubMed:20332504). However, some evidences suggest it is not the case (PubMed:24312054). Database for mutations in ABC proteins The unwalkable disease - Issue 222 of February 2020 |
Q5MB13 | MSSSNVEVFIPMSQENTNGFPTTTSNDRKAFTEGAVLSFHNICYRVKVKSGFLPGRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGALRPTNFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLPTTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKRDKPLVEKLAEIYVDSSFYKETKAELHQLSGGEKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVILGLVIGAIYFGLNNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFFGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPTADAFFIMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATVNNTCNYATCTGEEYLAKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS | Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes a wide variety of physiological compounds, dietary toxins and xenobiotics from cells. Involved in porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol to extracellular space, it also functions in the cellular export of heme. Also mediates the efflux of sphingosine-1-P from cells. Acts as a urate exporter functioning in both renal and extrarenal urate excretion (By similarity). In kidney, it also functions as a physiological exporter of the uremic toxin indoxyl sulfate (By similarity). Also involved in the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates (By similarity). Mediates the secretion of the riboflavin and biotin vitamins into milk. Extrudes pheophorbide a, a phototoxic porphyrin catabolite of chlorophyll, reducing its bioavailability (By similarity). Plays an important role in the exclusion of xenobiotics from the brain. It confers to cells a resistance to multiple drugs and other xenobiotics including mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, and the anthracyclines daunorubicin and doxorubicin, through the control of their efflux (By similarity). In placenta, it limits the penetration of drugs from the maternal plasma into the fetus. May play a role in early stem cell self-renewal by blocking differentiation (PubMed:15516692). ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2. ATP + H2O + urate(in) = ADP + H(+) + phosphate + urate(out) ATP + H2O + indoxyl sulfate(in) = ADP + H(+) + indoxyl sulfate(out) + phosphate ATP + H2O + sphing-4-enine 1-phosphate(in) = ADP + H(+) + phosphate + sphing-4-enine 1-phosphate(out) ATP + estrone 3-sulfate(in) + H2O = ADP + estrone 3-sulfate(out) + H(+) + phosphate ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP + dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate 4-methylumbelliferone sulfate(in) + ATP + H2O = 4-methylumbelliferone sulfate(out) + ADP + H(+) + phosphate 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D-glucuronate(in) + ATP + H2O = 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D-glucuronate(out) + ADP + H(+) + phosphate 4-methylumbelliferone beta-D-glucuronate(in) + ATP + H2O = 4-methylumbelliferone beta-D-glucuronate(out) + ADP + H(+) + phosphate 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(in) + ATP + H2O = 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(out) + ADP + H(+) + phosphate 17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O = 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) + phosphate ATP + H2O + methotrexate(in) = ADP + H(+) + methotrexate(out) + phosphate ATP + H2O + riboflavin(in) = ADP + H(+) + phosphate + riboflavin(out) ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide a(out) + phosphate Homodimer; disulfide-linked. The minimal functional unit is a homodimer, but the major oligomeric form in plasma membrane is a homotetramer with possibility of higher order oligomerization up to homododecamers. Enriched in membrane lipid rafts. The extracellular loop 3 (ECL3) is involved in binding porphyrins and transfer them to other carriers, probably albumin. N-glycosylated. Glycosylation-deficient ABCG2 is normally expressed and functional. Phosphorylated. Phosphorylation may regulate the localization to the plasma membrane, the homooligomerization and therefore, the activity of the transporter. Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. |
Q9Z1T0 | MSSSNDHVLVPMSQRNNNGLPRTNSRAVRTLAEGDVLSFHHITYRVKVKSGFLVRKTVEKEILSDINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPKGLSGDVLINGAPQPAHFKCCSGYVVQDDVVMGTLTVRENLQFSAALRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGKLVFHGPAQKALEYFASAGYHCEPYNNPADFFLDVINGDSSAVMLNREEQDNEANKTEEPSKGEKPVIENLSEFYINSAIYGETKAELDQLPGAQEKKGTSAFKEPVYVTSFCHQLRWIARRSFKNLLGNPQASVAQLIVTVILGLIIGAIYFDLKYDAAGMQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFFGKVMSDLLPMRFLPSVIFTCVLYFMLGLKKTVDAFFIMMFTLIMVAYTASSMALAIATGQSVVSVATLLMTIAFVFMMLFSGLLVNLRTIGPWLSWLQYFSIPRYGFTALQYNEFLGQEFCPGFNVTDNSTCVNSYAICTGNEYLINQGIELSPWGLWKNHVALACMIIIFLTIAYLKLLFLKKYS | Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes a wide variety of physiological compounds, dietary toxins and xenobiotics from cells (PubMed:10485464, PubMed:12477054, PubMed:12429862, PubMed:17145775, PubMed:30042379). Involved in porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol to extracellular space, it also functions in the cellular export of heme (PubMed:12429862, PubMed:15044468). Also mediates the efflux of sphingosine-1-P from cells (By similarity). Acts as a urate exporter functioning in both renal and extrarenal urate excretion (By similarity). In kidney, it also functions as a physiological exporter of the uremic toxin indoxyl sulfate (PubMed:30042379). Also involved in the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates (By similarity). Mediates the secretion of the riboflavin and biotin vitamins into milk (PubMed:17145775). Extrudes pheophorbide a, a phototoxic porphyrin catabolite of chlorophyll, reducing its bioavailability (PubMed:12429862). Plays an important role in the exclusion of xenobiotics from the brain (PubMed:10485464). It confers to cells a resistance to multiple drugs and other xenobiotics including mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, and the anthracyclines daunorubicin and doxorubicin, through the control of their efflux (PubMed:12477054). In placenta, it limits the penetration of drugs from the maternal plasma into the fetus (PubMed:12429862). May play a role in early stem cell self-renewal by blocking differentiation (Probable). ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2. ATP + H2O + riboflavin(in) = ADP + H(+) + phosphate + riboflavin(out) ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide a(out) + phosphate ATP + H2O + urate(in) = ADP + H(+) + phosphate + urate(out) ATP + H2O + indoxyl sulfate(in) = ADP + H(+) + indoxyl sulfate(out) + phosphate ATP + H2O + sphing-4-enine 1-phosphate(in) = ADP + H(+) + phosphate + sphing-4-enine 1-phosphate(out) ATP + estrone 3-sulfate(in) + H2O = ADP + estrone 3-sulfate(out) + H(+) + phosphate ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP + dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate 4-methylumbelliferone sulfate(in) + ATP + H2O = 4-methylumbelliferone sulfate(out) + ADP + H(+) + phosphate 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D-glucuronate(in) + ATP + H2O = 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D-glucuronate(out) + ADP + H(+) + phosphate 4-methylumbelliferone beta-D-glucuronate(in) + ATP + H2O = 4-methylumbelliferone beta-D-glucuronate(out) + ADP + H(+) + phosphate 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(in) + ATP + H2O = 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(out) + ADP + H(+) + phosphate 17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O = 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) + phosphate ATP + H2O + methotrexate(in) = ADP + H(+) + methotrexate(out) + phosphate Specifically inhibited by the fungal toxin fumitremorgin C and Ko143. Homodimer; disulfide-linked. The minimal functional unit is a homodimer, but the major oligomeric form in plasma membrane is a homotetramer with possibility of higher order oligomerization up to homododecamers. Enriched in membrane lipid rafts. Highly expressed in kidney. Lower expression in liver, colon, heart, spleen, and placenta (PubMed:11036110). Expressed in mammary gland (PubMed:17145775). Expressed in intestinal villi and renal proximal tubules, hepatic bile canalicular membranes, and placental labyrinth cells (at protein level) (PubMed:12429862). Up-regulated upon hypoxia. The extracellular loop 3 (ECL3) is involved in binding porphyrins and transfer them to other carriers, probably albumin. N-glycosylated. Glycosylation-deficient ABCG2 is normally expressed and functional. Phosphorylated. Phosphorylation may regulate the localization to the plasma membrane, the homooligomerization and therefore, the activity of the transporter. Mice lacking Abcg2 are born at the expected Mendelian ratio and do not display overt phenotype (PubMed:12429862). However, under specific housing conditions, they show phototoxic skin lesions induced by pheophorbide a, a porphyrin catabolite of chlorophyll found in their diet, that accumulates in mice plasma (PubMed:12429862). They also accumulate a red substance in their bile and display protoporphyria with an accumulation of protoporphyrin IX (PPIX) in erythrocytes (PubMed:12429862). Mice lacking Abcg2 present decreased elimination of some uremic toxins like indoxyl sulfate leading to their accumulation in plasma (PubMed:30042379). They also show reduced survival rate upon adenine-induced chronic kidney disease (PubMed:30042379). Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. |
Q8MIB3 | MSSNSYQVSIPMSKRNTNGLPGSSSNELKTSAGGAVLSFHDICYRVKVKSGFLFCRKTVEKEILTNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPHGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLPTTMTNHEKNERINMVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIAMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAREALGYFASIGYNCEPYNNPADFFLDVINGDSSAVVLSRADRDEGAQEPEEPPEKDTPLIDKLAAFYTNSSFFKDTKVELDQFSGGRKKKKSSVYKEVTYTTSFCHQLRWISRRSFKNLLGNPQASVAQIIVTIILGLVIGAIFYDLKNDPSGIQNRAGVLFFLTTNQCFSSVSAVELLVVEKKLFIHEYISGYYRVSSYFFGKLLSDLLPMRMLPSIIFTCITYFLLGLKPAVGSFFIMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTISFVFMMIFSGLLVNLKTVVPWLSWLQYFSIPRYGFSALQYNEFLGQNFCPGLNVTTNNTCSFAICTGAEYLENQGISLSAWGLWQNHVALACMMVIFLTIAYLKLLLLKKYS | Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes a wide variety of physiological compounds, dietary toxins and xenobiotics from cells. Involved in porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol to extracellular space, it also functions in the cellular export of heme. Also mediates the efflux of sphingosine-1-P from cells. Acts as a urate exporter functioning in both renal and extrarenal urate excretion (By similarity). In kidney, it also functions as a physiological exporter of the uremic toxin indoxyl sulfate (By similarity). Also involved in the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates (By similarity). Mediates the secretion of the riboflavin and biotin vitamins into milk. Extrudes pheophorbide a, a phototoxic porphyrin catabolite of chlorophyll, reducing its bioavailability (By similarity). Plays an important role in the exclusion of xenobiotics from the brain (PubMed:12054514). It confers to cells a resistance to multiple drugs and other xenobiotics including mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, and the anthracyclines daunorubicin and doxorubicin, through the control of their efflux (By similarity). In placenta, it limits the penetration of drugs from the maternal plasma into the fetus. May play a role in early stem cell self-renewal by blocking differentiation (By similarity). ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2. ATP + H2O + urate(in) = ADP + H(+) + phosphate + urate(out) ATP + H2O + indoxyl sulfate(in) = ADP + H(+) + indoxyl sulfate(out) + phosphate ATP + H2O + sphing-4-enine 1-phosphate(in) = ADP + H(+) + phosphate + sphing-4-enine 1-phosphate(out) ATP + estrone 3-sulfate(in) + H2O = ADP + estrone 3-sulfate(out) + H(+) + phosphate ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP + dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate 4-methylumbelliferone sulfate(in) + ATP + H2O = 4-methylumbelliferone sulfate(out) + ADP + H(+) + phosphate 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D-glucuronate(in) + ATP + H2O = 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D-glucuronate(out) + ADP + H(+) + phosphate 4-methylumbelliferone beta-D-glucuronate(in) + ATP + H2O = 4-methylumbelliferone beta-D-glucuronate(out) + ADP + H(+) + phosphate 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(in) + ATP + H2O = 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(out) + ADP + H(+) + phosphate 17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O = 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) + phosphate ATP + H2O + methotrexate(in) = ADP + H(+) + methotrexate(out) + phosphate ATP + H2O + riboflavin(in) = ADP + H(+) + phosphate + riboflavin(out) ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide a(out) + phosphate Homodimer; disulfide-linked. The minimal functional unit is a homodimer, but the major oligomeric form in plasma membrane is a homotetramer with possibility of higher order oligomerization up to homododecamers. Enriched in membrane lipid rafts. High expression in brain, kidney and lung. Also expressed in livere, colon, small intestine, heart, skeletal muscle, spleen, stomach and pancreas. The extracellular loop 3 (ECL3) is involved in binding porphyrins and transfer them to other carriers, probably albumin. N-glycosylated. Glycosylation-deficient ABCG2 is normally expressed and functional. Phosphorylated. Phosphorylation may regulate the localization to the plasma membrane, the homooligomerization and therefore, the activity of the transporter. Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. |
Q80XF3 | MSSSNDHVLVPMSQRNKNGLPGMSSRGARTLAEGDVLSFHHITYRVKVKSGFLVRKTAEKEILSDINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPRGLSGDVLINGAPQPANFKCSSGYVVQDDVVMGTLTVRENLQFSAALRLPKAMKTHEKNERINTIIKELGLDKVADSKVGTQFTRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGKLMFHGPAQKALEYFASAGYHCEPYNNPADFFLDVINGDSSAVMLNRGEQDHEANKTEEPSKREKPIIENLAEFYINSTIYGETKAELDQLPVAQKKKGSSAFREPVYVTSFCHQLRWIARRSFKNLLGNPQASVAQLIVTVILGLIIGALYFGLKNDPTGMQNRAGVFFFLTTNQCFTSVSAVELFVVEKKLFIHEYISGYYRVSSYFFGKLVSDLLPMRFLPSVIYTCILYFMLGLKRTVEAFFIMMFTLIMVAYTASSMALAIAAGQSVVSVATLLMTISFVFMMLFSGLLVNLRTIGPWLSWLQYFSIPRYGFTALQHNEFLGQEFCPGLNVTMNSTCVNSYTICTGNDYLINQGIDLSPWGLWRNHVALACMIIIFLTIAYLKLLFLKKYS | Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes a wide variety of physiological compounds, dietary toxins and xenobiotics from cells. Involved in porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol to extracellular space, it also functions in the cellular export of heme. Also mediates the efflux of sphingosine-1-P from cells. Acts as a urate exporter functioning in both renal and extrarenal urate excretion (By similarity). In kidney, it also functions as a physiological exporter of the uremic toxin indoxyl sulfate (By similarity). Also involved in the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates (By similarity). Mediates the secretion of the riboflavin and biotin vitamins into milk. Extrudes pheophorbide a, a phototoxic porphyrin catabolite of chlorophyll, reducing its bioavailability (By similarity). Plays an important role in the exclusion of xenobiotics from the brain. It confers to cells a resistance to multiple drugs and other xenobiotics including mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, and the anthracyclines daunorubicin and doxorubicin, through the control of their efflux (By similarity). In placenta, it limits the penetration of drugs from the maternal plasma into the fetus. May play a role in early stem cell self-renewal by blocking differentiation (By similarity). ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2. ATP + H2O + urate(in) = ADP + H(+) + phosphate + urate(out) ATP + H2O + indoxyl sulfate(in) = ADP + H(+) + indoxyl sulfate(out) + phosphate ATP + H2O + sphing-4-enine 1-phosphate(in) = ADP + H(+) + phosphate + sphing-4-enine 1-phosphate(out) ATP + estrone 3-sulfate(in) + H2O = ADP + estrone 3-sulfate(out) + H(+) + phosphate ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP + dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate 4-methylumbelliferone sulfate(in) + ATP + H2O = 4-methylumbelliferone sulfate(out) + ADP + H(+) + phosphate 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D-glucuronate(in) + ATP + H2O = 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D-glucuronate(out) + ADP + H(+) + phosphate 4-methylumbelliferone beta-D-glucuronate(in) + ATP + H2O = 4-methylumbelliferone beta-D-glucuronate(out) + ADP + H(+) + phosphate 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(in) + ATP + H2O = 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(out) + ADP + H(+) + phosphate 17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O = 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) + phosphate ATP + H2O + methotrexate(in) = ADP + H(+) + methotrexate(out) + phosphate ATP + H2O + riboflavin(in) = ADP + H(+) + phosphate + riboflavin(out) ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide a(out) + phosphate Homodimer; disulfide-linked. The minimal functional unit is a homodimer, but the major oligomeric form in plasma membrane is a homotetramer with possibility of higher order oligomerization up to homododecamers. Highly expressed in brain capillary, kidney and small intestine. Lower expression in heart. Preferentially expressed (at protein level) on the luminal membrane of brain capillaries, in kidney and small intestine. Down-regulated upon ischemia-reperfusion. The extracellular loop 3 (ECL3) is involved in binding porphyrins and transfer them to other carriers, probably albumin. N-glycosylated in brain capillary, kidney and small intestine but not in heart. N-glycosylated. Glycosylation-deficient ABCG2 is normally expressed and functional. Phosphorylated. Phosphorylation may regulate the localization to the plasma membrane, the homooligomerization and therefore, the activity of the transporter. Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. |
Q54KC2 | MEDKNNIELQEKAPDNYNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNDINNNDDDNNKIIYQNPTPASSSHIDSIEIDINYDLSNHIKQRVTQNKTGMFVSANNISYYIPKSIKKGESEELSKLYLLNNISFTMKPGRMILLMGIPGAGKSLLLKVLGNRLGKGKIEGELKFNNHEVDETTHQRDTIFVSQDDRHIALLTVRETLEFSAKCNMGENVSQEEQSERVDLVLDQLGLSHTSNTIIGNQFFRGISGGQKRRVTIANEFTKRSPNLILMDEPSTGLDSATSYNVISKVKTIAKEAKASVMVSLLQPSVELTNLFDDILILGEGGNLIYFGELNNLLPYFSSIGLAPLPNQPLAEFMQEVSVEPSKYMITDKIELSSKDGGDDESKSLLLGGADSGNVEKMDLVKLFKESELNQKTIQSMQQLIPSDIKVSDHLIKKLETGDNGKSSVRYELKHLLARHIKVMKIMKMQYAVRFFQAIFMGCVIGSLFVKMGFTQADARNRFGLVYFAMVLHIWTTIGSVEEFFTLRGIFDDQKDSKYYRNFPYFLSLVITKIPISLIEAILFSSCCYWIAGFQARVDNFIVFILGMALTNLIAQGIFQVTSAFTSAQLLASLICPAIVVLFMIMSGYMISRLQIPGWWIWLNALSPLRYVIDMVSSNELYGLEFHCSPMEKIPPSNYPLLNVSYADGGYQGNQICQYSTGSDFLNQFGFSDNSYMRWVDIVIILGFVCTFFFIFFLGVKYIRFENKKPPRQIKLKKKKEKKDKKDKEVKHKWNGCYMTFQNLNYVVPSVKDNKETGKKEKVTLELLKDVNGFIVPGMCALMGPSGAGKSTLMDVLAKRKNVGTITGDIRINGQLVKDMNITRFTGYVEQQDILSANLTVREAIEFSANCRLPSSYLQKDRVKLIDEILSVLSLTKMQNTTIGPNPTLGISLANRKKVSIGIELASDPHLIFLDEPTSGLDSSAALKVMNCVKKIAESGRTVVCTIHQPSQEIFEKFDQLLLLDKGKVIYFGDTGDNSSTVIQHFTSAGYQYEHGRNPADFILEIAEHPPSTGQSASDYFKSSIHYSNSIQRLESKTIVPEGVDVPKYKGKYSAPATAQLHSLVKRGWLNHVRRPQTILLRFLRSFIPAIVIGTLFLRLDNDQTGARNRIALVFLGFLFGGMASIGKVPTIVEDRSVYYRESSAGTYPAHLYILASVITDLPMMVLTAFSYWIPMFFLTGLTLGDHGWKFFFSLSVYLLVIMCYDSLATLFALTLPTIPIAILVSGVGLNFLGLFGGFFIPVNNIPRGWIWMHYLVFSKYGLETLSITELKGEPFFCEEDQYSIIPIAGTNFTKKYCAIQSGDTMLLQYGMNDAYDRQFYNLIILGGYFCAYTFLGYLALRFINHMKR | Belongs to the ABC transporter superfamily. ABCG family. PDR (TC 3.A.1.205) subfamily. |
Q8BKI5 | MASNNDPTVISMIERHLCDLPETNTSDLKTLTEEAVLSFHNISYQETVQSGFPLRKKAYVIERLSNISGIMKPGLNAIMGPQDGSRSLLLDVLAARRDPRGLSGDILINGKPRPANFKCTSGYVPQNDVVLGTVTVRDNLEFSAALRLPVTITRDEKRRRINEVLELLHLNKEQNIKPRSKELRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVILVLRRMSKKGRTIIFSINQPQYSIFKFFDSLTLVASGKVMFHGPAQDALEYFRSAGYNYESHNNPADFFLDVINGGFSNILDTEEDGHEDDKYEELFERQYQVTGKLANMYAQSPLYSETRAILDQLLGEQKLERSSAVETTCVTPFCHQLKWIICQSFKNFKGFPWVTVIQAIITVILATAVGTAFRVLKNDCIEVQMRAGLLYLLTIFQCITSVSAGELFVIDRVRFLHEHTSGYYRVSSYFFGKLLAELIPRRLLPSTVFSLITYVIAGVKMSMKCFFTMICTIMVLAYSASSLPLSIGAGENAVAVPTLLVTIYFVFMLFFSGLSLYSGSFLPKLSWIQYFSIPHYGFRALLHNEFLGQNFCPEHNTEEVSRCHNYVICTGEEFLMIQGIDLSSWGFWENHLALVCTMIILLTITYVQLLQVKNIRNF | May dimerize with another subunit to form a functional transporter. Highest levels of expression in thymus and spleen. Detected in lung and small intestine. Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. Seems to have a defective ATP-binding region. |
Q54H75 | MEDIGNNNFEIIDDKSDEKNDENFEDKNSRNNINEEQILSNQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQEQQQFKNEVINTLHPKQPNNEYSLSSLSLSPQTPQINLSEKLISDNSNLNSNSNNNNKDIESGIQTKIKNIENRRNSINSDSSGTFNNEITNGRSNDNEIININNNVGVQVTFENICYKVLNKKYNEQKKIIKKLESGKIDIEDIESQVNKLPIDRIIEKELTILSNVSGIVEKGEMVALMGPSGSGKSTLLDILANRKSTGTITGKILVNGKEIGEAYKMFCSYVTQEEVFLETSTVYETLKFHADLRLPDMTDTEKDIRIKQVLKDVGLDRKLNSKIGGILPGGMIVKGLSGGEKKRVSIGCALVTNPSLLFLDEPTSGLDSLNSLKVMKVLLELTKMKGVTVVCSVHQPRPEIFYLFSNIMVVLKGRMVYSGSNILEYLSSIDSNYKCPPQMNPADFILDVCDEIVNNPSQYSTTVDTWEKYWKHEIQPTISNDPINIDIPKRVGFIYQYWVCQKRSYQSFVRNRVVFFSKIVIAILIGLLFSACFGTVGYDGLDQNEAQSVSALFFFIITSLNLLPYSSISTFVSIRTLFNSERASKIYHPFPYFIGSMLIEIVSSFFVVLIITTIIYCIVHLRWSFEAYILSLISFYMVFLASVFMVIAMSNIAGTVDLTFSYCTGVSVVLVLFSGFLVPINSLPDSFGWIHHIDYLFYGFSSIVIIQYRDFEFQCPQPPIPCLYSNGNNLIEFLGLKNWEYNKSIGILTIWIAFFYILAYIGLYKFNKEKR | Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. |
Q8WWH2 | MAEKALEAVGCGLGPGAVAMAVTLEDGAEPPVLTTHLKKVENHITEAQRFSHLPKRSAVDIEFVELSYSVREGPCWRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGRPRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVASGEYGDLNPMLFRAVQNGLCAMAEKKSSPEKNEVPAPCPPCPPEVDPIESHTFATSTLTQFCILFKRTFLSILRDTVLTHLRFMSHVVIGVLIGLLYLHIGDDASKVFNNTGCLFFSMLFLMFAALMPTVLTFPLEMAVFMREHLNYWYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSALATATALVAQSLGLLIGAASNSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGVILTIYGMERGDLTCLEERCPFREPQSILRALDVEDAKLYMDFLVLGIFFLALRLLAYLVLRYRVKSER | ATP-dependent transporter of the ATP-binding cassette (ABC) family that may be involved in the cellular efflux of sterols, in particular cholesterol and desmosterol (a cholesterol precursor), to high-density lipoprotein (HDL) (PubMed:15240127, PubMed:33141061). May play an important role in the removal of amyloid-beta peptides from brain, in a process that can be antagonized by desmosterol. However it is unclear whether ABCG4 can directly transport amyloid-beta peptides or whether peptide export may be facilitated due to changes in the membrane lipid environment (By similarity). Induces apoptosis in various cells (PubMed:27228027). ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) + phosphate ATP + desmosterol(in) + H2O = ADP + desmosterol(out) + H(+) + phosphate Half-transporter that forms a functional transporter via homo- or heterodimerization. Homodimer (PubMed:27228027). Heterodimers with ABCG1 (Probable) (PubMed:27228027). Expressed specifically in the brain and the eye. Protein expression is stabilized by cellular cholesterol status and cholesterol synthesis intermediates desmosterol, lathosterol and lanosterol. Whether ABCG4 is an LXR target gene, is still under debate. Studies performed in monocytes, and in one astrocyte cell line indicated that ABCG4 expression could be up-regulated by oxysterols and other LXR ligands (PubMed:11606068, PubMed:33141061). However, subsequent observations in a number of different cell types (primary mouse cells, oligodendrocytes and neuron-like cell lines) have not confirmed this observation (By similarity) (PubMed:33141061). Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. Database for mutations in ABC proteins |
Q3UNF7 | MQRLAMDLRVLSRELALYLEHQVRVGFFGSGVGLSLILGFSVAYACYYLSSIAKKPQLVIGGESFSRFLQDHCPVVTETYYPTVWCWESRGQTLLRPFITSKPPVQYRNELIKTADGGQISLDWFDNNNSAYYVDASTRPTILLLPGLTGTSKESYILHMIHLSEELGYRCVVFNNRGVAGESLLTPRTYCCANTEDLEAVVHHVHSLYPGAPFLAAGVSMGGMLLLNYLGKIGSKTPLMAAATFSVGWNTFACSESLERPLNWLLFNYYLTTCLQSSVKKHRHMFVEQIDMDQVMKAKSIREFDKRFTAVMFGYRTLDDYYTDASPNRRLKSVGIPVLCLNATDDVFSPSHAIPIETAKQNPNVALVLTAYGGHIGFLEGIWPRQCTYMDRVFKQFVQAMVEHGHELSNM | Phospholipase that may play a role in phospholipids remodeling. May selectively cleave myristate (C14)-containing phosphatidylcholines through its predominant phospholipase 1 activity, cleaving preferentially acyl groups in sn1 position. In parallel, may have a minor phospholipase 2 activity acting on acyl groups in position sn2. In addition to (C14)-containing phosphatidylcholines, may also act on other medium-chain-containing and oxidatively truncated phospholipids. a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+) a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+) 1-tetradecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H(+) + tetradecanoate 1-tetradecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-tetradecanoyl-sn-glycero-3-phosphocholine + H(+) 1-tetradecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate 1-tetradecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine + H(+) + tetradecanoate 1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 2-tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate 1-octadecanoyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-octadecanoyl-sn-glycero-3-phosphocholine + acetate + H(+) 1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate 1-octadecanoyl-2-pentanoyl-sn-glycero-3-phosphocholine + H2O = 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + pentanoate 1-octadecanoyl-2-hexanoyl-sn-glycero-3-phosphocholine + H2O = 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexanoate 1-octadecanoyl-2-octanoyl-sn-glycero-3-phosphocholine + H2O = 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + octanoate 1-octadecanoyl-2-nonanoyl-sn-glycero-3-phosphocholine + H2O = 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + nonanoate 1-O-hexadecyl-2-nonadioyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + nonanedioate 1-hexadecanoyl-2-nonadioyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + nonanedioate 1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + 9-oxononanoate + H(+) 1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + 5-oxopentanoate + H(+) 1-hexadecanoyl-2-glutaroyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + glutarate + H(+) 1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+) Widely expressed with higher expression in liver. Detected in embryos from 7 dpc to 17 dpc. Mice lacking Abhd3 are viable, fertile and have normal behavior. Belongs to the AB hydrolase superfamily. AB hydrolase 4 family. |
Q24K17 | MADDLEQQPQGWLSSWLPTWRPTSMSQLKNVEARILQCLQNKFLARYVSLPNQNKIWTVTVSPELRDRTPLVMVHGFGGGVGLWILNMDSLSTRRTLHTFDLLGFGRSSRPTFPRDPEGAEDEFVTSIETWRESMGIPSMILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLRPADPSQVRAPPTWVKAVASVLGRSNPLAVLRVAGPWGPGLVQRFRPDFKRKFADFFDDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRKDVPITMIYGANTWIDTSTGKKVKLQRPDSYVRDLEIEGASHHVYADQPHIFNAVVEEICDSVD | Lysophospholipase selective for N-acyl phosphatidylethanolamine (NAPE). Contributes to the biosynthesis of N-acyl ethanolamines, including the endocannabinoid anandamide by hydrolyzing the sn-1 and sn-2 acyl chains from N-acyl phosphatidylethanolamine (NAPE) generating glycerophospho-N-acyl ethanolamine (GP-NAE), an intermediate for N-acyl ethanolamine biosynthesis. Hydrolyzes substrates bearing saturated, monounsaturated, polyunsaturated N-acyl chains. Shows no significant activity towards other lysophospholipids, including lysophosphatidylcholine, lysophosphatidylethanolamine and lysophosphatidylserine. H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine H2O + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine = a fatty acid + H(+) + N,1-diacyl-sn-glycero-3-phosphoethanolamine H2O + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-sn-glycero-3-phosphoethanolamine H2O + N-octadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-octadecanoyl-sn-glycero-3-phospho-ethanolamine H2O + N-eicosanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-eicosanoyl-sn-glycero-3-phosphoethanolamine H2O + N,1-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(N-hexadecanoyl)-serine + H2O = (9Z)-octadecenoate + 1-octadecanoyl-2-hydroxy-sn-glycero-3-phospho-(N-hexadecanoyl)-serine + H(+) 1-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + H2O = (9Z)-octadecenoate + 1-O-(1Z-octadecenyl)-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + H(+) H2O + N,1-diacyl-sn-glycero-3-phosphoethanolamine = a fatty acid + H(+) + N-acyl-sn-glycero-3-phosphoethanolamine Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily. Thr-291 is present instead of the conserved His which is expected to be an active site residue. |
Q9H9E0 | MADDLEQQSQGWLSSWLPTWRPTSMSQLKNVEARILQCLQNKFLARYVSLPNQNKIWTVTVSPEQNDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEGAEDEFVTSIETWRETMGIPSMILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLRPTNPSEIRAPPAWVKAVASVLGRSNPLAVLRVAGPWGPGLVQRFRPDFKRKFADFFEDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRKDVPITMIYGSDTWIDTSTGKKVKMQRPDSYVRDMEIKGASHHVYADQPHIFNAVVEEICDSVD | Lysophospholipase selective for N-acyl phosphatidylethanolamine (NAPE). Contributes to the biosynthesis of N-acyl ethanolamines, including the endocannabinoid anandamide by hydrolyzing the sn-1 and sn-2 acyl chains from N-acyl phosphatidylethanolamine (NAPE) generating glycerophospho-N-acyl ethanolamine (GP-NAE), an intermediate for N-acyl ethanolamine biosynthesis. Hydrolyzes substrates bearing saturated, monounsaturated, polyunsaturated N-acyl chains. Shows no significant activity towards other lysophospholipids, including lysophosphatidylcholine, lysophosphatidylethanolamine and lysophosphatidylserine. H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine H2O + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine = a fatty acid + H(+) + N,1-diacyl-sn-glycero-3-phosphoethanolamine H2O + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-sn-glycero-3-phosphoethanolamine H2O + N-octadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-octadecanoyl-sn-glycero-3-phospho-ethanolamine H2O + N-eicosanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-eicosanoyl-sn-glycero-3-phosphoethanolamine H2O + N,1-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(N-hexadecanoyl)-serine + H2O = (9Z)-octadecenoate + 1-octadecanoyl-2-hydroxy-sn-glycero-3-phospho-(N-hexadecanoyl)-serine + H(+) 1-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + H2O = (9Z)-octadecenoate + 1-O-(1Z-octadecenyl)-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + H(+) H2O + N,1-diacyl-sn-glycero-3-phosphoethanolamine = a fatty acid + H(+) + N-acyl-sn-glycero-3-phosphoethanolamine Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily. Thr-291 is present instead of the conserved His which is expected to be an active site residue. |
Q8VD66 | MADDLEQQPQGWLSSWLPTWRPTSMSQLKNVEARILQCLQNKFLARYVSLPNQNKIWTVTVSPEQKDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPTFPRDPEGAEDEFVASIETWRETMGIPTMILLGHSLGGFLATSYSIKYPERVKHLILVDPWGFPLRPTDPSEIRAPPTWVKAVASVLGRSNPLAVLRVAGPWGPGLVQRFRPDFKRKFADFFEDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRKDVPITMIYGANTWIDTSTGKKVKMQRPDSYVRDMEIEGASHHVYADQPHIFNAVVEEICNSVD | Lysophospholipase selective for N-acyl phosphatidylethanolamine (NAPE). Contributes to the biosynthesis of N-acyl ethanolamines, including the endocannabinoid anandamide by hydrolyzing the sn-1 and sn-2 acyl chains from N-acyl phosphatidylethanolamine (NAPE) generating glycerophospho-N-acyl ethanolamine (GP-NAE), an intermediate for N-acyl ethanolamine biosynthesis (PubMed:16818490, PubMed:25853435). Hydrolyzes substrates bearing saturated, monounsaturated, polyunsaturated N-acyl chains (PubMed:16818490, PubMed:25853435). Shows no significant activity towards other lysophospholipids, including lysophosphatidylcholine, lysophosphatidylethanolamine and lysophosphatidylserine (PubMed:16818490). H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine H2O + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine = a fatty acid + H(+) + N,1-diacyl-sn-glycero-3-phosphoethanolamine H2O + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-sn-glycero-3-phosphoethanolamine H2O + N-octadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-octadecanoyl-sn-glycero-3-phospho-ethanolamine H2O + N-eicosanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-eicosanoyl-sn-glycero-3-phosphoethanolamine H2O + N,1-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(N-hexadecanoyl)-serine + H2O = (9Z)-octadecenoate + 1-octadecanoyl-2-hydroxy-sn-glycero-3-phospho-(N-hexadecanoyl)-serine + H(+) 1-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + H2O = (9Z)-octadecenoate + 1-O-(1Z-octadecenyl)-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + H(+) H2O + N,1-diacyl-sn-glycero-3-phosphoethanolamine = a fatty acid + H(+) + N-acyl-sn-glycero-3-phosphoethanolamine Highest levels in the CNS and in testis, intermediate levels in liver and kidney. Hardly detectable in heart. Homozygous knockout ABHD4 mice are born at the expected Mendelian frequency, are viable and healthy, and show no overt differences in their cage behavior compared to that of wild-type littermates. Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily. Thr-291 is present instead of the conserved His which is expected to be an active site residue. |
Q9Y369 | MAAEEEEVDSADTGERSGWLTGWLPTWCPTSISHLKEAEEKMLKCVPCTYKKEPVRISNGNKIWTLKFSHNISNKTPLVLLHGFGGGLGLWALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWGFPERPDLADQDRPIPVWIRALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGKMHPDIPVSVIFGARSCIDGNSGTSIQSLRPHSYVKTIAILGAGHYVYADQPEEFNQKVKEICDTVD | Coenzyme A-dependent lysophosphatidic acid acyltransferase that catalyzes the transfert of an acyl group on a lysophosphatidic acid (PubMed:18606822). Functions preferentially with 1-oleoyl-lysophosphatidic acid followed by 1-palmitoyl-lysophosphatidic acid, 1-stearoyl-lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid as lipid acceptor. Functions preferentially with arachidonoyl-CoA followed by oleoyl-CoA as acyl group donors (By similarity). Functions in phosphatidic acid biosynthesis (PubMed:18606822). May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2 (PubMed:16679289). Involved in keratinocyte differentiation (PubMed:18832586). Regulates lipid droplet fusion (By similarity). a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + CoA 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + eicosanoyl-CoA = 1-(9Z)-octadecenoyl-2-eicosanoyl-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA Acyltransferase activity is inhibited by detergents such as Triton X-100 and 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS). Acyltransferase activity is inhibited by the presence of magnesium and calcium. Interacts with ADRP, PLIN and PNPLA2. Interacts with PLIN5; promotes interaction with PNPLA2 (By similarity). Colocalized with PLIN and ADRP on the surface of lipid droplets. The localization is dependent upon the metabolic status of the adipocytes and the activity of PKA (By similarity). Widely expressed in various tissues, including lymphocytes, liver, skeletal muscle and brain. Expressed by upper epidermal layers and dermal fibroblasts in skin, hepatocytes and neurons (at protein level). Detected in fetal epidermis from 49 to 135 days estimated gestational age (at protein level). Up-regulated upon keratinocyte differentiation (at protein level). The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. The disease is caused by variants affecting the gene represented in this entry. Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily. |
Q9CTY3 | MKAMAAEEEVDSADAGGGSGWLTGWLPTWCPTSTSHLKEAEEKMLKCVPCTYKKEPVRISNGNRIWTLMFSHNISSKTPLVLLHGFGGGLGLWALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPWGFPERPDLADQERPIPVWIRALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGGLHPDIPVSVIFGARSCIDGNSGTSIQSLRPKSYVKTIAILGAGHYVYADQPEEFNQKVKEICHTVD | Coenzyme A-dependent lysophosphatidic acid acyltransferase that catalyzes the transfert of an acyl group on a lysophosphatidic acid (PubMed:19801371). Functions preferentially with 1-oleoyl-lysophosphatidic acid followed by 1-palmitoyl-lysophosphatidic acid, 1-stearoyl-lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid as lipid acceptor (PubMed:19801371). Functions preferentially with arachidonoyl-CoA followed by oleoyl-CoA as acyl group donors (PubMed:19801371). Functions in phosphatidic acid biosynthesis (By similarity). May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2 (PubMed:16679289). Involved in keratinocyte differentiation (By similarity). Regulates lipid droplet fusion (PubMed:26083785). a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + CoA 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + eicosanoyl-CoA = 1-(9Z)-octadecenoyl-2-eicosanoyl-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA Acyltransferase activity is inhibited by detergents such as Triton X-100 and 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS). Acyltransferase activity is inhibited by the presence of magnesium and calcium. Optimum pH is 7-8.5. Preincubation of the enzyme for 10 min at temperatures above 35 degrees Celsius decreases acyltransferase activity subsequently measured at 30 degrees Celsius. Acyltransferase activity is reduced by approximately 60% following 10 min preincubation at47 degrees Celsius. Interacts with ADRP (By similarity). Interacts with PLIN. Interacts with and PNPLA2. Interacts with PLIN5; promotes interaction with PNPLA2. Colocalized with PLIN and ADRP on the surface of lipid droplets. The localization is dependent upon the metabolic status of the adipocytes and the activity of PKA. Highly expressed in the adipose tissue and testes. Weakly expressed in the liver, muscle, kidney, and heart. Expressed by upper epidermal layers and dermal fibroblasts in skin, hepatocytes and hypothalamus in brain (at protein level). The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily. |
Q5EE05 | MAAEEEEMDSTDACERSGWLTGWLPTWCPTSTSHLKEAEEKILKCVPCIYKKGPVRISNGNKIWTLKLSHNISNKIPLVLLHGFGGGLGLWALNFGDLCTNRPVYAFDLLGFGRSSRPRFDTDAEEVENQFVESIEEWRCALGLDKVILLGHNLGGFLAAAYSLKYPSRVSHLILVEPWGFPERPDLADQERPIPVWIRALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLHRIGKMNPDIPVSVIYGARSCIDGNSGTSIQSLRPHSYVKTIAILGAGHYVYADQPEDFNLKVKEICDTVD | Coenzyme A-dependent lysophosphatidic acid acyltransferase that catalyzes the transfert of an acyl group on a lysophosphatidic acid. Functions preferentially with 1-oleoyl-lysophosphatidic acid followed by 1-palmitoyl-lysophosphatidic acid, 1-stearoyl-lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid as lipid acceptor. Functions preferentially with arachidonoyl-CoA followed by oleoyl-CoA as acyl group donors (By similarity). Functions in phosphatidic acid biosynthesis (By similarity). May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2 (By similarity). Involved in keratinocyte differentiation (By similarity). Regulates lipid droplet fusion (By similarity). a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + CoA 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + eicosanoyl-CoA = 1-(9Z)-octadecenoyl-2-eicosanoyl-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA Acyltransferase activity is inhibited by detergents such as Triton X-100 and 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS). Acyltransferase activity is inhibited by the presence of magnesium and calcium. Interacts with ADRP, PLIN and PNPLA2. Interacts with PLIN5; promotes interaction with PNPLA2 (By similarity). Colocalized with PLIN and ADRP on the surface of lipid droplets. The localization is dependent upon the metabolic status of the adipocytes and the activity of PKA (By similarity). The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily. |
Q5RBI4 | MAAEEEEVDSADTGERSGWLTGWLPTWCPTSTSHLKEAEEKMLKCVPCTYKKEPVHISNGNKIWTLKFSHNISNKTPLVLLHGFGGGLGLWALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWGFPERPDLADQDRPIPVWIRALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGKMHPDIPVSVIFGARSCIDGNSGTSIQSLRPHSYVKTIAILGAGHYVYADQPEEFNQKVKEICDTVD | Coenzyme A-dependent lysophosphatidic acid acyltransferase that catalyzes the transfert of an acyl group on a lysophosphatidic acid. Functions preferentially with 1-oleoyl-lysophosphatidic acid followed by 1-palmitoyl-lysophosphatidic acid, 1-stearoyl-lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid as lipid acceptor. Functions preferentially with arachidonoyl-CoA followed by oleoyl-CoA as acyl group donors (By similarity). Functions in phosphatidic acid biosynthesis (By similarity). May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2 (By similarity). Involved in keratinocyte differentiation (By similarity). Regulates lipid droplet fusion (By similarity). a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + CoA 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + eicosanoyl-CoA = 1-(9Z)-octadecenoyl-2-eicosanoyl-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA Acyltransferase activity is inhibited by detergents such as Triton X-100 and 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS). Acyltransferase activity is inhibited by the presence of magnesium and calcium. Interacts with ADRP, PLIN and PNPLA2. Interacts with PLIN5; promotes interaction with PNPLA2 (By similarity). Colocalized with PLIN and ADRP on the surface of lipid droplets. The localization is dependent upon the metabolic status of the adipocytes and the activity of PKA (By similarity). The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily. |
Q6QA69 | MKAMAAEEEVDSADAGGGSGWLTGWLPTWCPTSTSHLKEAEEKMLKCVPCTYKKEPVRISNGNSIWTLMFSHNMSSKTPLVLLHGFGGGLGLWALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPWGFPERPDLADQERPIPVWIRALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGGLHPDIPVSVIFGARSCIDGNSGTSIQSLRPKSYVKTIAILGAGHYVYADQPEEFNQKVKEICHTVD | Coenzyme A-dependent lysophosphatidic acid acyltransferase that catalyzes the transfert of an acyl group on a lysophosphatidic acid. Functions preferentially with 1-oleoyl-lysophosphatidic acid followed by 1-palmitoyl-lysophosphatidic acid, 1-stearoyl-lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid as lipid acceptor. Functions preferentially with arachidonoyl-CoA followed by oleoyl-CoA as acyl group donors (By similarity). Functions in phosphatidic acid biosynthesis (By similarity). May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2 (By similarity). Involved in keratinocyte differentiation (By similarity). Regulates lipid droplet fusion (By similarity). a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + CoA 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + eicosanoyl-CoA = 1-(9Z)-octadecenoyl-2-eicosanoyl-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA (9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA Acyltransferase activity is inhibited by detergents such as Triton X-100 and 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS). Acyltransferase activity is inhibited by the presence of magnesium and calcium. Interacts with ADRP and PLIN. Interacts with PNPLA2 (By similarity). Interacts with PLIN5; promotes interaction with PNPLA2. Colocalized with PLIN and ADRP on the surface of lipid droplets. The localization is dependent upon the metabolic status of the adipocytes and the activity of PKA. Increased in the early stage of adipocyte differentiation. The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily. |
Q1LZ86 | MDLDVVNMFVIAGGTLALPILAFVASFLLWPSALIRIYYWYWRRTLGMQVRYVRHEDYQFCYSFRGRPGHKPSILMLHGFSAHKDMWLSMVKFLPKNLHLVCVDMPGHEGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKPFHLVGTSMGGHVAGVYAAHYPSDVCSLSLVCPAGLQYSTDNKFVQRLKELQESAAVEKIPLIPTTPKEMSEMLQLCSYVRFKVPQQILQGLVDVRIPHNTFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIANSQVELLENCGHSVVMERPRKTAKLLVDFLASVHSTDNSKKLD | Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol (By similarity). Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways. Also has a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (By similarity). Also able to degrade bis(monoacylglycero)phosphate (BMP) and constitutes the major enzyme for BMP catabolism. BMP, also known as lysobisphosphatidic acid, is enriched in late endosomes and lysosomes and plays a key role in the formation of intraluminal vesicles and in lipid sorting (By similarity). Hydrolyzes glycerol monoesters of long-chain fatty acids. 1-octanoylglycerol + H2O = glycerol + H(+) + octanoate 1-decanoylglycerol + H2O = decanoate + glycerol + H(+) 1-dodecanoylglycerol + H2O = dodecanoate + glycerol + H(+) 1-tetradecanoylglycerol + H2O = glycerol + H(+) + tetradecanoate 2-hexadecanoylglycerol + H2O = glycerol + H(+) + hexadecanoate 2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+) 1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+) 2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+) 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+) 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+) 1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+) (S,S)-3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(3'-(9Z-octadecenoyl)-1'-sn-glycerol) + H2O = (9Z)-octadecenoate + (S,S)-3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) + H(+) (S,S)-2-(9Z-octadecenoyl)-sn-glycero-1-phospho-(2'-(9Z-octadecenoyl)-1'-sn-glycerol) + H2O = (9Z)-octadecenoate + (S,S)-2-(9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) + H(+) (R,R)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(2'-(9Z-octadecenoyl)-3'-sn-glycerol) + H2O = (9Z)-octadecenoate + (R,R)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(3'-sn-glycerol) + H(+) Belongs to the AB hydrolase superfamily. |
Q6ZMF7 | MDLDVVNMFVIAGGTLAIPILAFVASFLLWPSALIRIYYWYWRRTLGMQVRYVHHEDYQFCYSFRGRPGHKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKPFHLVGTSMGGQVAGVYAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKELQGSAAVEKIPLIPSTPEEMSEMLQLCSYVRFKVPQQILQGLVDVRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVELLENCGHSVVMERPRKTAKLIIDFLASVHNTDNNKKLD | Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol (PubMed:22969151). Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways (By similarity). Also has a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (By similarity). Also able to degrade bis(monoacylglycero)phosphate (BMP) and constitutes the major enzyme for BMP catabolism (PubMed:26491015). BMP, also known as lysobisphosphatidic acid, is enriched in late endosomes and lysosomes and plays a key role in the formation of intraluminal vesicles and in lipid sorting (PubMed:26491015). Hydrolyzes glycerol monoesters of long-chain fatty acids. 1-octanoylglycerol + H2O = glycerol + H(+) + octanoate 1-decanoylglycerol + H2O = decanoate + glycerol + H(+) 1-dodecanoylglycerol + H2O = dodecanoate + glycerol + H(+) 1-tetradecanoylglycerol + H2O = glycerol + H(+) + tetradecanoate 2-hexadecanoylglycerol + H2O = glycerol + H(+) + hexadecanoate 2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+) 1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+) 2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+) 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+) 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+) 1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+) (S,S)-3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(3'-(9Z-octadecenoyl)-1'-sn-glycerol) + H2O = (9Z)-octadecenoate + (S,S)-3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) + H(+) (S,S)-2-(9Z-octadecenoyl)-sn-glycero-1-phospho-(2'-(9Z-octadecenoyl)-1'-sn-glycerol) + H2O = (9Z)-octadecenoate + (S,S)-2-(9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) + H(+) (R,R)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(2'-(9Z-octadecenoyl)-3'-sn-glycerol) + H2O = (9Z)-octadecenoate + (R,R)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(3'-sn-glycerol) + H(+) Optimum pH is 7.2-9 with 2-arachidonoyglycerol as substrate. Belongs to the AB hydrolase superfamily. |
Q9DCD4 | MDLDVVNMFVIAGGTLAIPILAFVASFLLWPSALIRIYYWYWRRTLGMQVRYAHHEDYQFCYSFRGRPGHKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTRSSLDDLSIVGQVKRIHQFVECLKLNKKPFHLIGTSMGGHVAGVYAAYYPSDVCSLSLVCPAGLQYSTDNPFVQRLKELEESAAIQKIPLIPSTPEEMSEMLQLCSYVRFKVPQQILQGLVDVRIPHNSFYRKLFLEIVNEKSRYSLHENMDKIKVPTQIIWGKQDQVLDVSGADILAKSISNSQVEVLENCGHSVVMERPRKTAKLIVDFLASVHNTDNKKLN | Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol (PubMed:18096503, PubMed:20657592). Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways (PubMed:18096503, PubMed:20657592). Also has a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (PubMed:24095738). Also able to degrade bis(monoacylglycero)phosphate (BMP) and constitutes the major enzyme for BMP catabolism (PubMed:26491015). BMP, also known as lysobisphosphatidic acid, is enriched in late endosomes and lysosomes and plays a key role in the formation of intraluminal vesicles and in lipid sorting (PubMed:26491015). Hydrolyzes glycerol monoesters of long-chain fatty acids. 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+) 1-octanoylglycerol + H2O = glycerol + H(+) + octanoate 1-decanoylglycerol + H2O = decanoate + glycerol + H(+) 1-dodecanoylglycerol + H2O = dodecanoate + glycerol + H(+) 1-tetradecanoylglycerol + H2O = glycerol + H(+) + tetradecanoate 2-hexadecanoylglycerol + H2O = glycerol + H(+) + hexadecanoate 2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+) 1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+) 2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+) 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+) 1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+) (S,S)-3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(3'-(9Z-octadecenoyl)-1'-sn-glycerol) + H2O = (9Z)-octadecenoate + (S,S)-3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) + H(+) (S,S)-2-(9Z-octadecenoyl)-sn-glycero-1-phospho-(2'-(9Z-octadecenoyl)-1'-sn-glycerol) + H2O = (9Z)-octadecenoate + (S,S)-2-(9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) + H(+) (R,R)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(2'-(9Z-octadecenoyl)-3'-sn-glycerol) + H2O = (9Z)-octadecenoate + (R,R)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(3'-sn-glycerol) + H(+) Optimum pH is 7.5-8.0. Widely expressed with higher expression in small intestine, liver and brown adipose tissue (PubMed:24095738). In brain, expressed postsynaptically in cortical neurons but not detected in microglia (at protein level) (PubMed:20657592). Up-regulated in small intestine and liver by high-fat diet. Abhd6 partial knockdown inducing a stronger depletion in liver, kidney and white adipose tissues protects mice against hight-fat diet-induced metabolic disorder and obesity. De novo lipogenesis in liver is reduced and associated with a reduced expression of lipogenic genes. Accumulation of phospholipids and lysophospholipds in the liver is also observed. Belongs to the AB hydrolase superfamily. Extended N-terminus. |
Q5XI64 | MDLDVVNMFVIAGGTLAIPILAFVASFLLWPSALIRIYYWYWRRTLGMQVRYVHHEDYQFCYSFRGRPGHKPSVLMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTRSSLDDLSIVGQVKRIHQFVECLKLNKKPFHLIGTSMGGNVAGVYAAYYPSDVCSLSLVCPAGLQYSTDNRFVQRLKELEDSAATQKIPLIPSTPEEMSEMLQLCSYVRFKVPQQILQGLVDVRIPHNSFYRKLFLEIVSEKSRYSLHENMDKIKVPTQIIWGKQDQVLDVSGADILAKSITNSQVEVLENCGHSVVMERPRKTAKLVVDFLASVHNPDNNKKLN | Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol (By similarity). Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways. Also has a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (By similarity). Also able to degrade bis(monoacylglycero)phosphate (BMP) and constitutes the major enzyme for BMP catabolism. BMP, also known as lysobisphosphatidic acid, is enriched in late endosomes and lysosomes and plays a key role in the formation of intraluminal vesicles and in lipid sorting (By similarity). Hydrolyzes glycerol monoesters of long-chain fatty acids. 1-octanoylglycerol + H2O = glycerol + H(+) + octanoate 1-decanoylglycerol + H2O = decanoate + glycerol + H(+) 1-dodecanoylglycerol + H2O = dodecanoate + glycerol + H(+) 1-tetradecanoylglycerol + H2O = glycerol + H(+) + tetradecanoate 2-hexadecanoylglycerol + H2O = glycerol + H(+) + hexadecanoate 2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+) 1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+) 2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+) 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+) 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+) 1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+) (S,S)-3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(3'-(9Z-octadecenoyl)-1'-sn-glycerol) + H2O = (9Z)-octadecenoate + (S,S)-3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) + H(+) (S,S)-2-(9Z-octadecenoyl)-sn-glycero-1-phospho-(2'-(9Z-octadecenoyl)-1'-sn-glycerol) + H2O = (9Z)-octadecenoate + (S,S)-2-(9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) + H(+) (R,R)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(2'-(9Z-octadecenoyl)-3'-sn-glycerol) + H2O = (9Z)-octadecenoate + (R,R)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(3'-sn-glycerol) + H(+) Belongs to the AB hydrolase superfamily. |
Q17QP1 | MLTGVTDGIFCCLLGAPPNAVGPLESVESSDGYTFVEVKPGRVLRVKHAGPAPAPTPPPPLSDAAQGDQSGLVRCQRRITVYRNGRLLVENLGRAPRADLLHGQNGSGEPPAALEVELADPAGSDGRSVPGSAGSGSGGRRRRARRPKRTIHIDCEKRITSCKGAQADVVLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFKRYAKKRNVLIGHSYGVSFCTFLAHEYPDLVHKVIMINGGGPTALEPSLCSVFNMPTCVLHCLSPCLAWSFLKAGFARQGAKEKQLLKEGNAFNVSSFVLRAMMSGQYWPEGDEVYHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIDEGSHMVMLECPETVNTLLHEFLLWEPEPSPKALPEPLPAPPEEKK | Belongs to the AB hydrolase superfamily. |
Q9HAE9 | MLTGVTDGIFCCLLGTPPNAVGPLESVESSDGYTFVEVKPGRVLRVKHAGPAPAAAPPPPSSASSDAAQGDLSGLVRCQRRITVYRNGRLLVENLGRAPRADLLHGQNGSGEPPAALEVELADPAGSDGRLAPGSAGSGSGSGSGGRRRRARRPKRTIHIDCEKRITSCKGAQADVVLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFKRYAKKRNVLIGHSYGVSFCTFLAHEYPDLVHKVIMINGGGPTALEPSFCSIFNMPTCVLHCLSPCLAWSFLKAGFARQGAKEKQLLKEGNAFNVSSFVLRAMMSGQYWPEGDEVYHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIDEGSHMVMLECPETVNTLLHEFLLWEPEPSPKALPEPLPAPPEDKK | Belongs to the AB hydrolase superfamily. |
Q4R584 | MLTGVTDGIFCCLLGTPPNAVGPLESVESSDGYTFVEVKPGRVLRVKHAGPAPASAAPPPLSASSDAAQGDLSGLVRCQRRITVYRNGRLLVENLGRAPRADLLHGQNGSGEPPAALEMELADPAGSDGRSAPGSGSGSGSGSGSGGRRRRARRPKRTIHIDCEKRITSCKGAQADVVLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFKRYAKKRNVLIGHSYGVSFCTFLAHEYPDLVHKVIMINGGGPTALEPSFCSIFNMPTCVLHCLSPCLAWSFLKAGFARQGAKEKQLLKEGNAFNVSSFVLRAMMSGQYWPEGDEVYHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIDEGSHMVMLECPETVNTLLHEFLLWEPEPSPKALPEPLPAPPEDKK | Belongs to the AB hydrolase superfamily. |
Q9JMF5 | MTSEHTMLTGVTDGFFCCLLGTPPNAVRPLESVESSDGYTFVEVKPGRVLRVKHAGPAPIPTPPPPPPEDDPGVKTGLVRCQRRITVYRNGRLVVENLGRAPRADLQGRSGSGDPPAALEVELAEPAGGDTRANPGSGRRRRPRRPKRTIHIDCEQRITSCKGAQADVVLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFTRYAKKRNVLIGHSYGVSFCTFLAHEYPDLVHKVIMINGGGPTALEPSLCSIFNMPTCVLHCLSPCLAWSFLKAGFARQGAKEKQLLKEGNAFNVSSFVLRAMMSGQYWPEGDEVYHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIEEGSHMVMLECPETVNTLLHEFLLWEPEPEAEPKLEPKPKPQLLQPEPAPGEEK | Belongs to the AB hydrolase superfamily. It is uncertain whether Met-1 or Met-7 is the initiator. |