lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Plays a crucial role in elastic fiber formation in tissue, and in the formation of ultrastructural connections between elastic laminae and smooth muscle cells in the aorta, therefore participates in terminal differentiation and maturation of smooth muscle cell (SMC) and in the mechanical properties and wall integrity maintenance of the aorta. In addition, is involved in the control of collagen fibril assembly in tissue throught proteolytic activation of LOX leading to cross- linking of collagen and elastin (By similarity). Also promotes ELN coacervation and participates in the deposition of ELN coacervates on to microfibrils but also regulates ELN cross- linking through LOX interaction. Moreover adheres to the cells through heparin binding in a calcium-dependent manner and regulates vascularlar smooth muscle cells proliferation through angiotensin signaling.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix. Secreted, extracellular space, extracellular matrix, basement membrane. Note=Localizes on the microfibrils surrounding ELN cores.
Sequence:
MLPCASCLPGSLLLWALLLLLLGSASPQDSEEPDSYTECTDGYEWDPDSQHCRDVNECLTIPEACKGEMKCINHYGGYLCLPRSAAVINDLHGEGPPPPVPPAQHPNPCPPGYEPDDQDSCVDVDECAQALHDCRPSQDCHNLPGSYQCTCPDGYRKIGPECVDIDECRYRYCQHRCVNLPGSFRCQCEPGFQLGPNNRSCVDVNECDMGAPCEQRCFNSYGTFLCRCHQGYELHRDGFSCSDIDECSYSSYLCQYRCINEPGRFSCHCPQGYQLLATRLCQDIDECESGAHQCSEAQTCVNFHGGYRCVDTNRCVEPYIQVSENRCLCPASNPLCREQPSSIVHRYMTITSERSVPADVFQIQATSVYPGAYNAFQIRAGNSQGDFYIRQINNVSAMLVLARPVTGPREYVLDLEMVTMNSLMSYRASSVLRLTVFVGAYTF
The following text describes a protein:
Function:
O-linked N-acetylglucosamine transferase (OGT) that mediates O-glycosylation of capsid protein (CP) of virus in case of infection by Plum pox virus. OGTs catalyze the addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Probably acts by adding O-linked sugars to yet unknown proteins. Its OGT activity has been proved in vitro but not in vivo. Required with SPY for gamete and seed development. Mediates O-glycosylation of the DELLA protein RGA, a repressor of the gibberellin (GA) signaling pathway. O-glycosylation by SEC inhibits RGA binding to four of its interactors PIF3, PIF4, JAZ1, and BZR1 that are key regulators in light, jasmonate, and brassinosteroid signaling pathways, respectively. Activates ATX1 through O-GlcNAc modification to augment ATX1-mediated H3K4me3 histone epigenetic modification at FLC locus, thus preventing premature flowering.
Sequence:
MISSKNGAAMISRPVFLSDRVDEVFSRKLDLSVSSSSSSSLLQQFNKTHEGDDDARLALAHQLYKGGDFKQALEHSNMVYQRNPLRTDNLLLIGAIYYQLQEYDMCIARNEEALRIQPQFAECYGNMANAWKEKGDTDRAIRYYLIAIELRPNFADAWSNLASAYMRKGRLSEATQCCQQALSLNPLLVDAHSNLGNLMKAQGLIHEAYSCYLEAVRIQPTFAIAWSNLAGLFMESGDLNRALQYYKEAVKLKPAFPDAYLNLGNVYKALGRPTEAIMCYQHALQMRPNSAMAFGNIASIYYEQGQLDLAIRHYKQALSRDPRFLEAYNNLGNALKDIGRVDEAVRCYNQCLALQPNHPQAMANLGNIYMEWNMMGPASSLFKATLAVTTGLSAPFNNLAIIYKQQGNYSDAISCYNEVLRIDPLAADALVNRGNTYKEIGRVTEAIQDYMHAINFRPTMAEAHANLASAYKDSGHVEAAITSYKQALLLRPDFPEATCNLLHTLQCVCCWEDRSKMFAEVESIIRRQINMSVLPSVQPFHAIAYPIDPILALEISRKYAAHCSIIASRFGLPPFTHPAGLPVKREGGFKRLRIGYVSSDFGNHPLSHLMGSVFGMHNRENVEVFCYALSANDNTEWRQRIQSEAEHFLDVSAMSSDAIAKIINQDKIQILINLNGYTKGARNEIFAMQPAPIQVSYMGFPGTTGATYIDYLVTDEFVSPLQYAHIYSEKLVHLPHCYFVNDYKQKNQDVLDPNSKPKRSDYGLPEDKFIFACFNQLYKMDPEIVNTWCNILKRVPNSALWLLRFPAAGEMRFRTYAAAQGVQPDQIIFTDVAMKSEHIRRSVLADVILDTPLCNGHTTGTDVLWAGVPMITLPLEKMATRVAGSLCLATGLGHGMIVNSLEEYEEKAVSLALNKPKLQALTKELRASRLTCPLFDTMRWVKNLERSYFKMWNLHCSGQQPQHFKVLENDLEFPHDR
The following text describes a protein:
Function:
Controls stomatal patterning.
Subcellular Localization:
Secreted.
Sequence:
MASTMGKVVVILIILCLLLLQSFKPADALKFTRIGYRSMNGRVPVPPRCMNKCTVCSPCKPVLVTRPPKLYPKEEEYYPLAWKCSCGGHLYDP
The following text describes a protein:
Function:
Inorganic phosphate and glucose-6-phosphate antiporter of the endoplasmic reticulum. Transports cytoplasmic glucose-6-phosphate into the lumen of the endoplasmic reticulum and translocates inorganic phosphate into the opposite direction. Forms with glucose-6-phosphatase the complex responsible for glucose production through glycogenolysis and gluconeogenesis. Hence, it plays a central role in homeostatic regulation of blood glucose levels.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAAQGYGYYRTVIFSAMFGGYSLYYFNRKTFSFVMPSLVEEIPLDKDDLGFITSSQSAAYAISKFVSGVLSDQMSARWLFSSGLLLVGLVNIFFAWSSTVPVFAALWFLNGLAQGLGWPPCGKVLRKWFEPSQFGTWWAILSTSMNLAGGLGPILATILAQSYSWRSTLALSGALCVVVSFLCLLLIHNEPADVGLRNLDPMPSEGKKGSLKEESTLQELLLSPYLWVLSTGYLVVFGVKTCCTDWGQFFLIQEKGQSALVGSSYMSALEVGGLVGSIAAGYLSDRAMAKAGLSNYGNPRHGLLLFMMAGMTVSMYLFRVTVTSDSPKLWILVLGAVFGFSSYGPIALFGVIANESAPPNLCGTSHAIVGLMANVGGFLAGLPFSTIAKHYSWSTAFWVAEVICAASTAAFFLLRNIRTKMGRVSKKAE
The following text describes a protein:
Function:
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Subcellular Localization:
Cytoplasm.
Sequence:
MEKIRTRYAPSPTGYLHVGGTRTAIFNFLLAKHFNGEFIIRIEDTDTERNIKEGINSQFDNLRWLGVIADESVYNPGNYGPYLQSQKLAVYKKLAFDLIEKNLAYRCFCSKEKLESDRKQAINNHKTPKYLGHCRNLHSKKITNHLEKNDPFTIRLKINNEAEYSWNDLVRGQITIPGSALTDIVILKANGVATYNFAVVIDDYDMEITDVLRGAEHISNTAYQLAIYQALGFKRIPRFGHLSVIVDESGKKLSKRDEKTTQFIEQFKQQGYLPEALLNFLALLGWHPQYNQEFFNLKQLIENFSLSRVVSAPAFFDIKKLQWINANYIKQLTDNAYFNFIDNYLDVKVDYLKDKNREISLLFKNQITHGVQINELIRESFATKIGVENLAKKSHILFKNIKLFLEQLAKSLQGLEEWKAEQIKTTINKVGAVFNLKGKQLFMPIRLIFTNKEHGPDLAHIIEIFDKESAINLIKQFINATNLF
The following text describes a protein:
Function:
Involved in the biosynthesis of carotenoids spheroidene and spirilloxanthin. Catalyzes the hydration of neurosporene to the corresponding hydroxylated carotenoids 1-HO-neurosporene and that of lycopene to 1-HO-lycopene. It exhibits negligible activity in converting HO-neurosporene, HO-lycopene, or any other derivative such as spheroidene, 1-HO-3,4-didehydrolycopene.
Sequence:
MIAFIGSVFSPWYRWSGRREPQNHCCINMVTTGTDGRFTMTDRGRSALRQSRDSFQVGPSKLTWTGKELVIDVDEWGALPKLGKLKGRVVLTPRAVTGVEVRLTPDAGHTWRPFAPIADVEVDLAPGHKWTGHGYFDANFGTRALEEDFSFWTWGRFPLKDRTVCFYDATRLDRTKVALAVQINPDGSVCEIDSPPPLVKMKRTPWFVRRETRCDAGAHPAGVYSLLEAPFYSRALMRTQIDGEETVGMHEALDLVRFRQPVLKPMLAVRVPRRAGWKHKD
The following text describes a protein:
Function:
Membrane-associated protein that warps the membrane surface to access and bind aromatic isoprenes with high specificity, including ubiquinone (CoQ) isoprene intermediates and presents them directly to Coq7, therefore facilitating the Coq7-mediated hydroxylase step. Participates in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration.
Subcellular Localization:
Mitochondrion.
Sequence:
MIIDTNNNSYNFNDNNNCNNSNHEFLFWKVWRNRYLINLIINNICGQELLFTSMDSYYIGNRIKFENILDLTWLVNKKQYSILKDKLISNQPLEITSRGLKLLYEQIDELSQSEILNLLYQIKKNQISDIKYIDLSKVPLKGLKEYYRLNPSGRDILKNKSIVDNAILNMDFNILNFIKSIYQQQQQQQQQQTNIINNNNNNNNSNNINNNTTYNNSIFKNSFTESQLIENACKSNDPEKMFKFIEEELNLDLKKLIDKYPQNYYNMFMNILDKLTPERIKLIFHCANDGCTYEKPFHYIFPFKYTVDSLKCLILDTVPLKKTLISKELSIEELLEGYKAGYEHKYFPFFIDYFFKQNQIEKVISYLKVSKTISTINYHYKNLYSDMQVFFYVETVRNFNIRALDYIIETKVSLNFLNKDSVIEPLTPIASNSQVFDFLKKFIVHFDVYCYIIKLLFIFYPIDTIKSLMKIEEFEIKFIKELHEKNEIIQTLLPIISNEPEKIEFLLKYRVKRISTINLNIGSNNALLERSNKEKLEFFNHCCYHDINSIITNECKKELLQNLKLKNESVQDSIEIYNLIDYNSIGIEKEIIQSLLFTEHIKQFFFSQDLDSVKNLILALLYNNNDTSLINKQKIGEFKKINNDFNKKRNNSNINNNINNLIIENIILLSNRYIIEKFTKELIENDSVSNEVLLKLIEEVIKLKEKLPFSIILLLLKKNKYLILENLFETQKEQIMNSLNGTSKSKFLMEPNEGVDQLFSNFKDINIIKPSHFISPNSYDHCKTLFLTYGYPNYLIDYLSKNQQSIETFPLTKHLKDSIFKYTTLDQFLELSKHYSFKDINDQLNNNNNNNNNNNNNQQNQQQIAMQIQQINNEIDDTNLMIDDDIINNNHIIGNNNNNANNNNINNYINENDDEEPDNEISISNNFQQLHQEESNEVIILNNSIQFNRVDIICWLLENKKLSVSFIIVSLFNLDRYHILDYIIRKYKNRYFSNPIEKRLNLVFLSLVNSNSLSIFKMIESLYPNHKFIVGRSIINSLVLNDKNNEKLKYLNKKNYLVDLEYLNHKSKKVNGKTIKLTFPDSISKTIFEIINQNKKRPNNDINLYLTNNNNINNNNNNISSIDKKRLNKKYKRF
The following text describes a protein:
Function:
Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used in anaerobic growth, and succinate dehydrogenase is used in aerobic growth. Anchors the catalytic components of the fumarate reductase complex to the cell inner membrane, binds quinones. The QFR enzyme complex binds 2 quinones in or near the membrane; 1 near the [3Fe-4S] cluster (QP is proximal to the [3Fe-4S] cluster, on the cytoplasmic side of the membrane) while QD (the distal cluster) is on the other side of the membrane. It is not clear if both of the quinol-binding sites are functionally relevant.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MTTKRKPYVRPMTSTWWKKLPFYRFYMLREGTAVPAVWFSIELIFGLFALKNGPEAWAGFVDFLQNPVIVIINLITLAAALLHTKTWFELAPKAANIIVKDEKMGPEPIIKSLWAVTVVATIVILFVALYW
The following text describes a protein:
Function:
Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence.
Domain:
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase. NRPS5 has the following architecture: A-T-C-A-T-C-T.
Sequence:
MNLTLTTTSITIQPSATMANRAPTLLDHFHDQLQKHSSSVAIEDGTQSADQGAWERVTYAQLDALSDSWSKRLRQAGVGAGCIVPLLSKRSVAMVAATLAILKLRAAYVSIDIDSWGKDRIDTVLKTVNPQIIVSTSPCPKDHYPYPVVALERNDFDETVTSNGTQWTRNDEDSIDRGNDLAYIIFTSGTTGIPKGVKIGQRSISRYVKEGGDLPFNFNTTHGTRVLLICSIAFDVCAGVMFNTLCNGGTLVLADPSTFETAAKTCHVLPLTPSILVTLDPKAGFDTVEKIFLGGESPSPSLIEAWSSPRRRLYNAYGPTETTCTAFMGELLPGSPITIGYPISYSTVTLLDEDGMESVEGEICIAGLGLALGYFHDPERTNSAFVEWNGVRIYKTGDYGRRTKHGLQFCGRRDSVVKNRGFLINLEADVEPALLSYDKVDSASAFMSQGQLIAFVTPTSAKEGLREYLANTVSSFLVPDTIYSLDEFPRTSNGKVDRRSLMRMHELEQGSDTASLERGLGAVESVRRGLSHVLRLPESQILPASSFRHLGGHSLAAVMLVSVLRRMGFGISVAEVLLLDTVENIAAAVVELSDIPHALSAQEDLIERLRHDISTTRPLDEGVTIAPMTDMQTRLLGASVATPGLSFIKTSFTLDHPEKEDLTSTLRAAWVRLHQTHEILRTAFVLTASNGTQIISQEPDFSWKEKFVTESEWESVCRREEHLDVADFPDFDAENRASLSRVVLIIAPRRRTRFVWTVHHSLIDGWSMATLMRDFASCLDGKPIPAPPQFAQVAQAIGQLKAESSDRAVSFWKEYLDGYTPAQRLRVSPPSDVSDYTQAALSRKLTVSVSALEDAARDRFAVTPATLLYAAWGLLLSRYSGTDRAALGAVLSGRSLPIPGVENIIGPLINTLPLAINTQEAQSTYSFVQSVFRRLCDILEFQWSPVALIQEGCGCNPSELFETLFALQYDFPQTPWKSSEVPEPRDIRYEEATQVPLTVLLDNANGQFEVRFIYRRSHFGDATVQRMIGQFGNLLENLIAAQPDTDLSNVTGQMFNNRVYEMSIAKPGQPVSACKVPESLTEAIENSIQAHPDIYAVEGLTGRLTYREFGRMTEHISQRLLQHIQPGSVACMISDGSLLWLLAMVAIIRAGAIYCPVDEKLPRDRKDYMVRNSRAALILYANSSQEPLCNGVPSLNMESIMQEISSSSGSPIATSRNRPSGDTVACLVYTSGSTGLPKAVQLQHKGILNVISQPEGRLYSRPGQRNAQMLSLGFDCCIKEVFSTICFGATLVLKDPENPISHLARVDATMATPSLLATLEPTDYPNLKVITVAGEAVSQVLNDKWAAGRTLINGYGPAECTLISTTAILHPGNRVSIGKPLPGLSCYLLDSNKRPVPMGVSGEIYISGVQVTPGYLHNEQETSKRFLSDSFNPGQVMYRTGDIGRMLEDGNIEYIGREDNQIKLRGFRIDLGEVQSTISKLASTASNVALIVSNGNLVAFMTPETIDVRSLAKSLETQLPQYAVPNRIIALATLPTSANNKVDSSALQRYLRDHGKDGAVVEDLETDTQRVLAVIWADMLGRDLNQTPISPSDRFFELGGHSLLQIKVAQAISKRWNIRPLPLKQVIRHHSLQDLSLAIDELVSDPRTVSTMPFLEMTPVARNGQLPLSYLEKEMLLNHLISGGSPAGNMNFVCKIRGDINAETLADAFQRVTADVEVFRTRYSVIEGTLFRQQAPGSVKVPRVVQTGNLSSFVHGRITKSFDLSTEPPVDVSIIIGTPMQAMLVVVMSHVVGDAATMATYLNRVSRTYDLLRSNSQTTNTSTVPDNLTYIDWAHWASTLQPNPRALTFWSSYLSNPPSPLTFGNPSPAPATYIGLTRSWTLPPSMYRKLSDLAAKASVTMHQLILAAVFFSLQCVDRRDDILVAAPFTHRTEPGTESLPGLFLDRLLLRIQRSPHQSSIFDFLSSVRETSQQALAHVIPFHTLRHSLAHKPSLIDPLFKVMVTYHTAADQRPLLDLSGAEVQPIPWRHTGGSKFPLKFEFTEMATQDLEVDMEYDLGCIREDIALRLEFALSFALQLMVLERETDDIIQLVQMSFCPGEGSPVGLTPSHEGSAELTNGTNKTDSTTGQQELENNLTDVVCECLGLEIQDVDADKSFWDLGAQSMDALKLQHLCEKRGVRVRLRDIFVSRSLLELATCAVII
The following text describes a protein:
Function:
Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Subcellular Localization:
Mitochondrion.
Sequence:
MNCSTQRIVNQFSRQTARRRFNIRSRRWNSTFETREWSTPLARTLANVIKTTGPVPIAAFMRQVLTSPEGGYYTTKPGGGGEVFGKKGDFVTSPEISQVFGELVGIWTIAEWMAQGGKKSGVQLMEIGPGKGTLMDDMLRTFRNFKPFTSSLEAIYLVEASPTLREVQKQLLCGNAVMEETDIGHRCTSKYFNVPVIWVEDIRLLPHEEDKTPFIFAHEFFDALPIHAFESVPPSPENEQQEQEIMTPTGRTKLQRPPKAANTPQWRELMVTLNPKAVDENIKDEPEFKLTLAKASTPSSLVIPEISERYRALKSQPGSTIEVSPESRIYASDIARRIGGSSQPPRTAAGRNASAPSAIAKRIPSGAALIMDYGTMSTVPINSLRGIQNHKIVPALSSPGRVDVSADVDFTSLAEAALEASEGVEVHGPVEQGHFLQAMGIAERMQQLLSTVKDEKKRKILETGWQRLVERGGGGMGKLYKVMTIIPENGGRRRPVGFGGGVPL
The following text describes a protein:
Function:
Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon. Plays a role in metaphase spindle orientation. Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitment to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole. Plays a role in primary cilia formation (By similarity).
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton.
Sequence:
MSEKNLKVGARVELTGKDLLGTVAYVGMTSFAVGKWVGVVLDEPKGKNSGSIKGQQYFQCDENCGMFVRPTQLRLLEAAPGSRRSIEDVSGATPTAAQPTKARLSSSRTSLSSSRQSLLGSRTQLTTSLSERTASSSSIGPRKSLAPQNSKDKESPSTSLAEGAPAASGGNGAASHASSKRASFVETGFLEILKPQFTPSQPLRSPSFTMPSNSGAEDKVALLEAQKTSAELQAQLADLTEKLETLKQRRNEDKERLREFDKMKIQFEQLQEFRTKIMGAQASLQKELLRAKQEAKDAIEAKEQHAQEMADLADNVEMITLDKEMAEEKADTLQLELESSKERIEELEVDLELLRSEMQNKAESAIGNISGGGDSPGLSTYEFKQLEQQNIRLKETLVRLRDLSAHDKHDIQKLSKELEMKRSEVTELERTKEKLSAKIDELEAIVADLQEQVDAALGAEEMVEQLAEKKMELEDKVKLLEEEIAQLEALEEVHEQLVESNHELELDLREELDLANGAKKEVLRERDAAIETIYDRDQTIVKFRELVQKLNDQLTELRDRNSSNEKESLQDPSLKMVTETIDYKQMFAESKAYTRAIDVQLRQIELSQANEHVQMLTAFMPESFMSRGGDHDSILVILLISRIVFKCDIVVSQTRERFPPVDAITREAVTQGHAVQQYAFKCRLLHYVHSLQCALHQILYGLNSCQPDTLLRAGSSLPEMVAQEKIVDGIIELLKSNQLDENSTTDNIEKCVAFFNAMNSVLLAGEQLLNEIQMIRDCVASLGAACESILSDTAIAKVIIQEAGATSDSVLLIQFLNENMESVRQQVKLIKRRLPSDQHVIKSGLSQHKVEAMRGLAQNISRIMSAMHQATKQSLAAIVSTIESDNAAEHTLPQEKYWALLTASCERIYEQDDRGPTQNFKTLLAQANSDLQLIAQHLLDKEYDIISAANNASNQQKSGAHSTPITQRAQLIKKQLEQKNVLAATLENREADVKQLKVAAKMKQNELSEMQIRKDLAEKKLSVLQNEYEHAVDKWKQKYEETSLQLQLKEKEFEETMDHLQSDIDALESEKSDLRDKLKLNSTTGKVQPGSESHSPHNISLSGNTSTAPGISNVSYSAPAGTAPVVAEEVELLKNAFNQERNQRLRLQAQDMRAKLSQFEPLHVPQPQDQRITALESELTRMKHAWVLSLLQVRSQDSVNSGTRIDAVALQRRNQPVPLKGEISSKASQLASDILTEYLQRKPHRATHGQFASFPTVDVKRVLQI
The following text describes a protein:
Function:
Plays a role in microtubule organization and/or maintenance for the formation of primary cilia (PC), a microtubule-based structure that protrudes from the surface of epithelial cells. Plays a critical role in G2/M checkpoint and nuclear divisions. A key player in the DNA damage-activated ATR/ATM signaling cascade since it is required for the proper phosphorylation of H2AX, RPA, CHEK2 and CHEK1. Plays a critical role in chromosome segregation, acting as a mediator required for the maintenance of genomic stability through modulation of MDC1, RPA and CHEK1.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Nucleus.
Sequence:
MAGPPAFCIGDQLILEEVYDETYIPNDREILQYAVEIGIDPQNEPELMWLAREGIVASLPAAWKPCQDITGDIYYFNFTNGESTWDHPCDEYYRSLVVQERGKLLDLGTPKKKDRKKKKEKRDKDKEPPRALLEMKNSWCSSSIPRGLPSSTADLELTLGSGVRGREPDNVSCPPWLPHQEPPLRTRRTLDDTEALLGRATALSSPDPASLRQDSPLGFLDHGEEGVGGRTRLPGSRASEDLRFPGGARVQPTQGASAGASAGDRRVSSGEPVLPKGQKPEEEAVQPGPGSAASSGAGPNPCSGPLPGPGPGREFIGPSGDRDPGPVPGDTGHGTGGESSTDSPAQELSPPGDPAPDRGLGSGWPQGKKEPPGQAAEPAEGSATDTEPGVIAPRGALPPQDALPAALLPGPDPAPSPGHGHQSGEKWPPKAQAVPGPRSESQLGHRKGEPDPRGAGPAGHTPLAAPSWRLAPLLALGADAAPWESLGSLACTRTREPRRPPGGIPQRKGSSWAPEAESGRSPMSPLELPVPGEPTRSSSRDLQSPGVEDWPSELPSPHPSLPPRSRSPTSWADEGSESEGYSEDQRFYRHILRMVKISRRPEGRALQKIPAAADGDALTTASGRGEQPEGTERRVGSAARGPEAGGCPASALSSGETTLLPSRSRGSLWQEETEAAPGRGLAAEPGGKRRSEQAAGSSLAPLFSPPGIRAEVGECSKAPAALCGTQSGPTKGRVKPRPRRETVLQPQLPEPQPAGPSRDLLAALNAGKRPLSSLGFDKTPEEEDEESDSQTPPGAWGLFKNLHLDLEALGGGFEYQETPQTSQREEGKDISLNSDSGGPPAADPLLSRGTDGSLGSVAGDGPWEKPARLQLQRKDGGEEPGPAASGLQAEGAESGPGKASDQPVEGASLKKDCKGDTSEESEVSEHLWELQPSVGSNPDSFLGLDLGFRSRLAEQLLEVSELSPLPDRFPRETPEPEEEGGDQNSPVVEAPQPGNSRGLESERSRSPPRASWAEDGQCGTPGEPEEPQAGSPFAGGPLQGLNEEPIVSPQPPGASLKDMESLAEDVEPDPESEPLPEPELEPMPRRLQAEQREEVQQEKVQQQQEELRQEAEVEASKLPEPNKQSLRALKEQLQGTSEEEEEKEEVEGEEKACVNEEGSQKPSRLRAQLRSSWQATEDQMRAEQATKLQELREELASRLVTERASLEQERRQELEHLRKELVAAEARERAALEEEKELALRQLRERLEGERKEAVAVLDREHAADLERLRALAEENHREVEVALEKQVPDVKWGAEGLGRAQQGVQQKAHLVLEYERELSDLLAEKRQGVEKDHERKMERLREEHQLALARIRQQYAEEERQQRTELLEGLTGELEQLRRAHHVERESVRQELDGQLDDLRLRHREQEKKLHDLALELETRTKATRASLAQLDVQEEMVRKKRQQLLEEEKQIAKEREEAAASSRHLREARAEQAALGEATRELRRAVEELRAQRTDLESQVEELQGRSQRLQQRIRDLDRAAQRKQEALDVLVARESPAAPPPEETLLVEDLQKPEPSLPQEPAALPSRDHRDDDSSNCQLDEIRHLLSTEGVSVRSAKEFLARQTRSLRKRQAALKAAKQQWRHDLASPQRASEGPATSLDLEDVPRSLKEETKHLGEIRSAMRQGQALLKRKEERLSQLESSLREELSDDNSLRGASSRKKVVTFDFSDLEDSSSSTLSSSSPVTPDPQPDLPLPQHKKIQFLNSSLQHITRELNGVLGVLGSLSSQQSPLFTPAPGPMSRPPTAPATSTPFPTSSKTWAPPAVPPSPAASLPSQWAWRPNPSLATSAAQSVDSFLEEKWRKYFPAGLPVLSGGPAPLENKLGYVSASEQLRLLQHSHPRTHKVGSLNVQHMIEANKKWLEHFKKDLKVPLLSHTLRPSAGPGILQLGLDETNQLKVYHS
The following text describes a protein:
Function:
Bifunctional wax ester synthase/diacylglycerol acyltransferase. Involved in cuticular wax biosynthesis. Required to reduce leaf water loss, especially during drought.
Subcellular Localization:
Cell membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MKAEKVMEREIETTPIEPLSPMSHMLSSPNFFIVITFGFKTRCNRSAFVDGINNTLINAPRFSSKMEINYKKKGEPVWIPVKLRVDDHIIVPDLEYSNIQNPDQFVEDYTSNIANIPMDMSKPLWEFHLLNMKTSKAESLAIVKIHHSIGDGMSLMSLLLACSRKISDPDALVSNTTATKKPADSMAWWLFVGFWFMIRVTFTTIVEFSKLMLTVCFLEDTKNPLMGNPSDGFQSWKVVHRIISFEDVKLIKDTMNMKVNDVLLGMTQAGLSRYLSSKYDGSTAEKKKILEKLRVRGAVAINLRPATKIEDLADMMAKGSKCRWGNFIGTVIFPLWVKSEKDPLEYIRRAKATMDRKKISLEAFFFYGIIKFTLKFFGGKAVEAFGKRIFGHTSLAFSNVKGPDEEISFFHHPISYIAGSALVGAQALNIHFISYVDKIVINLAVDTTTIQDPNRLCDDMVEALEIIKSATQGEIFHKTEV
The following text describes a protein:
Function:
Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Sequence:
MRKIPRTMSTQHPDNAKVPEWNQGEAISGENEIIEAYLAFSRYGVEEVMWDAEGKDVDTHVVRKLLSQYPEFFRHRILGKDIFLTYRVPNPKIEGAERKVFAETLNTIPITYDLAEKFYGENPNPPVFEVILPFTTSYEELIAVIKFYEKVIVNSDNTKLVDDTYVKDIIGETNPKKIEVIPLIEDRDSMLRIDTIVGKYIEIERPPYLRVFLARSDPAMNYGLLSAVLSVKYALSRLSKMEKIYGVKIFPLLGVGSLPFRGHFSPYNVENTLNEYRGIYTFTVQSAFKYDYEDDLVISAIKKVNGTNVTEKIELSEEDEEIISNVTRKYTQGYQNKIEALADVINKVALLLPRRRARKLHIGLFGYSRSTGKVTLPRAISFVGSLYTIGIPPEIIGLSSLSKMTDQELNAIFNNYKYLKNDLQFAARFVNFEALQLLKDIWNIDAEVVKAIKEDIDYAENSLGIRIGESDYMSKKHVLLSTLALLSIKEGKLDEAKTYIKEMAIVRRAIG
The following text describes a protein:
Function:
Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for arginine/glycine-rich nuclear localization signals (rg-NLS) and PY-NLS in cargo substrates. Its predominant cargo substrate seems to be mRNA-binding proteins. Required for nuclear transport of NAB2, HRP1/NAB4 and TFG2. Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo. Efficient GTP-Ran-mediated substrate release requires RNA. The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
Miscellaneous:
MISCELLANEOUS: Binds to nucleoporin FxFG but not PSFG repeat regions; MISCELLANEOUS: Present with 2130 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus, nuclear pore complex. Nucleus. Note=Predominantly cytoplasmic.
Sequence:
MASTWKPAEDYVLQLATLLQNCMSPNPEIRNNAMEAMENFQLQPEFLNYLCYILIEGESDDVLKQHYSLQDLQNNRATAGMLLKNSMLGGNNLIKSNSHDLGYVKSNIIHGLYNSNNNLVSNVTGIVITTLFSTYYRQHRDDPTGLQMLYQLLELTSNGNEPSIKALSKIMEDSAQFFQLEWSGNTKPMEALLDSFFRFISNPNFSPVIRSESVKCINTVIPLQTQSFIVRLDKFLEIIFQLAQNDENDLVRAQICISFSFLLEFRPDKLVSHLDGIVQFMLHLITTVNEEKVAIEACEFLHAFATSPNIPEHILQPYVKDIVPILLSKMVYNEESIVLLEASNDDDAFLEDKDEDIKPIAPRIVKKKEAGNGEDADDNEDDDDDDDDEDGDVDTQWNLRKCSAATLDVMTNILPHQVMDIAFPFLREHLGSDRWFIREATILALGAMAEGGMKYFNDGLPALIPFLVEQLNDKWAPVRKMTCWTLSRFSPWILQDHTEFLIPVLEPIINTLMDKKKDVQEAAISSVAVFIENADSELVETLFYSQLLTSFDKCLKYYKKKNLIILYDAIGRFAEKCALDETAMQIILPPLIEKWALLSDSDKELWPLLECLSCVASSLGERFMPMAPEVYNRAFRILCHCVELEAKSHQDPTIVVPEKDFIITSLDLIDGLVQGLGAHSQDLLFPQGTKDLTILKIMLECLQDPVHEVRQSCFALLGDIVYFFNSELVIGNLEDFLKLIGTEIMHNDDSDGTPAVINAIWALGLISERIDLNTYIIDMSRIILDLFTTNTQIVDSSVMENLSVTIGKMGLTHPEVFSSGAFANDSNWNKWCLSVNALDDVEEKSSAYMGFLKIINLTSTEVTMSNDTIHKIVTGLSSNVEANVFAQEIYTFLMNHSAQISAINFTPDEISFLQQFTS
The following text describes a protein:
Function:
Plasma membrane Na(+)/H(+) antiporter. Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry, playing a key role in salt and fluid absorption and pH homeostasis. Major apical Na(+)/H(+) exchanger in kidney and intestine playing an important role in renal and intestine Na(+) absorption and blood pressure regulation.
Subcellular Localization:
Apical cell membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein. Recycling endosome membrane; Multi-pass membrane protein.
Sequence:
MGLHRHAGLWLLGSAMLLCCVSPLKAELKNSQHESHSNSNITGISIVTLKWEHVKAPYLVAVWILVCFLCKLVIEANHHVTSIIPESALLICAGFILGGIIWGADHQQTFSLTPVVFFYYLLPSIIVDSGYHMPNKLFFSNLGAILVHAIIGTCWNAATLGLSLWGCQKGGAMGDLDIGLLQYLLFGSLIAAVDPVAVLAVFEQVHVNDVLFILVFGESLLNDGVTVVLFNVFDAFVTLGGAQIDAVEIIKGIISFFVVAFGGSLLGMVFGILMCFLTRCTKNIEIIEPGFIFVVGYLSYLTAEMLSLSAILSCVFCGVCCQKYINANMNENSVKTVKYVMKVLANGSETMIFVFLGISAIDKTIWVWNTGFILLTLLFIFVYRFIGVFLLTWPLNRYRLVPLEFIDQLIMGFGGLRGAVAYGLAVMMDEKKIKEKNLMVSTTLIVVFFTVIIQGILMKPVVTWLKVKRATLHDLTLIEKVQNRVFDHMLVAVEDISGQIGHNYFRDKWKNFEEKWMMWMLMKPSARKTQDHVFSVFHQLNLKDAVEYVTEGERSGSLEFIRNDSVLIDFKKKLGDDMLDAMPDVTADTSFDQGIMLPFRRDPVPSVSLEMHEQTMNGLREMEDLNSHHLLQEHLYKGRKQHRHRFSRNHLSINTDEDEVQEIFQRTMRKRLESFKSAKMGMALPKTISKHTKKEQQKTPNGKNRISVDEDYEFSEADSASGYDPSFTYRAGGGIENPAFMADLDPVVPLQIPPWLAEAELDSGGVAPSQRAQTRPPLTAGDLRRLAPLRISTQSTDSFMMADIPDAEQRRDSFDLPPPPPPPPKDGYHQ
The following text describes a protein:
Function:
Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MKRYQKVFLTFASLMAVWFLILIEKIQLNLSEPVQSIIPFLPLYALVVFGSYSLGVIAYNLLIMSDCKEAADSLYDEIKEAKESLRSKGMKL