lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles. Plays a role in the trafficking of clathrin between the Golgi network and endosomes. Binds to membranes enriched in phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) and, in association with VPS27, is involved in protein sorting at the multivesicular body (MVB).
Miscellaneous:
MISCELLANEOUS: Present with 8100 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Endosome membrane; Peripheral membrane protein. Note=Found predominantly on endosomal structures.
Sequence:
MDSLSKKIQNLGIHDIRNAARFAQNVIVQYEPYQIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLYLMTEYTLKRLVDHIATRPKNLYEKARKDYVNYGSEWRVVLKCLVVIEFLLLNVDTGDELNQIRSCLLTHKHILTREIAQFKVKFSNDGKMEIHERGIRKKGELILQYLEDSQFLKKERAKNKKNALKIRQQGESSIYNANQISTSASYDNIDDDEFDADADGFDSEMDANNVTNFNVPVETEANSNTRRRSHMEEQRRQRREILREQIKNKEQQRKRKQQQDSIPDLIDLDDSTSTTNNITIDNGNNDNKNNNINSNSDDDDDEFGDFQSETSPDTTAPKTSNSKIDDLLDWDGPKSDTDTTAAAQTSLPFAEKKQQKARPQATKDKSKGNDAFSDLFSYSKSLV
The following text describes a protein:
Function:
Resistance to the epoxide antibiotic methylenomycin A; probably by mediating its efflux.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTTVRTGGAQTAEVPAGGRRDVPSGVKITALATGFVMATLDVTVVNVAGATIQESLDTTLTQLTWIVDGYVLTFASLLMLAGGLANRIGAKTVYLWGMGVFFLASLACALAPTAETLIAARLVQGAGAALFMPSSLSLLVFSFPEKRQRTRMLGLWSAIVATSSGLGPTVGGLMVSAFGWESIFLLNLPIGAIGMAMTYRYIAATESRATRLAVPGHLLWIVALAAVSFALIEGPQLGWTAGPVLTAYAVAVTAAALLALREHRVTNPVMPWQLFRGPGFTGANLVGFLFNFALFGSTFMLGLYFQHARGATPFQAGLELLPMTIFFPVANIVYARISARFSNGTLLTAFLLLAGAASLSMVTITASTPYWVVAVAVGVANIGAGIISPGMTAALVDAAGPENANVAGSVLNANRQIGSLVGIAAMGVVLHSTSDWDHGAAISFLAVGLAYLLGGLSAWRLIARPERRSAVTAAT
The following text describes a protein:
Function:
Plays a role in pre-mRNA splicing by facilitating excision of introns featuring long spacing between the branchpoint and 3'-splice site (ss). Recruited to the spliceosome by sde2, which may enable folding of the RNA between the BP and 3'-ss to guide the splice site towards the spliceosome's catalytic center. Assists the splicing of several components involved in chromatin organization.
Sequence:
MAFRDSTRDFNRSRPEKRHASRSSSPRSFRPSNQNARANYNLPRVRDAMKEEERSRETKEMQEREFLRLQQLRRAIIRLKNDRSKPIDKLLVSVYLMPGPEWEENGEKNSIDFGTVDMFDPLSVIQSYKAEDLEEISRNIGDIQQLETNQCRLTYWKYVKMLVNSRMEHNKVGQFSRGLKVVAGEVQRILAPKSFEQLEQLEAQIQKKLKSNVPLDTDYWVDLLNSLKSYKAIAYLKKTFNEELQIRKNKLDNEEWDKAFSDAKKLSNMKDREEKLYIVPIDPKPILRAQAIPRRIQPEEQADYEKELNDHVNIVKSSTYIPISIPTQKQKPTLPKNSNLINEDEFSIANRARLEREYLQSDDAEEQEMLGDYVEGQTRVVNENGVTLKKPHYFNRVLLGFEWNSYNQAHFNEAHPPPKAVQGYRFNVFYPDLIGTGRAPTYRIERTRRKNKSDTTDLQDDVCIIRFIAGEPYQDIAFSIVDKDWDYSAKRDHGFKSSFDNGVLSLHFRFKKLHHRR
The following text describes a protein:
Function:
Involved in the biosynthesis of the Lewis X (LeX) trisaccharide of the lipopolysaccharide (LPS) O-antigen. Catalyzes the addition of fucose in alpha 1-3 linkage to Gal-beta-1-4-GlcNAc-beta-O-R (LacNAc-R) type II acceptor.
Subcellular Localization:
Membrane; Peripheral membrane protein. Cytoplasm. Note=Predominantly localizes at the membrane.
Domain:
The tandem repeat region, which may form a leucine zipper structure, is essential for dimerization as well as for enzyme stability.
Sequence:
MFQPLLDAYVESASIEKMASKSPPPLKIAVANWWGDEEIKEFKNSVLYFILSQRYTITLHQNPNEFSDLVFGNPLGSARKILSYQNAKRVFYTGENESPNFNLFDYAIGFDELDFNDRYLRMPLYYDRLHHKAESVNDTTAPYKLKDNSLYALKKPSHCFKEKHPNLCAVVNDESDPLKRGFASFVASNPNAPIRNAFYDALNSIEPVTGGGSVRNTLGYNVKNKNEFLSQYKFNLCFENTQGYGYVTEKIIDAYFSHTIPIYWGSPSVAKDFNPKSFVNVHDFKNFDEAIDYIKYLHTHKNAYLDMLYENPLNTLDGKAYFYQNLSFKKILAFFKTILENDTIYHDNPFIFCRDLNEPLVTIDDLRVNYDDLRVNYDDLRINYDDLRVNYDDLRINYDDLRVNYDDLRVNYDDLRINYDDLRVNYDDLRVNYERLLSKATPLLELSQNTTSKIYRKAYQKSLPLLRAIRRWVKKLGL
The following text describes a protein:
Function:
Phosphatase with a broad specificity. Can dephosphorylate a variety of substrates including phosphorylated sugars like fructose-6-phosphate (F6P). Is able to function in vivo as a fructose-1,6-bisphosphatase (FBPase) and to maintain gluconeogenesis when the classical FBPase GlpX is absent. Shows negligible phosphoglycerate mutase activity. Has no phosphatase activity against 3-phosphoglycerate, 2,3-bisphosphoglycerate, or hydrophobic substrates such as alpha-napthyl phosphate.
Miscellaneous:
MISCELLANEOUS: Gluconeogenesis is critical to M.tuberculosis ability to establish infection and is necessary for its survival in the host.
Sequence:
MGVRNHRLLLLRHGETAWSTLGRHTGGTEVELTDTGRTQAELAGQLLGELELDDPIVICSPRRRTLDTAKLAGLTVNEVTGLLAEWDYGSYEGLTTPQIRESEPDWLVWTHGCPAGESVAQVNDRADSAVALALEHMSSRDVLFVSHGHFSRAVITRWVQLPLAEGSRFAMPTASIGICGFEHGVRQLAVLGLTGHPQPIAAG
The following text describes a protein:
Function:
Plays a critical role in homologous recombination repair (HRR) through its ability to recruit BRCA2 and RAD51 to DNA breaks. Strongly stimulates the DNA strand-invasion activity of RAD51, stabilizes the nucleoprotein filament against a disruptive BRC3-BRC4 polypeptide and helps RAD51 to overcome the suppressive effect of replication protein A (RPA). Functionally cooperates with RAD51AP1 in promoting of D-loop formation by RAD51. Serves as the molecular scaffold in the formation of the BRCA1-PALB2-BRCA2 complex which is essential for homologous recombination. Via its WD repeats is proposed to scaffold a HR complex containing RAD51C and BRCA2 which is thought to play a role in HR-mediated DNA repair. Essential partner of BRCA2 that promotes the localization and stability of BRCA2. Also enables its recombinational repair and checkpoint functions of BRCA2. May act by promoting stable association of BRCA2 with nuclear structures, allowing BRCA2 to escape the effects of proteasome-mediated degradation. Binds DNA with high affinity for D loop, which comprises single-stranded, double-stranded and branched DNA structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with BRCA2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity (By similarity).
Subcellular Localization:
Nucleus. Note=Colocalizes with BRCA2 in nuclear foci.
Domain:
Interaction with BRCA2 occurs through a hydrophobic pocket at the crossover between WD repeats 4 and 5; The coiled coil domain mediates self-association; The chromatin-association motif (ChAM) mediates association with chromatin, probably through nucleosome core particles, independently from binding to D loop, ssDNA or dsDNA structures.
Sequence:
MEELSGKPLSYAEKEKLKEKLAFLKKEYSRTLARLQRAKRAEKAKNSKKAIEDGVPQPEASSQLSHSESINKGFPCDTLQSNHLDEETGENISQILDVEPQSFNCKQGKEVLHTPRAGDIQGQLLHSTSSPDGKKEQNTLPGTTKTPWEKSSVSQEKEDYFDTNSLALLGKHRKGQESISRKNSRTPVSEKTHLLSLRSQIPDPPALVTGIGEGILIPPSGKSERGIDTLVRGNTVSAEAAVPSCTASNSNHSQHLEHTPPKSGCKITTQGPASSTNLVAQDQKMTIFTVNSVVYKAVRAHGQLPGSPNSCSVNDLTHSNLPANSTPNSKSLKSPSNTVDERNEPLQEDEILGPSKNFNLAAVSPPSTESQIHSCTMLEGLLFPAEYYVRTTRRMSDCQRKIALEAVIQSHLGVKKKELKKKTKATKAVVLSSEDTDQSESGMLDTSTGQSSSGSLSQKLLSPAEVSSPPGPAGKATTPPPGRGHRGKRKSARTSTLGHCQLLFPPCAALAVNRSKGKFTKHKCQNRGVVIHDFELPDEDFGLLKLEKLKSCSEKLIESPDSKNCGERLPREGNHAALEELQRDSETEGLEEELTVPPGEAYRPGPTLRRQPGSKDLSSSIVLFTPADTAAPNDSGRPPPSLCSPAFPILGMTPALGSQAAGETLSTEAAQPCSTSQPPLLGDTNSLVNNSKQCNSSACSPKPDTNLQASGRQGQPACDSDSGPQATPLPVESFTFRENQLCGNACLELHEHSTEQTETADRPACDNLNPGNLQLVSELKNPSSSCSVDVSAMWWERAGAKEPCIVTACEDVVSLWKPLNSLQWEKVHTWHFTEVPVLQIVPVPDVYNLICVALGSLEIREIRALLCSSGDDSEKQVLLKSGDIKAMLGLTKRRLVSSTGTFCNQQIQIMTFADDGSSKDEQLLMPPDETVLTFAEVQGTQEALLGTTTVNSIVIWNLKTGQLLKKMHIDDSYQASVCHGAYSEKGLLFVVVSQPCAKESQALGSPVFQLLVINPKTAQSVGVLLCSLPQGQAGRFLEGDVKDHVAAAVLTSGTIAIWDLLLGHCTALLPPVSDQSWSLVKWSGTDSHLLAGQKDGNIFIYRYF
The following text describes a protein:
Function:
Disease resistance (R) protein that specifically recognizes the AvrRpm1 type III effector avirulence protein from Pseudomonas syringae. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response (HR), which restricts the pathogen growth. Acts via its interaction with RIN4, and probably triggers the plant resistance when RIN4 is phosphorylated by AvrRpm1. It is then degraded at the onset of the hypersensitive response.
Subcellular Localization:
Endomembrane system; Peripheral membrane protein. Cell membrane; Peripheral membrane protein.
Domain:
The LRR repeats probably act as specificity determinant of pathogen recognition.
Sequence:
MASATVDFGIGRILSVLENETLLLSGVHGEIDKMKKELLIMKSFLEDTHKHGGNGSTTTTTQLFQTFVANTRDLAYQIEDILDEFGYHIHGYRSCAKIWRAFHFPRYMWARHSIAQKLGMVNVMIQSISDSMKRYYHSENYQAALLPPIDDGDAKWVNNISESSLFFSENSLVGIDAPKGKLIGRLLSPEPQRIVVAVVGMGGSGKTTLSANIFKSQSVRRHFESYAWVTISKSYVIEDVFRTMIKEFYKEADTQIPAELYSLGYRELVEKLVEYLQSKRYIVVLDDVWTTGLWREISIALPDGIYGSRVMMTTRDMNVASFPYGIGSTKHEIELLKEDEAWVLFSNKAFPASLEQCRTQNLEPIARKLVERCQGLPLAIASLGSMMSTKKFESEWKKVYSTLNWELNNNHELKIVRSIMFLSFNDLPYPLKRCFLYCSLFPVNYRMKRKRLIRMWMAQRFVEPIRGVKAEEVADSYLNELVYRNMLQVILWNPFGRPKAFKMHDVIWEIALSVSKLERFCDVYNDDSDGDDAAETMENYGSRHLCIQKEMTPDSIRATNLHSLLVCSSAKHKMELLPSLNLLRALDLEDSSISKLPDCLVTMFNLKYLNLSKTQVKELPKNFHKLVNLETLNTKHSKIEELPLGMWKLKKLRYLITFRRNEGHDSNWNYVLGTRVVPKIWQLKDLQVMDCFNAEDELIKNLGCMTQLTRISLVMVRREHGRDLCDSLNKIKRIRFLSLTSIDEEEPLEIDDLIATASIEKLFLAGKLERVPSWFNTLQNLTYLGLRGSQLQENAILSIQTLPRLVWLSFYNAYMGPRLRFAQGFQNLKILEIVQMKHLTEVVIEDGAMFELQKLYVRACRGLEYVPRGIENLINLQELHLIHVSNQLVERIRGEGSVDRSRVKHIPAIKHYFRTDNGSFYVSLSS
The following text describes a protein:
Function:
Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins.
Subcellular Localization:
Nucleus.
Sequence:
MSSFKDWALQYVLSDDETAQSEIAKKAAKEIENTRASSASVGSWAASIQPWITITKQDDDQSDDDDDDSGTGDIIARAKALGFLADTLEALDKSLLRPEQVIRLVGFFGAMFSYDHKAGITASAKALRQLHAMKGFKPAVGVKMIEDVCKLKEDFKLQTAATRFEIYELFLSLIQDQSVNNELQDKYGTSSGFIVEILQLCQNERDPRNLMLWFKLLPIFLTEYSTSDEVTEEIFKAFSAYFPITLRNSASPIGITADDLKNAVRACFASHYKVAKLAFPFLIGKLDQGDAVTVSVKLDILKTIKACIEQYDNPQTSIVPHINKIWNSLKYEVRNGEVKETIDATLDVLRAIANRLDGTSTQKFDVSLLKNYIDTVVDDCRDDLANPTYTKQAGLLLMTVITTNIRAYTLESAAFVDIIRKNLRLPKSPSHTKDLLLLLNSTLKSRADLFKNRKQGHPEDEEAFKTEPSDHLVALYHDVYLPIWTGKSEETTPEVLKQVVQGLASLATQQTLRPDGQISLLVSRSVCSEICSLLTHTLTKGLALSQNDNSTDAAVEDEAVLALQAVVATYTDGYAELVERAKAEIEKRDWTSPTKYTLNALRDILSRLAFIGCSRIPLNVALDGESPKTFKPLQHFLKLATTLHDLFPLSPLPTSEKESLANSYIISALHGGILHFRDACFEKFEPKVLEAYSGSDRNWLEEFKGLSKDWLHQLQREDGSSEVVIEEDDPEVYREFLRICLFIVRHLYREAAYGKQAPWSERVFAQAANLAALVVRSLDENLQKSCNLAQNAFNFFSPENLSPSGPSSIAPFRKLLILGILQGLRPAAMAELYAPQGIAETFICDTSRMATVLLAVGEIRGTICAVLANKYKGGQSTFDPESETMKRVLNFWGEQIKTATTTDDTDPAIFEVYNTVAMHTLAGACARQDKNVLALVPILHEAIASPGPNGAIVARTIGGLVKTNELLSPENHAVVKRFYKQWAYTHFAKPLYDLALPTGDEDTAFAAGRYTTAILSLVSNCPFEVYQEDLSHLVRLLITALNNSSVSGDITQPQVATSLEVLVEILANEPEALKGHLKAIITAGMKTYEEAAKNTSKGNVARALAAVRKLTLQLLGAIPKKFEERHLLAYALPMQRMLATASGDKSREARKVALLARENWAKVV
The following text describes a protein:
Function:
Plays a role in the regulation of glomerular permeability, acting probably as a linker between the plasma membrane and the cytoskeleton.
Subcellular Localization:
Membrane.
Sequence:
MEKRSRSSSRESPKQNRSPPRKNKRGKSDKKDQRNGRDTEQEKQNSKKRKGKEDTDNVTLIETDNRIQTSTVVDVDDVMGSLEDETEVMALFESEQQEEGIKSSHLGMCEWLLIILSLLLIVATFPVSIWFCIKVVREYERVIIFRLGHLLPGRARGPGLFFFLPCLDTYHKVDLRLQTLEIPFHEVVTKDMLIMELDAICYYRMENASLLLSNLAQVSKAVQLLVQITMKRLLAHRSFTEILLERKSIAQDTKVALDAITCRWGIKVERTEIKDVRLPAGLQQSLAIEAEAQRQAKVRMIAAEGEKAASESLRMAAEILSGSPAAVQLRYLHTLQSLSTEKPSTVILPLPFDLMNLLPPAGNRMQGSLPLPNPPRQAETRDPSKKDSPML
The following text describes a protein:
Function:
Substrate-specific adapter of the anaphase promoting complex/cyclosome (APC/C) complex that confers substrate specificity by binding to substrates and targeting them to the APC/C complex for ubiquitination and degradation. Recognizes and binds the destruction box (D box) on protein substrates. Involved in the metaphase/anaphase transition of cell cycle. Is regulated by MAD2L1: in metaphase the MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the CDC20-APC/C binary complex is active in degrading substrates. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces presynaptic differentiation. The CDC20-APC/C complex promotes proper dilation formation and radial migration by degrading CCDC41.
Sequence:
MAQFLFESDLHGLLKLDAPIPNAPPARWQRKAKEAAATSMGSVPDVTAPSPMKPANRPRSTSKTPSKTPGKSSSKGQNTPSKTGGDRYIPNRSAMQMDVANFLLTKEDSSDETPTKKEHQKAWAMNLNGFDVEEAKVLRLSGKPQNAPEGYQNNLKVLYSQKNTPGSTRKNTRYISSMSDRILDAPDIRNDYYLNLIDWSSLNFLAVALDKTLYLWHYDSREIIQLLQLEHPDDYISSVSWIKEGNYLAIGTSNAEVQLWDIQHNKRLRNMVSHSSRVSSLSWNNYILSSGSRTGHIHHHDVRVAQHHVATLAGHTQEVCGLKWAPDGRYLASGGNDNLVNIWPATQGDSASLHPVQTFTQHQGAVKAVAWSPWQSNVLATGGGTSDRHIRIWNICSGTCLNEVDAQSQVCAVLWSTNYKELVSAHGFAQNQLVVWKYPSMSKVIELKGHTARVLSLTMSPDGSTVASAAADETLRLWRCFELDPTKKKEKDSNTKSSIIHQGIR
The following text describes a protein:
Function:
Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking.
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, ruffle. Note=Localizes to microtubule plus ends. Localizes preferentially to the ends of tyrosinated microtubules. Accumulates in plasma membrane regions with ruffling and protrusions. Associates with the membranes of intermediate macropinocytic vesicles (By similarity).
Domain:
Intramolecular interaction between the zinc finger domain and the CAP-Gly domains may inhibit interaction with tubulin.
Sequence:
MSMLKPSGLKAPTKILKPGSTALKTPAAAAAPVEKTIPSEKASGPPSSETQEEFVDDFRVGERVWVNGNKPGFIQFLGETQFAPGQWAGIVLDEPIGKNDGSVAGVRYFQCEPLKGIFTRPSKLTRKVQAEDEANGLQAAPGRTASPLSTAAATMVSSSPATPSNIPHKPSQSTAKEPSATPQISNLTKTASESISNLSEAGSVKKGERELKVGDRVLVGGTKAGVVRFLGETDFAKGEWCGVELDEPLGKNDGAVAGTRYFQCQPKYGLFAPVHKVTKIGFPSTTPAKAKAAAVRRVMAATPASLKRSPSASSLSSMSSVASSVSSKPSRTGLLTETSSRYARKISGTTALQEALKEKQQHIEQLLAERDLERAEVAKATSHVGEIEQELALARDGHDQHVLELEAKMDQLRTMVEAADREKVELLNQLEEEKRKVEDLQFRVEEESITKGDLEVATVSEKSRIMELEKDLALRAQEVAELRRRLESSKPPGDVDMSLSLLQEISALQEKLEAIHTDHQGEMTSLKEHFGAREEAFQKEIKALHTATEKLSKENESLRSKLDHANKENSDVIALWKSKLETAIASHQQAMEELKVSFSKGIGTDSAEFAELKTQIERLRLDYQHEIESLQSKQDSERSAHAKEMETMQAKLMKIIKEKEDSLEAVKARLDSAEDQHLVEMEDTLNKLQEAEIKVKELEVLQAKYTEQSEVIGNFTSQLSAVKEKLLDLDALRKANSEGKLELETLRQQLEGAEKQIKNLETERNAESSKANSITKELQEKELVLTGLQDSLNQVNQVKETLEKELQTLKEKFASTSEEAVSAQTRMQDTVNKLHQKEEQFNVLSSELEKLRENLTDMEAKFKEKDDREDQLVKAKEKLENDIAEIMKMSGDNSSQLTKMNDELRLKERSVEELQLKLTKANENASFLQKSIGEVTLKAEQSQQQAARKHEEEKKELEEKLLELEKKMETSYNQCQDLKAKYEKASSETKTKHEEILQNLQKMLADTEDKLKAAQEANRDLMQDMEELKTQADKAKAAQTAEDAMQIMEQMTKEKTETLASLEDTKQTNARLQNELDTLKENNLKTVEELNKSKELLSVENQKMEEFKKEIETLKQAAAQKSQQLSALQEENVKLAEELGRTRDEVTSHQKLEEERSVLNNQLLEMKKRESEFRKDADEEKASLQKSISLTSALLTEKDAELEKLRNEVTVLRGENATAKSLHSVVQTLESDKVKLELKVKNLELQLKENKRQLSSSSGNTDAQAEEDERAQESQIDFLNSVIVDLQRKNQDLKMKVEMMSEAALNGNGEDLNSYDSDDQEKQSKKKPRLFCDICDCFDLHDTEDCPTQAQMSEDPPHSTHHGSRSEERPYCEICEMFGHWATNCNDDETF
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MALVPYTSPLDIVFYPVCAFLFCVIGFAFFATFIVSEMTTAKAQKNIFRELTLALIASMSLGLGLFFVLLAGGIYV
The following text describes a protein:
Function:
GTPase-activating protein for Rho family members.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Cytoplasm.
Sequence:
MMAKNKEPRPPSYTISVVGLSGTEKDKGNCGVGKSCLCNRFVRSKADEYYPEHTSVLSTIDFGGRVVNNDHFLYWGDIIQNGEDGVECKIHVIEQTEFIDDQTFLPHRSTNLQPYIKRAAASKLQSAEKLMYICTDQLGLEQDFEQKQMPEGKLNVDGFLLCIDVSQGCNRKFDDQLKFVNNLFVQLSKSKKPVIIAATKCDECVDHYLREVQAFASNKKNLLVVETSARFNVNIETCFTALVQMLDKTRSKPKIIPYLDAYKTQRQLVVTATDKFEKLVQTVRDYHATWKTVSNKLKNHPDYEEYINLEGTRKARNAFSKHIEQLKQEHIRKRREEYINTLPRAFNTLLPNLEEIEHLNWSEALKLMEKRADFQLCFVVLEKTPWDETDHIDKINDRRIPFDLLSTLEAEKYQNHVQHLISEKRRVEMKEKFKKTLEKIQFISPGQPWEEVMCFVMEDEAFKYITEADSKEVYGRHQREIVEKAKEEFQEMLFEHSELFYDLDLNATPSSDKMSEIHTVLSEEPRYKALQKLAPDRESLLLKHIGFVYHPTKETCLSGQNCTDIKVEQLLASSLLQLDHSRLRLYHDSTNIDKVNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDAKSPYFLSQLWTAAFKPHGCFCVFNSIESLSFIGEFIGKIRTEASQIRKDKYMANLPFTLILANQRDSISKNLPILRHQGQQLANKLQCPFVDVPAGTYPRKFNETQIKQALRGVLESVKHNLDMVSPVPANKDISEADLRIVMCAMCGDPFSVDLILSPFLDSHSCSAAQAGQNNSLMLDKIIGEKRRRIQITILSYHSSIGVRKDELVHGYILVYSAKRKASMGMLRAFLSEVQDTIPVQLVAVTDSQADFFENEAIKELMTEGEHIATEITAKFTALYSLSQYHRQTEVFTLFFSDVLEKKNMIENSYLSDNTRESTHQSEDVFLPSPRDCFPYNNYPDSDDDTEAPPPYSPIGDDVQLLPTPSDRSRYRLDLEGNEYPIHSTPNCHDHERNHKVPPPIKPKPVVPKTNVKKLDPNLLKTIEAGIGKNPRKQTSRVPLAHPEDMDPSDNYAEPIDTIFKQKGYSDEIYVVPDDSQNRIKIRNSFVNNTQGDEENGFSDRTSKSHGERRPSKYKYKSKTLFSKAKSYYRRTHSDASDDEAFTTSKTKRKGRHRGSEEDPLLSPVETWKGGIDNPAITSDQELDDKKMKKKTHKVKEDKKQKKKTKNFNPPTRRNWESNYFGMPLQDLVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHSINLVSMEVTVNAVAGALKAFFADLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQNKINLMTADNLSICFWPTLMRPDFENREFLSTTKIHQSVVETFIQQCQFFFYNGEIVETTNIVAPPPPSNPGQLVEPMVPLQLPPPLQPQLIQPQLQTDPLGII
The following text describes a protein:
Function:
Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
Subcellular Localization:
Secreted.
Sequence:
MKVWLASLFLCALVVKNSEGGSVLGAPDESNCGCQNGGVCVSYKYFSRIRRCSCPRKFQGEHCEIDASKTCYHGNGDSYRGKANTDTKGRPCLAWNAPAVLQKPYNAHRPDAISLGLGKHNYCRNPDNQKRPWCYVQIGLRQFVQECMVHDCSLSKKPSSSVDQQGFQCGQKALRPRFKIVGGEFTEVENQPWFAAIYQKNKGGSPPSFKCGGSLISPCWVASAAHCFIQLPKKENYVVYLGQSKESSYNPGEMKFEVEQLILHEYYREDSLAYHNDIALLKIRTSTGQCAQPSRSIQTICLPPRFTDAPFGSDCEITGFGKESESDYLYPKNLKMSVVKLVSHEQCMQPHYYGSEINYKMLCAADPEWKTDSCKGDSGGPLICNIEGRPTLSGIVSWGRGCAEKNKPGVYTRVSHFLDWIQSHIGEEKGLAF
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:
MKRNCNLDLRLVTPSLPPPSMINWNNRNDTQELTIFYNGRVAVCDATELQARAIIWVASHAVVEDKTNGSPGSDPVSSSPLLSPSMYSPSSVVSMKRSLKMFLQKRKTRSQASSPYPVITTKYSSQNWRPT
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:
MTKLMQWLFGASLLGGLWALVSFDLLDLNLPHTYREVAWPMPLYLLVSFGCFSLATVGYRVATFNDCDAAAKELQEQIREAREDLRRRGLKM
The following text describes a protein:
Function:
Metallothioneins have a high content of cysteine residues that bind various heavy metals.
Sequence:
MDPNCSCSTGLLLGREVPGKCIADTCPHLSPGCCSCCPVGCAKCAQGCICKGASDKCSCCA
The following text describes a protein:
Function:
Substrate recognition component of an ECS (Elongin BC-CUL5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Specifically binds to the methyltransferase cofactor S-adenosylmethionine (AdoMet) via the N-terminal AdoMet binding motif, but does not display methyltransferase activity. May provide an alternate maintenance pathway for modified proteins by acting as a damage-specific E3 ubiquitin ligase adaptor protein.
Subcellular Localization:
Cytoplasm. Membrane; Lipid-anchor.
Sequence:
GWEVFPGPVDWRLSSEGASRVRSSQEVVATRAVQLPWSRVAGRAPPSRAGAGGRCARPVGCLCGAPPAAGLPLLWPGGLPPTQARDAGAGTGLWGQSGRCCCVSVFCVFGPFGINHGIELHSDVVEYAKEKLESFIKNSDSFDKFEFCEPAFVVGNCLQIASDSHQYDRIYCGAGVQKDHENYMKILLKVGGILVMPIEDQLTQIMRTGQNTWESKNILAVSFAPLVQPSKNDNGTPDSVGLPPCAVRNLQDLARIYIRRTLRNFINDEMQAKGIPQRAPPKRKRKRVKQRINTYVFVGNQLIPQPLDSEEDEKMEEDSKEEEEKDHSEAMKREEPPQNLLREKIMKLPLPESLKAYLTYFRDK
The following text describes a protein:
Function:
Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMOs to their mature forms and deconjugation of SUMO from targeted proteins.
Sequence:
MTQRSSCSSSSPINKFDVFDFSEDSKTEKMFRKFRTPMKSPSPPISKYEFLQAFADGSKPQSRIVSIDLDNDDQEDAKCSPVKVLNKPLEIDDDEDDTDDTGFNKLLEVDDDEDDAGLNEPVDVDEEDDDAGIDDDRGKNVNACSMDSPLQHFAEKESDRDAEFVDSDVDLENQVFDMRCDDDDEDDEDDSSEMSSSSNSTFDSSKFEDCFEDHLVEDDSTAFKIDDNEKVVDVFPDFIQYGELYSTSSRLIFSSSSLKLEGPTNNQTGKTFKIEWETEDIIKIESCWFEKIKTAWINLLLRSKDSEDIGSTNEKPGVTTFVNNISDLFMCHYGSNIPILDLLTSDTSIAGFRLLKFAVYDSYWSRAEEAIKFLDMRYTSIWSTVFDVDANNYGNNSILGQDSLFSQRHYFPIFDEAFEEVIYPEGEPDAVSISKRDVALLQPETFVNDTIIDFYIKYLKNKLPTDEQERFHFFNSFFFRKLADLDKDPESASDGRAAFQRVRKWTRKVNLFEKDYILIPVNYSLHWSLIVICHPGEVPSFRDEEIKESSKVPCILHMDSLKGSHKGLKNLFQSYLCEEWKERHPNMADDFSSKFLQLRFISLELPQQDNFYDCGLFLLYFVERFLEEAPIKFNPFKITKFSKFLNSNWFPSDEASLRRSHIQNLIYDIFENGSLKAPPIDCRGKGPLSELPGVIEHKVEADSSGASCYPGIWHGNLSNGSTETDIQFRPVSPVRAASCSRDPGIVFKDLQAAVVPPHFDCRQMSLCHQSGFLSPIEETEEFGNEVSKSMERANSQVGILASDFPSTSYIGKDHRASETTQQGFPMNFVESVEGIPYSNWIQDSLEDQLLEKIEESNFPNKTALEEIADSVVQDSQESNGRHEIYIVQDSQESNGGHEIYVVQDSQESNDVHEVDACVKSHSSFQDNINSMTHQILDLAQNTSVENDSLAGKREQPASESQEQNDKKRKLMSETGGPSRRLTRRMLKETCV
The following text describes a protein:
Function:
Proton-sensing G-protein coupled receptor activated by extracellular pH, which is required to monitor pH changes and generate adaptive reactions (By similarity). The receptor is almost silent at pH 7.8 but fully activated at pH 6.8 (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as phospholipase C (By similarity). GPR68 is mainly coupled to G(q) G proteins and mediates production of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (By similarity). Acts as a key mechanosensor of fluid shear stress and membrane stretch. Expressed in endothelial cells of small-diameter resistance arteries, where it mediates flow-induced dilation in response to shear stress. May represents an osteoblastic pH sensor regulating cell-mediated responses to acidosis in bone. Acts as a regulator of calcium-sensing receptor CASR in a seesaw manner: GPR68-mediated signaling inhibits CASR signaling in response to protons, while CASR inhibits GPR68 in presence of extracellular calcium. Also functions as a metastasis suppressor gene in prostate cancer.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
A multitude of proton-sensing residues, which include extracellular histidine residues (His-17, His-20, His-84, His-169 and His-269) or triad of buried acidic residues (Asp-67, Glu-149 and Asp-282), contribute to activation of the G-protein coupled receptor activity and pH sensitivity.
Sequence:
MGNITTENSSLSCPIDHTIHQTLAPVVYVTVLVVGFPANCLSLYFGYLQIKARNELGVYLCNLTIADLFYICSLPFWLQYVLQHDDWSHGDLSCQVCGILLYENIYISVGFLCCISIDRYLAVAHPFRFHQFRTLKAAVGVSVLIWAKELLTSIYFLNHKEVIEDEDQHRVCFEHYPIQAWQRSINYYRFLVGFLFPICLLLASYQGILRAVRRSHGTQKSRKDQIQRLVLSTVVIFLACFLPYHVLLLVRSLWERNCEFAKSIFNVYHFSLLLTSFNCVADPVLYCFVSETTHRDLARLRGACLAVLTCSRTSRAREAYPLGAPEASGKSGAQGEEPELLTKLHSAFQTPSSLGVGGPSTVGLA