lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Exhibits acyltransferase activity. Exhibits acetyltransferase activity (By similarity). Activity is calcium-independent (By similarity). Catalyzes the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC). Catalyzes the conversion 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity). Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively (By similarity). Involved in platelet-activating factor (PAF) biosynthesis by catalyzing the conversion of the PAF precursor, 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) into 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (PAF) (By similarity). May synthesize phosphatidylcholine in pulmonary surfactant, thereby playing a pivotal role in respiratory physiology (By similarity). Involved in the regulation of lipid droplet number and size.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus membrane; Single-pass type II membrane protein. Cell membrane; Single-pass type II membrane protein. Lipid droplet. Note=May adopt a monotopic topology when embedded in the lipid monolayer of the lipid droplet, with both termini exposed to the cytoplasm.
Domain:
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphocholine; The di-lysine motif may confer endoplasmic reticulum localization.
Sequence:
MRLRGCGPRAAPASSAGASDARLLAPPGRNPFVHELRLSALQKAQVALMTLTLFPVRLLVAAAMMLLAWPLALVASLGSAEKEPEQPPALWRKVVDFLLKAIMRTMWFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPNKLDTITWTWQGPGALEILWLTLCQFHNQVEIEFLPVYSPSEEEKRNPALYASNVRRVMAEALGVSVTDYTFEDCQLALAEGQLRLPADTCLLEFARLVRGLGLKPEKLEKDLDRYSERARMKGGEKIGIAEFAASLEVPVSDLLEDMFSLFDESGSGEVDLRECVVALSVVCRPARTLDTIQLAFKMYGAQEDGSVGEGDLSCILKTALGVAELTVTDLFRAIDQEEKGKITFADFHRFAEMYPAFAEEYLYPDQTHFESCAETSPAPIPNGFCADFSPENSDAGRKPVRKKLD
The following text describes a protein:
Function:
Repressor of jasmonate responses.
Subcellular Localization:
Nucleus.
Domain:
The jas domain is required for interaction with COI1.
Sequence:
MSTSSEIADSGRFSGQNMPSRAPEKSSFSQTCNLFSQYMKENATFPDLTLGRRTTPSTATMNLFPMAETSPTPVQPQTTAGQNQSRPMTIFYNGQVIVFNDLAPEKVKEILMLAGKGVPQKPTKQDEVSNSIVHDSIKIQRPQPVVADLPIARKASLARFLEKRKDRITARSPYQTQGDSKQEDSKTWLGLGAQSHIQFQLQQ
The following text describes a protein:
Function:
Regulatory subunit of the dimeric UBA3-ULA1 E1 enzyme.
Subcellular Localization:
Cytoplasm.
Sequence:
MSIDKSAKYDRQLRLWASTGQSNLENSHICLINATSTGSEILKNLILPGIGQFTIIDEKKVTKQDLSSNFFLKNQDLNEDLAVAIQKNLNELNNDVNGHAIVESLSTILAQESNLFWDQFNVVIVSDYTPNLEPLINLLWSKQIPLFIVNTIGFYGSLNIIANETTVIETHDPSKLYDLRIDHPWPELQEFADSFDLDKLNDVEHAHVPYIVIFIKALDHWRSQHDGQVPITYADKKKFRLYVKSLSRNFELETNFIDADNAHLRPHQKTEIPESIIQLISISETKKLDDSTTSIFWIFIAALKNFLNLNDQLLPLPGTLPDMASDTENYVRLQQIYRDRALKDQKLFTEQVYQILDSLGRSRDEVNQESIASFCKNARLLFATVGSKDLINDKLVNQYNYNPTTAISSGSGGGGSITILDDEEKHKLGIYFGLLTFNLFIDKYHYKPTINDFNKFLKIYHDEISPKFKLNENGEKIFKEILTHNTTNYHNLNSLMGGIVSQEVLKSTTAQYIPLDNLFVFDGIHSKSEKFKI
The following text describes a protein:
Function:
Accessory subunit of hyperpolarization-activated cyclic nucleotide-gated (HCN) channels, regulating their cell-surface expression and cyclic nucleotide dependence.
Subcellular Localization:
Cytoplasm. Membrane; Peripheral membrane protein.
Sequence:
MYQGHIQGKSSREADKAVAMVMKEIPRHPSGEEKPLLSMTSQLVNEQQESRPLLSPSIDDFLCDTKSEAKPRPVTSNTAGLDLLDLSEPLPPTQSKGKKAEAALKGESSRSQSIKKKVDESELIKAEAEKTIKTVRIPEKTTLDLVHIQMQLEKWGEGRLRGDKGSEGLQNLERKSSKEISKEILWSTDVRTQSSRGSIVAENEKISELELATAPKGLTRESRLGGAFLSRNQSLEEEFERAKAAVESDTEFWDKMQAEWEEMARRNWISENGDSPSQSGSSKETGYYFHTENPFRECSGAFEEGMRKLKEGDLPITILYLEAAILQDSSDAEAWQYLGIAQAENENEQAAIISLQRCLQLQPNNLKALMALAVSFTNIRHQQEAYEALNKWVKQNPRYKHLVKGKSPALTRRMSKAVCDSVSLEEVKELYLEAAHQNGELIDPDLQTGLGVLFNLSGEYDRAVDAFNSALVVRPEDYSLWNRLGATLANGDRSEEAVEAYSRALEIQPGFIRSRYNLGISCINLGAYREAVSNFLTALSLQRKSRTQLKIQPPVSSGNIWAALKIALSMMDQPELYHAANVGDLDILLRAFNIES
The following text describes a protein:
Function:
Involved in inflorescence stems gravitropism, by modulating vacuolar membrane (VMs) dynamics in gravity-sensing cells (e.g. endodermal cells) during the amyloplast sedimentation process.
Subcellular Localization:
Vacuole membrane.
Sequence:
MASSSLGSSIPAPEAVQLLVSSLADDSSVVREASMASLRDIASLNPLLVLDCCYAVSRGGRRRFGNMAGVFQVMAFSVGALEKGESDSVFMGKLAKIATAEIISSKELNADWQRQASGLLVSIGTHFPDLMMEEIFLHLSGPATAAPAMVQILADFASSDALQFTPRLKGVLSKVSPILGNVRDIHRPIFANAFKCWSQAVWLYITDLTSDSPLDSDVMSFLNSVFELLLRVWAVSRDHKVRVSTVDALGQMVGLITRTQLKSALPRLIPAILELYKKDHDDALLATCSLHNLLNASLLSESGPPLLDFEDLTIVLSTLLPVIGINNERKRFSDISVGRKTYNEVQRCFLTVGLVYPEDLFTFLLNKCKLKEDPLTFGALCILKHLLPRLFEAWHSKRPLLVDTASSLLDEQSLAVRKALSELIVVMASHCYLVGPSGELFVEYLVRHSAIGESDHLKAKGELVSPTQLRAVCGKGLLLLTVTIPEMELSDFNAKEYMKLQYILWPFLLKMIIPKVYTGAVASVCRCITELCRRRSSTTPMLIECKARADIPNPEELFTRLVVLLHNPLAKEQLASQILTVLGYLSPLFPKNISMFWQDEIPKMKAYVYDTEDLKLDPTYQETWDDMIINFLAESLDVTQDADWVISLGNSFAKQYILYAPDDDHAALLHRCIGILLQKVNDRAYVRDKIDWMYEQADISIPANRLGLAKAMGLVAASHLDTVLEKLKIIVDNVGQSIFQRILSLFSESYKTEDSDDIHAALALMYGYAAKYAPSSVIEARIDALVGTNMLSRLLHVRQQTAKQAVITAIDLLGRAVINAAETGATFPLKRRDQMLDYILTLMGRDENEGFAESSLEVLHTQALALNACTTLVSVEPKLTIETRNRVMKATLGFFALPNDPSDVISPLIDNLVTLLCAILLTSGEDGRSRAEQLLHLLRQLDQYVSSPIDYQRKRGCVAVHEMLLKFRKLCVGGYCALGCSGDCPHRKYADRSMQGNFSNLPSVFLFPDREVLCLGDRVITYLPRCADTNSEVRKISAQILDQFFSISLSLPKAVLTSGLDSEDSYKALSSLEDVIAILKSDASIDPSEVFNRIVSSICSLLTEHELVAALHSCTAAICDKIRQSAEGAIQAVTEFVSRRGSQLSDNDISRTTHSLLSAAVHITDKNLRVEAIGAISALAENTQSSIVFNEVLATAGKDIVTKDITRMRGGWPMQDAFYAFSQHTELSVLFMEHLISILNRSSLVKSDSHKGENTSSSSETHVEDDILQAAIFALTAFFRGGGKIGKKAVEKSYSSVVGALTLQLGSCHGLASSGQQDPLRVLLTSFQAFCECVGDLEMGKILARNGEQIEKEKWVGLIGDIAGCISIKRPKEVRHICMILTKALNRPQRFQREAAAAALSEFIRYSGDFSSVMEEMVEALCRHVSDDSPTVRRLCLRGLVQMPSACMSHYTTQVIGVILALLDDLDESVQLTAVSCLLMVTESASNDAVEPILLNLSVRLRNLQVSMDPKMRANAFSALGALSKYATGGQREGFVEQIHSTLPRLVVHLHDDDPSIRQACRVTLKRFAPLVDIINYSTLYDSRAFGSEDRTDYENFVRDLSKHLVQESERVDTYMASTIQAFDAPWPVIQANAIHFSTTMLSLSEDQHIISLYYPQVFETLVSKMTRSQDSVVRAACSSAFGLLLRSSKSTLWRGARLDGTDSGRKANDLESVKK
The following text describes a protein:
Function:
Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.
Subcellular Localization:
Cytoplasm, cytosol. Peroxisome membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MENRICTLAKPLPKLDESKQAWVSYLWLKKALPGFEEHSAYVYMTTNPTIAGRIFLPINNEDLEDGTVEISGYDNLLADALYISTIAPVKLDFVQLIVIDDNSQDQDAIIERIKGRNAILMESDFINQNILVQVCQPVRHGVVDSETKFVIERKDSFTFLASNEKNISSFKRGKTETDAELVIRPSKVHTEIQWCLQNCSLIHVPFELLFNVGKKNGCPISLRLSDGKNVYGIASIKSDTEHDSVQLSPSLHYFDEFNESVISEEGTEAFLVARGPSVGIASRISLRTIPTQSCFSEKLLKAANLCVVQQVKQKVFLQSKQIFCVPINSLMANSDSVDILELTRNTDAYIWYSVEEIDPLNTYNIYYTNEDTSIVLDTQLSHRLLPSLRKPLLNFVKVHPPSQKLLRFCRAFFDPQQVPGFNPFFLLHGNPFTGKTKAVEEVASLFSAPVFTISSYEFADATADHLEAKLDMFVQNVVKSPCAIIFVKDLDVLSISSDEGNIVPGSKSIQILLSKIDLVKSPQGRYIVIGTCHSIEKIPYEILSESFFELKFSELEMDERLELLKIYANNVIIDKRISLKDVALKTNSMSFGELECLPDHMTKAAVDRIKRTGYDNDSIILSGPIITEQDVDVSINRIRKEKSNTIFTVPKVNWDDIGGLEEAKTVLRDTLQLPLQFPELFSQGLKPRSGVLLYGPPGTGKTLLAKAVATELSLEFVSIKGPELLNMYVGESEANVRNVFEKARNSSPCVIFFDELDSIAPHRGNSSDSGNVMDRVVSQLLAELDSISKDNNKYVFVIGATNRPDLLDPSLLRPGRFDKLVYLGINKSEESKASMLRALTKTFKLDETIDLNEIAKNCHPNFTGADMYALCSDAVLSAIKRKTNEIDLLIQASGTDLSTEEFFKRNENQDSLELRITKEDFLTSLKKLRPSISEQELHRYEMVRHQFS
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane. Mitochondrion membrane; Single-pass membrane protein.
Sequence:
MFGLNRQYLWSVVPLFGFGVGWFLDRKETERMTMFRDKSALYGRTLKEGEKPSWP
The following text describes a protein:
Function:
Error-prone polymerase lacking a proofreading 3'-5' exonuclease which catalyzes the gap-filling reaction during the DNA repair process. Specifically binds intermediates in the single-nucleotide base-excision repair process. Also catalyzes DNA polymerization with low nucleotide-insertion fidelity. Probably acts as a strategic DNA mutase, which gives rise to a rapid emergence of variants. Generates mismatched G-G pairs, in that case, the polymerase first binds the deoxynucleotide followed by mismatch formation. Together with the viral DNA ligase, fills the single nucleotide gaps generated by the AP endonuclease (Probable). Binds DNA with high affinity via the helix alphaE.
Miscellaneous:
MISCELLANEOUS: Consistent with its intracellular location, ASFV encodes its own replicative DNA polymerase and three base excision repair enzymes: a class II AP endonuclease, the repair polymerase Pol X, and an ATP-dependent DNA ligase.
Subcellular Localization:
Virion. Note=Found in association with viral nucleoid.
Domain:
Small DNA polymerase formed from only a palm and a C-terminal subdomain. Unlike other polymerases, binds DNA via the helix alphaE. The total DNA-binding site of pol X is composed of two DNA-binding subsites.
Sequence:
MLTLIQGKKIVNHLRSRLAFEYNGQLIKILSKNIVAVGSLRREEKMLNDVDLLIIVPEKKLLKHVLPNIRIKGLSFSVKVCGERKCVLFIEWEKKTYQLDLFTALAEEKPYAIFHFTGPVSYLIRIRAALKKKNYKLNQYGLFKNQTLVPLKITTEKELIKELGFTYRIPKKRL
The following text describes a protein:
Function:
[Gasdermin-E]: Precursor of a pore-forming protein that converts non-inflammatory apoptosis to pyroptosis. This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-E, N-terminal) binds to membranes and forms pores, triggering pyroptosis; [Gasdermin-E, N-terminal]: Pore-forming protein produced by cleavage by CASP3 or granzyme B (GZMB), which converts non-inflammatory apoptosis to pyroptosis or promotes granzyme-mediated pyroptosis, respectively. After cleavage, moves to the plasma membrane, homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, allowing the release of mature interleukins (IL1B and IL16) and triggering pyroptosis. Binds to inner leaflet lipids, bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate. Cleavage by CASP3 switches CASP3-mediated apoptosis induced by TNF or danger signals, such as chemotherapy drugs, to pyroptosis. Mediates secondary necrosis downstream of the mitochondrial apoptotic pathway and CASP3 activation as well as in response to viral agents. Exhibits bactericidal activity. Cleavage by GZMB promotes tumor suppressor activity by triggering robust anti-tumor immunity. Suppresses tumors by mediating granzyme-mediated pyroptosis in target cells of natural killer (NK) cells: cleavage by granzyme B (GZMB), delivered to target cells from NK-cells, triggers pyroptosis of tumor cells and tumor suppression. May play a role in the p53/TP53-regulated cellular response to DNA damage.
Subcellular Localization:
[Gasdermin-E, N-terminal]: Cell membrane; Multi-pass membrane protein; [Gasdermin-E]: Cytoplasm, cytosol.
Domain:
Intramolecular interactions between N- and C-terminal domains may be important for autoinhibition in the absence of activation signal. The intrinsic pyroptosis-inducing activity is carried by the N-terminal domain, that is released upon cleavage by CASP3 or granzyme B (GZMB).
Sequence:
MFAKATRSFLREVDAEGDLIAVSNLNDSDKSQLLSLVTKKKRFWCWQRPKYQFLSVTLGDVLTEAQCLSPVVVESDFVKYEGKFENHVSGTIETALGKVKLNFGDKGLRESQSSFGTLRKQEVDLQQLIRDSVERTINLKNPVLQQMLESKNEVLCILTQKIVTTQKCVISEHIQTEEKCGGMVGIKTKTVQVSVTKDENIIKDASVALEIPAPTTIAYSVIELYVKLDGQFEFCLLRGKHGGFEHQRRSDIVFPDAGALQDFPFWDVPDAGQGLPTPDGPLSVLKQGTRLLEKNFFPFVELPEQHRTALNTVLQAVLSDEELLAVLEQVCDDLVHSLSPPLAMLGELKPPHRQDLTAFLRLVGYRVQGGCPCLEDGVGSQKLFSTAYFLVSALAEMPDNAAALLGTCCKLQIIPALCHLLHAMSHDGVCDLEDPALAPLKDTERFGVAQRLFASADINLERVQSSVKAVTPLKDPSVLPLILYISLKGLCALGREH
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSNLTPIATYNLALQPFQPVPAIEDDFPISIRITLASLDPEAADDKAEPSSLRILKKSNSLLSDDYFEDDDDDEEEDDEEDELDDEEEEEEAEEEKSSKKSNGKKSSKKDEDEEEDDEEEDDEDNDEDDVSEYIVCTLSPKHQYQQTLDLTITPDEEVYFVVTGSYPIHLTGNYIEHPADQDEEDYDNEDEDYDDEYDLSPDEDEIIYGAPLDDEYDDEEESEEEGTPKIEEIVEEKEKVKESPKESKKRVAEESTSKKSKKAKKDEKKSVQFSKELEQGPTGSTLVEKDNKKATPTKDKKETPVKDDGDKKKKFPTKTLLGGVITEDRKIGSGATAKSGAKVGIRYIGKLKNGKVFDKNTSGKPFSFKLGKGECIKGFDLGVTGMAVGGERRVIIPPKMGYGSQALPGIPANSELTFDIKLVSLK
The following text describes a protein:
Function:
Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde).
Sequence:
MRFSANISWLFPEVPDFPGRIKAASQSGFRAVEVAWPYATDRTLFKAALNTHRMSLVLLNTPPGNIEAGELGLAAVPGRQDEFRTGLNEAVSWASDLGCDRIHIMAGRVPLGLEHQFIEKEMEETFIENLQYAADILGQAGMVGLLEPINSLITEPRYFLNTPQHVCYFLAASILQKVKRPNLKLQMDLYHWQIMGGNLTQNIKTYFPLIGHVQIAQIPHRNEPDSPGELNFMYLFDLLQDLGYQGYVGCEYKPQGDTVKGLGWMEKYLKNCDGDEDKTK
The following text describes a protein:
Function:
Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand.
Sequence:
MNLILVLVLVLVLVLVLVYVIKDKLDIRRTLEEEARKCQWLVLWLDCDREGENIAYEVVEVCLNVNSHLNIWRARFSSLIDREIHQAAQQLARPNQLFSEAVDVRQEIDLRIGASFTRFQTMLLKDAFDFNFSTDGRNLILSYGPCQFPTLGFVVERYWEIQAHEPEEFWKIQCSHTTDEGTANFNWMRGHLFDYTCAVLLYEMCFEEPIATVTKVRKQEKLKYPPHPLNTIELEKRASRYFRMSSEQTMKIAEDLYQSGFISYPRTETDSFSTRTDLHILVQEQQEHPVWGPYAQRLLDPSSGLWRNPSGGGHDDKAHPPIHPTKFSAGESRWSEDHKKLYELVVRHYLACVSQPAVGAETTVEIDIAGEMFSALGRTIVAKNYLEVYRFESWGGSLIPNYTFGQQFTPTSLTLESGITRPPPLLSESDLLDYMDKAGIGTDATMHDHIKKLTDRFYAIKEGSHFKPTNLGEALVMGYDDMGYELWKPYLRSMMEEDMKAVSIGNKRKDDVLATCLQQMKACFLDARVNKTKLFQALEIFFDRTNRTTGGDDQHNHAQQLVRKCDVCHDSDLVLRKKPDGKFMIGCSGYPQCRNVIWLPGSISEAVVTTTVCNMCTPGPVFKIQFTFRRLEIPPNFNVHHLGCVGGCDDIMRQLIEMSGSGQRNTSSTPARGRGIAAPSRNDSRNNNNNQQQLQQATCSFCHQTGHNSSDCYSLTSQNRSARSQRVNSNSGDSPIPCPTCGSLCVLKTANTESNRGRKFYSCQTQGCKFFVCWEDSVPTTRGGGSGSATTTSRRGGRGGGRGGGGGQGGGDVRFVSATGDPVSGRSCFICGDPSHFANACPNRGMRN
The following text describes a protein:
Function:
Acetylates the N-terminal alanine of ribosomal protein bS18.
Subcellular Localization:
Cytoplasm.
Sequence:
MSDAISFRPMTEADLDAVLKIEYAAFSHPWTRGIFSEGLKNYHCWLMFEGSQQVGHGVIQIILDEAHLLNITVKPESQGRGLGLRLLEHLMREAAGHQARECFLEVRASNQAAYRLYERYGFNEIGRRRDYYPAVGGREDALVMACTLFD
The following text describes a protein:
Function:
Retinoids dehydrogenase/reductase with a clear preference for NADP. Displays high activity towards 9-cis, 11-cis and all-trans-retinal. Shows very weak activity towards 13-cis-retinol. Also exhibits activity, albeit with lower affinity than for retinaldehydes, towards lipid peroxidation products (C9 aldehydes) such as 4-hydroxynonenal and trans-2-nonenal. May play an important function in photoreceptor cells to detoxify 4-hydroxynonenal and potentially other toxic aldehyde products resulting from lipid peroxidation. Has no dehydrogenase activity towards steroids.
Miscellaneous:
MISCELLANEOUS: Shows clear specificity for the pro-S hydrogen on C4 of NADPH and the pro-R hydrogen on C15 of retinols.
Sequence:
MLVVLGLLTSFLSFLYVIAPSIRKFFAGGVCRTDVQLFGKVVVITGANTGIGKETARELARRGARVYIACRDVLKGESAASEIQADTKNSQVLVRKLDLSDTKSIRAFAEGFLAEEKQLHILINNAGVMLCPYSKTADGFETHLAVNHLGHFLLTHLLLGRLKESAPARVVNLSSVAHHLGKIRFHDLQGDKYYNLGFAYCHSKLANVLFTRELAKRLKGTGVTTYAVHPGIVRSKLVRHSFLLCLLWRLFSPFLKTTWEGAQTSLHCALAEGLEPLSGKYFSDCKKTWVSPRARNNKTAERLWNVSCELLGIRWE
The following text describes a protein:
Function:
Plays a role in the arabinosylation of cell wall components. Involved in the arabinosylation of extensin proteins in root hair cells. Extensins are structural glycoproteins present in cell walls and its arabinosylation is important for root hair cell development.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Domain:
The conserved DXD motif is involved in enzyme activity.
Sequence:
MAGRRDRIQQLRGSRIAIAIFVGILIGCVCSVLFPNGFFNSGSSLIANEERISKSTSTDGLASCESSERVKMLKSDFSIISVKNAELRKQVRELTEKVRLAEQETENARKQVLVLGSEIKAGPFGTVKSLRTNPTVVPDESVNPRLAKLLEKVAVNKEIIVVLANSNVKPMLELQIASVKRVGIQNYLIVALDDSMESFCESKEVVFYKRDPDKAVDMVGKSGGNHAVSGLKFRVLREFLQLGYSVLLSDVDIVFLQNPFSHLHRDSDVESMSDGHDNNTAYGFNDVFDEPSMGWARYAHTMRIWVFNSGFFYLRPTIPSIDLLDRVADTLSKSEAWDQAVFNEQLFYPSHPGYTGLHASKRVMDMYEFMNSKVLFKTVRKNQELKKLKPVIVHLNYHPDKLERMHAVVEFYVNGKQDALDSFPDGSD
The following text describes a protein:
Function:
Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MFFPFMFGIMFGDIGHGGVLFVLAFLLVKNADTLKKLPDFAALVQVRYLFLLMGLCALYCGIIYNDFMSLTWNIFGSCFENVPDSEETVYIKGCTYPIGFDPKWYIASNELNFFNSFKMKFAIIYGVSQMIFGILLKGVNNLYFKDYLSFICEFLPQLIFMCITFGYMGVMIMLKWGQSWEGRTDQAPSIINAMINIPLQGGSTEGKPLFDLESQESLQQSILFWSFLCIPWMLLPKPIVEVIQHYSGKEHEKKPSKALEPKDESKEALLPVQSSQKSINQSALAEELRLQLIQKEKEKEQRRKQLEEQRLKEQVAEEDLQNDQPQKLLPKQPEKTGEHGHGHDEFDIGELAVHQIIETIEFVLGSISNTASYLRLWALSLAHGQLAKVFFEKCIGAGIEDGNVIVLVIGWPVFLHCTIGVLMCMDLMECFLHALRLQWVEFQSKFYKADGIKFMPFSFKEVLTNQPKDQ
The following text describes a protein:
Function:
Plays a role in innate immunity limiting microbial proliferation in the gut. Acts downstream of a hh-signaling pathway to induce the production of reactive oxygen species (ROS) in response to intestinal bacterial infection. May generate antimicrobial oxidative burst through its peroxidase-like domain.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSVPSAPHQRAESKNRVPRPGQKNRKLPKLRLHWPGATYGGALLLLLISYGLELGSVHCYEKMYSQTEKQRYDGWYNNLAHPDWGSVDSHLVRKAPPSYSDGVYAMAGANRPSTRRLSRLFMRGKDGLGSKFNRTALLAFFGQLVANEIVMASESGCPIEMHRIEIEKCDEMYDRECRGDKYIPFHRAAYDRDTGQSPNAPREQINQMTAWIDGSFIYSTSEAWLNAMRSFHNGTLLTEKDGKLPVRNTMRVPLFNNPVPSVMKMLSPERLFLLGDPRTNQNPAILSFAILFLRWHNTLAQRIKRVHPDWSDEDIYQRARHTVIASLQNVIVYEYLPAFLGTSLPPYEGYKQDIHPGIGHIFQAAAFRFGHTMIPPGIYRRDGQCNFKETPMGYPAVRLCSTWWDSSGFFADTSVEEVLMGLASQISEREDPVLCSDVRDKLFGPMEFTRRDLGALNIMRGRDNGLPDYNTARESYGLKRHKTWTDINPPLFETQPELLDMLKEAYDNKLDDVDVYVGGMLESYGQPGEFFTAVIKEQFQRLRDADRFWFENERNGIFTPEEIAELRKITLWDIIVNSTDVKEEEIQKDVFMWRTGDPCPQPMQLNATELEPCTYLEGYDYFSGSELMFIYVCVFLGFVPILCAGAGYCVVKLQNSKRRRLKIRQEALRAPQHKGSVDKMLAREWLHANHKRLVTVKFGPEAAIYTVDRKGEKLRTFSLKHIDVVSVEESATNHIKKKPYILLRVPSDHDLVLELESYGARRKFVKKLEDFLLLHKKEMTLMEVNRDIMLARAETRERRQKRLEYFFREAYALTFGLRPGERRRRSDASSDGEVMTVMRTSLSKAEFAAALGMKPNDMFVRKMFNIVDKDQDGRISFQEFLETVVLFSRGKTDDKLRIIFDMCDNDRNGVIDKGELSEMMRSLVEIARTTSLGDDQVTELIDGMFQDVGLEHKNHLTYQDFKLMMKEYKGDFVAIGLDCKGAKQNFLDTSTNVARMTSFNIEPMQDKPRHWLLAKWDAYITFLEENRQNIFYLFLFYVVTIVLFVERFIHYSFMAEHTDLRHIMGVGIAITRGSAASLSFCYSLLLLTMSRNLITKLKEFPIQQYIPLDSHIQFHKIAACTALFFSVLHTVGHIVNFYHVSTQSHENLRCLTREVHFASDYKPDITFWLFQTVTGTTGVMLFIIMCIIFVFAHPTIRKKAYNFFWNMHTLYIGLYLLSLIHGLARLTGPPRFWMFFLGPGIVYTLDKIVSLRTKYMALDVIDTDLLPSDVIKIKFYRPPNLKYLSGQWVRLSCTAFRPHEMHSFTLTSAPHENFLSCHIKAQGPWTWKLRNYFDPCNYNPEDQPKIRIEGPFGGGNQDWYKFEVAVMVGGGIGVTPYASILNDLVFGTSTNRYSGVACKKVYFLWICPSHKHFEWFIDVLRDVEKKDVTNVLEIHIFITQFFHKFDLRTTMLYICENHFQRLSKTSIFTGLKAVNHFGRPDMSSFLKFVQKKHSYVSKIGVFSCGPRPLTKSVMSACDEVNKTRKLPYFIHHFENFG
The following text describes a protein:
Function:
Transcription activator that plays a role in the regulation of cell expansion in leaf and cotyledons tissues. Component of a network formed by miR396, the GRFs and their interacting factors (GIFs) acting in the regulation of meristem function, at least partially through the control of cell proliferation. microRNA396-GRF1/GRF3 regulatory module acts as a developmental regulator in the reprogramming of root cells during cyst nematode infection, leading to the formation of the syncytium.
Subcellular Localization:
Nucleus.
Domain:
The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence:
MDLQLKQWRSQQQQQHQTESEEQPSAAKIPKHVFDQIHSHTATSTALPLFTPEPTSSKLSSLSPDSSSRFPKMGSFFSWAQWQELELQALIYRYMLAGAAVPQELLLPIKKSLLHLSPSYFLHHPLQHLPHYQPAWYLGRAAMDPEPGRCRRTDGKKWRCSRDVFAGHKYCERHMHRGRNRSRKPVETPTTVNATATSMASSVAAAATTTTATTTSTFAFGGGGGSEEVVGQGGSFFFSGSSNSSSELLHLSQSCSEMKQESNNMNNKRPYESHIGFSNNRSDGGHILRPFFDDWPRSSLQEADNSSSPMSSATCLSISMPGNSSSDVSLKLSTGNEEGARSNNNGRDQQNMSWWSGGGSNHHHHNMGGPLAEALRSSSSSSPTSVLHQLGVSTQAFH
The following text describes a protein:
Function:
NodD regulates the expression of the nodABCFE genes which encode other nodulation proteins. NodD is also a negative regulator of its own expression. Binds flavonoids as inducers.
Sequence:
MELHQLRCFVAAAEQLHFGHAAQQLQMLPSALGRQIRLLEEDLGTRLFARTTRAVSLTEDGATLLRDARAILARVEAVENNLRNRSRAGAARRLRVGAIDSAAAGLLPPLLRDFRDKHPDIAVQLLEDKTVRLLPKILTGALDLAFVRPPDSADKRLEFRDLLQETAIVAFPQRHALAERKSITLAQIADEAMLVPDRRSRPHSHDLTIKLFEQAGLTPRIVQVADEKQTIIHLVATKLGVAIVPRWTTRMAVSGVRFVPLRPKQSGPVGRLPLAAAWLRGSRDPARDAMLAVLEARLRSYAREA
The following text describes a protein:
Function:
Transcription factor, is involved in craniofacial development, and in stomach organogenesis.
Subcellular Localization:
Nucleus.
Sequence:
MQHPLEIGAHYYPPDAHLDQRSHRYRSFMIEEILTDHPDQKISSPTGDLLKFGVHALLSARPYHNHLVLKADQTGILKFPVSPLSCSLGAPLSSALLSGAAGLQVGSSSHHLPLDLHLRGKLDPGADAVSKTKKGRRSRTVFTELQLMGLEKRFEKQKYLSTPDRIDLAESLGLSQLQVKTWYQNRRMKWKKIVLQGGGLESPTKPKGRPKKNSIPTSEQLSEQERTREADRLSDGGASSLSDANQEE
The following text describes a protein:
Function:
Involved in tracheal paracellular barrier functions mediated by epithelial cell septate junctions. Involved in paracellular barrier functions mediated by glial cell septate junctions in the peripheral nervous system, including the chordotonal organs, but not the hemolymph-brain barrier (the insect blood-brain barrier) of the central nervous system. Required for septate junction assembly, possibly by organizing the preassembly and transport of septate junction proteins such as dlg1/disks large 1, Nrx-IV/Neurexin-IV and the claudin protein kune. Involved in chitin fiber organization during tracheal development. Secreted, possibly in association with extracellular vesicles, to act non-autonomously on tissues distant from its site of expression.
Miscellaneous:
MISCELLANEOUS: 'Boudin' is an Anglo-Norman word meaning 'sausage' (specifically blood sausage) or 'entrails'. Mutant larvae exhibit developmental defects resulting in an abnormal tracheal network structure with the dorsal trunk adopting bulging cysts resembling a string of sausages.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Cell junction, septate junction. Cytoplasm, cell cortex. Secreted. Apicolateral cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Note=Accumulates in the apical cell cortex, possibly associated with secretory vesicles. Cell membrane localization includes, but is not restricted to, the septate junction region. The secreted form, potentially associated with extracellular vesicles called 'boudosomes' via its GPI-anchor, diffuses through the extracellular space and is endocytosed by distant cells and incorporated into their cell membrane, where it co-localizes with septate junctions.
Domain:
The C-terminal transmembrane domain, directly involved in membrane association or indirectly through facilitating GPI-anchorage, is required for autonomous activity in cells expressing bou/boudin and non-autonomous activity on remote tissues. This region is required for exit from the endoplasmic reticulum.
Sequence:
MWPPKHAHIGWLSSLALVVLLMSLQMVMVSGIECYVCDTSDTEHPFQCGEWFERYDIPDIQPQNCSSVHGAQFCVKHVGRFEGGIGAKRFCSSKDMGNYCDYVRNKGDRMDYRSCIYTCDTDGCNAAGRLELEWGVAAALLTLTWLLRH