ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q7TQQ0 | MGALNQTRVTEFIFLGLTDNWVLEILFFVPFTVTYMLTLLGNFLIVVTIVFTPRLHNPMYFFLSNLSFIDICHSSVTVPKMLEGLLLERKTISFDNCIAQLFFLHLFACSEIFLLTIMAYDRYVAICIPLHYSNVMNMKVCVQLVFALWLGGTIHSLVQTFLTIRLPYCGPNIIDSYFCDVPPVIKLACTDTYLTGILIVSNSGTISLVCFLALVTSYTVILFSLRKQSAEGRRKALSTCSAHFMVVALFFGPCIFLYTRPDSSFSIDKVVSVFYTVVTPLLNPLIYTLRNEEVKTAMKHLRQRRICS | Function: Olfactory receptor that is activated by the binding of organosulfur odorants with thioether groups such as (methylthio)methanethiol (MTMT) and bis(methylthiomethyl) disulfide . Also binds odorants cis-cyclooctene and tert-butyl mercaptan . The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (Potential).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34986
Sequence Length: 308
Subcellular Location: Cell membrane
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Q6IEY1 | MDGENHSVVSEFLFLGLTHSWEIQLLLLVFSSVLYVASITGNILIVFSVTTDPHLHSPMYFLLASLSFIDLGACSVTSPKMIYDLFRKRKVISFGGCIAQIFFIHVVGGVEMVLLIAMAFDRYVALCKPLHYLTIMSPRMCLSFLAVAWTLGVSHSLFQLAFLVNLAFCGPNVLDSFYCDLPRLLRLACTDTYRLQFMVTVNSGFICVGTFFILLISYVFILFTVWKHSSGGSSKALSTLSAHSTVVLLFFGPPMFVYTRPHPNSQMDKFLAIFDAVLTPFLNPVVYTFRNKEMKAAIKRVCKQLVIYKRIS | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35074
Sequence Length: 312
Subcellular Location: Cell membrane
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Q8NGB9 | MDEANHSVVSEFVFLGLSDSRKIQLLLFLFFSVFYVSSLMGNLLIVLTVTSDPRLQSPMYFLLANLSIINLVFCSSTAPKMIYDLFRKHKTISFGGCVVQIFFIHAVGGTEMVLLIAMAFDRYVAICKPLHYLTIMNPQRCILFLVISWIIGIIHSVIQLAFVVDLLFCGPNELDSFFCDLPRFIKLACIETYTLGFMVTANSGFISLASFLILIISYIFILVTVQKKSSGGIFKAFSMLSAHVIVVVLVFGPLIFFYIFPFPTSHLDKFLAIFDAVITPVLNPVIYTFRNKEMMVAMRRRCSQFVNYSKIF | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35355
Sequence Length: 312
Subcellular Location: Cell membrane
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Q8NGD2 | MDVGNKSTMSEFVLLGLSNSWELQMFFFMVFSLLYVATMVGNSLIVITVIVDPHLHSPMYFLLTNLSIIDMSLASFATPKMITDYLTGHKTISFDGCLTQIFFLHLFTGTEIILLMAMSFDRYIAICKPLHYASVISPQVCVALVVASWIMGVMHSMSQVIFALTLPFCGPYEVDSFFCDLPVVFQLACVDTYVLGLFMISTSGIIALSCFIVLFNSYVIVLVTVKHHSSRGSSKALSTCTAHFIVVFLFFGPCIFIYMWPLSSFLTDKILSVFYTIFTPTLNPIIYTLRNQEVKIAMRKLKNRFLNFNKAMPS | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35357
Sequence Length: 314
Subcellular Location: Cell membrane
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Q96R72 | MAWSNQSAVTEFILRGLSSSLELQIFYFLFFSIVYAATVLGNLLIVVTIASEPHLHSPMYFLLGNLSFIDMSLASFATPKMIADFLREHKAISFEGCMTQMFFLHLLGGAEIVLLISMSFDRYVAICKPLHYLTIMSRRMCVGLVILSWIVGIFHALSQLAFTVNLPFCGPNEVDSFFCDLPLVIKLACVDTYILGVFMISTSGMIALVCFILLVISYTIILVTVRQRSSGGSSKALSTCSAHFTVVTLFFGPCTFIYVWPFTNFPIDKVLSVFYTIYTPLLNPVIYTVRNKDVKYSMRKLSSHIFKSRKTDHTP | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35408
Sequence Length: 315
Subcellular Location: Cell membrane
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Q8NGD3 | MDKSNSSVVSEFVLLGLCSSQKLQLFYFCFFSVLYTVIVLGNLLIILTVTSDTSLHSPMYFLLGNLSFVDICQASFATPKMIADFLSAHETISFSGCIAQIFFIHLFTGGEMVLLVSMAYDRYVAICKPLYYVVIMSRRTCTVLVMISWAVSLVHTLSQLSFTVNLPFCGPNVVDSFFCDLPRVTKLACLDSYIIEILIVVNSGILSLSTFSLLVSSYIIILVTVWLKSSAAMAKAFSTLASHIAVVILFFGPCIFIYVWPFTISPLDKFLAIFYTVFTPVLNPIIYTLRNRDMKAAVRKIVNHYLRPRRISEMSLVVRTSFH | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36258
Sequence Length: 323
Subcellular Location: Cell membrane
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Q8NH41 | MNETNHSRVTEFVLLGLSSSRELQPFLFLTFSLLYLAILLGNFLIILTVTSDSRLHTPMYFLLANLSFIDVCVASFATPKMIADFLVERKTISFDACLAQIFFVHLFTGSEMVLLVSMAYDRYVAICKPLHYMTVMSRRVCVVLVLISWFVGFIHTTSQLAFTVNLPFCGPNKVDSFFCDLPLVTKLACIDTYVVSLLIVADSGFLSLSSFLLLVVSYTVILVTVRNRSSASMAKARSTLTAHITVVTLFFGPCIFIYVWPFSSYSVDKVLAVFYTIFTLILNPVIYTLRNKEVKAAMSKLKSRYLKPSQVSVVIRNVLFLETK | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36484
Sequence Length: 324
Subcellular Location: Cell membrane
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Q9BRQ5 | MKGGEGDAGEQAPLNPEGESPAGSATYREFVHRGYLDLMGASQHSLRALSWRRLYLSRAKLKASSRTSALLSGFAMVAMVEVQLESDHEYPPGLLVAFSACTTVLVAVHLFALMVSTCLLPHIEAVSNIHNLNSVHQSPHQRLHRYVELAWGFSTALGTFLFLAEVVLVGWVKFVPIGAPLDTPTPMVPTSRVPGTLAPVATSLSPASNLPRSSASAAPSQAEPACPPRQACGGGGAHGPGWQAAMASTAIMVPVGLVFVAFALHFYRSLVAHKTDRYKQELEELNRLQGELQAV | Function: Ca(2+) release-activated Ca(2+)-like (CRAC-like) channel subunit which mediates Ca(2+) influx and increase in Ca(2+)-selective current by synergy with the Ca(2+) sensor, STIM1.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31499
Sequence Length: 295
Subcellular Location: Cell membrane
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Q09232 | MPRSHDPSRVELLRKEGGLTEKRVSISVEDIRGAVANWKNSGGAGDPITPYPLPQFFLQPPSTAGGGSRNGVGSKEGSVTSLRMPLKKAGDDVDLGHRGELDLSEKYNYDLSRAQLKASSRTSALLAGFAMVCLVELQYDQSTPKPLLIVLGVVTSLLVSVHLLALMMSTCILPYMEATGCTQDSPHIKLKFYIDLSWLFSTCIGLLLFLVEIGVIFYVKFTAVGYPTAGYITTAMLVPVGVVFVVFSYLIHKNRVSHSLGRFKHKVDTMKQFLDVEANLQKSTLAPSTIRDI | Function: Ca(2+) release-activated Ca(2+)-like (CRAC-like) channel subunit which mediates Ca(2+) influx and increase in Ca(2+)-selective current by synergy with the Ca(2+) sensor, stim-1. Required for Ca(2+) and IP3-dependent contractile activity of sheath cells and the spermatheca. Affects brood size and somatic cell function.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32024
Sequence Length: 293
Subcellular Location: Membrane
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Q9VSR3 | MDSLKLPKANSATSSASGSNSNLSGSTSASASAATSPTSSGTAVGGILSGAPKSPPGLGSSTPISVRFNANEESLDDILQSFHHSKHSPSGGASGGGDASPTSNLLGMKNNGLGLVVGNCDSLSSSPSQPQMHAGSASLFGNDEVSLRNNFMQAGGFFNRKSCGGLPNLNLNKPPQLHQQQHQQQHQQHQQHQQQQQLHQHQQQLSPNLSALHHHHQQQQQLRESGGSHSPSSPGGGGGGSPYNGSQAGCSSGGISPIPPQMGVSPKYRRSISFPIKGNSPTAIYGNMHMDGMGSGHMNIPTLSIGNGGGGGSTGMVSAGATGGGDAPYLGNSYGNMMTSNGQMHHGGGLDNSLCDYMRNMSLGGNGGGDGSNSMSLMQDRMRVMGGPKHLSEADAMAIAASGNDPSVYLNALKMGSPSRLSPHSPHSPIQGGNGGNVGDGTARFSRKVFVGGLPPDIDEDEITTSFRRFGPLVVDWPHKAESKSYFPPKGYAFLLFQDESSVQQLIDSCITDEDKLYLCVSSPTIKDKAVQIRPWRLADADYVLDATMSLDPRKTVFVGGVPRPLKAFELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGDIDKRVEVKPYVLDDQMCDECEGQRCGGKFAPFFCANVTCLQYYCEHCWAVIHSRPGREYHKPLVKEGADRPRAVPFRWC | Function: RNA-binding protein involved in translational regulation and required for long-term memory . Required in mushroom body gamma neurons for long-term memory in male courtship . Binds to mRNA 3'-UTRs . In its monomeric form, acts as a translational repressor of genes involved in neuronal growth, synapse formation and protein turnover . In its amyloid-like oligomeric form, acts as a translational activator . The monomeric form reduces poly(A) tail length and destabilizes mRNA while the oligomeric form protects and elongates the poly(A) tail and stabilizes mRNA . Involved in asymmetric cell division in the central nervous system . Plays a role in synapse formation and morphology at neuromuscular junctions by modulating the translation of the tumor suppressor brat . Required for the progression of spermatogenesis through meiosis and for sperm differentiation . During sperm differentiation, required to asymmetrically localize and activate the translation of protein kinase aPKC mRNAs which is necessary for spermatid cyst polarization . Also required during spermatid cyst polarization for localization and translation of its own mRNA .
PTM: Phosphorylation regulates interaction with Tob and oligomerization. Protein phosphatase 2A keeps both Orb2 and Tob in an unphosphorylated form. Following synaptic activation, unphosphorylated Orb2 is bound and stabilized by unphosphorylated Tob. Tob recruits activated LimK which phosphorylates both Orb2 and Tob and enhances Orb2 oligomerization.
Sequence Mass (Da): 74504
Sequence Length: 704
Domain: The RNA-binding region is not essential for long-term memory.
Subcellular Location: Perikaryon
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O13310 | MDKNDYLHFERNPSLFPKSTLDKVQKTKKYIEHYYKVAVDHAVERNQRRINLEQRLATERGSEERKNRQLRASGEKESQFLRFRRTRLSLEDFSTIKVIGKGAFGEVRLVQKLDTGKIYAMKSLLKTEMFKRDQLAHVKAERDLLVESDSPWVVSLYYAFQDSLYLYLIMEFLPGGDLMTMLINYDTFSEDVTRFYMAECVLAIADVHRMGYIHRDIKPDNILIDRDGHIKLSDFGLSTGFYKQDQSASYMKPRTGNTVKRGQMVDAIWLTMSSKDKMATWKKNRRVMAYSTVGTPDYIAPEIFLQQGYGQDCDWWSLGAIMFECLIGWPPFCSENSHETYRKIINWRETLTFPNDIHLSIEARDLMDRLMTDSEHRLGRGGAIEIMQHPFFTGIDWDHIRETAAPFIPNLKSITDTHYFPVDELEQVPEQPVTQQPASVDPQTLEQTNLAFLGYTYKKFNYLTMKGAL | Function: Interacts with pak1/shk1 and coordinates cell morphogenesis with the cell cycle. It is essential for maintenance of cell polarity and is involved in mitotic control.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 54691
Sequence Length: 469
EC: 2.7.11.1
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Q13415 | MAHYPTRLKTRKTYSWVGRPLLDRKLHYQTYREMCVKTEGCSTEIHIQIGQFVLIEGDDDENPYVAKLLELFEDDSDPPPKKRARVQWFVRFCEVPACKRHLLGRKPGAQEIFWYDYPACDSNINAETIIGLVRVIPLAPKDVVPTNLKNEKTLFVKLSWNEKKFRPLSSELFAELNKPQESAAKCQKPVRAKSKSAESPSWTPAEHVAKRIESRHSASKSRQTPTHPLTPRARKRLELGNLGNPQMSQQTSCASLDSPGRIKRKVAFSEITSPSKRSQPDKLQTLSPALKAPEKTRETGLSYTEDDKKASPEHRIILRTRIAASKTIDIREERTLTPISGGQRSSVVPSVILKPENIKKRDAKEAKAQNEATSTPHRIRRKSSVLTMNRIRQQLRFLGNSKSDQEEKEILPAAEISDSSSDEEEASTPPLPRRAPRTVSRNLRSSLKSSLHTLTKVPKKSLKPRTPRCAAPQIRSRSLAAQEPASVLEEARLRLHVSAVPESLPCREQEFQDIYNFVESKLLDHTGGCMYISGVPGTGKTATVHEVIRCLQQAAQANDVPPFQYIEVNGMKLTEPHQVYVQILQKLTGQKATANHAAELLAKQFCTRGSPQETTVLLVDELDLLWTHKQDIMYNLFDWPTHKEARLVVLAIANTMDLPERIMMNRVSSRLGLTRMCFQPYTYSQLQQILRSRLKHLKAFEDDAIQLVARKVAALSGDARRCLDICRRATEICEFSQQKPDSPGLVTIAHSMEAVDEMFSSSYITAIKNSSVLEQSFLRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSHLGSCRLLLVEPSRNDLLLRVRLNVSQDDVLYALKDE | Function: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
PTM: Phosphorylated during mitosis.
Sequence Mass (Da): 97350
Sequence Length: 861
Domain: The BAH domain mediates binding to dimethylated histone H4 'Lys-20' (H4K20me2), which is enriched at replication origins.
Subcellular Location: Nucleus
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G4MVZ4 | MHHFFKGQFFDFETCRILGTAVYGGADVAEVLEAVGQIRDGDPVSWGRAWAIQAERALVLAEEACKSGDRTAARDAYLRGSNYTRASGYMLTGEGPNRPDPRSREIVERVQAIFRKAAALFDHPVQFLKIPFEGGLKLPCTLYLPPPDRRLPGKIPILISGGGADALQEELYYMHPSAGPDLGYAVLTFEGPGQGVMLRKHDAKMRPDWEAVAGAVIDFLEELARSQPDLDLDTSRIAFSGCSLGGYFALRAAADPRVKACVSLDPLYSFWDFAMEHVSPTFINAWEAGWLKDGAVDAVVRMMMAMSFQMRWELSIAGTFFGQTSPARIMKEMKKFSLAGGQLRRVQCPVLVSGASHSLYLEGNHHTMRIYNELVNHTKGDKQLWLTATPGQGSLQAKMGALRLANQKTFKFLDEHFGIERPQL | Function: Hydrolyase; part of the gene cluster that mediates the biosynthesis of a tyrosine-derived cytochalasan acting as a fungal signal recognized by resistant rice plants and leads to avirulence in Pi33 resistant rice cultivars . The first step in the pathway is catalyzed by the hybrid PKS-NRPS ACE1, assisted by the enoyl reductase RAP1, that are responsible for fusion of the tyrosine precursor and the polyketide backbone . The polyketide synthase module (PKS) of ACE1 is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the tyrosine precursor . Because ACE1 lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase RAP1 . Reduction by the hydrolyase ORFZ, followed by dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase ORF3 then yield the required isoindolone-fused macrocycle (Probable). A number of oxidative steps catalyzed by the tailoring enzymes identified within the cluster, including cytochrome P450 monooxygenases CYP1 to CYP4, the FAD-linked oxidoreductase OXR2 and the short-chain dehydrogenase/reductase OXR1, are further required to afford the final cytochalasans that confer avirulence and which have still to be identified (Probable). The monooxygenase CYP1 has been shown to be a site-selective C-18 hydroxylase whereas the function of CYP3 is the site-selective epoxidation of the C-6/C-7 olefin that is present in some intermediate compounds . Finally, SYN2 and RAP2 are not required for avirulence in Pi33 resistant rice cultivars .
Sequence Mass (Da): 46951
Sequence Length: 424
Pathway: Secondary metabolite biosynthesis.
EC: 3.7.1.-
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Q94526 | MSPNRWILLLIFYISYLMFGAAIYYHIEHGEEKISRAEQRKAQIAINEYLLEELGDKNTTTQDEILQRISDYCDKPVTLPPTYDDTPYTWTFYHAFFFAFTVCSTVGYGNISPTTFAGRMIMIAYSVIGIPVNGILFAGLGEYFGRTFEAIYRRYKKYKMSTDMHYVPPQLGLITTVVIALIPGIALFLLLPSWVFTYFENWPYSISLYYSYVTTTTIGFGDYVPTFGANQPKEFGGWFVVYQIFVIVWFIFSLGYLVMIMTFITRGLQSKKLAYLEQQLSSNLKATQNRIWSGVTKDVGYLRRMLNELYILKVKPVYTDVDIAYTLPRSNSCPDLSMYRVEPAPIPSRKRAFSVCADMVAAQREAGMVHANSDTELSKLDREKTFETAEAYRQTTDLLAKVVNALATVKPPPAEQEDAALYGGYHGFSDSQILASEWSFSTVNEFTSPRRPRARACSDFNLEAPRWQSERPLRSSHNEWTWSGDNQQIQEAFNQRYKGQQRANGAANSTMVHLEPDALEEQLKKQSPGAGRVKKFSMPDGLRRLFPFQKKRPSQDLERKLSVVSVPEGVISQQARSPLDYYSNTVTAASSQSYLRNGRGPPPPFESNGSLASGGGGLTNMGFQMEDGATPPSALGGGAYQRKAAAGKRRRESIYTQNQAPSARRGSMYPPTAHALAQMQMRRGSLATSGSGSAAMAAVAARRGSLFPATASASSLTSAPRRSSIFSVTSEKDMNVLEQTTIADLIRALEVVHTHAVLDEQQQAAAAGGAAGGGGISRGSRKQRKMGNAGLEPPQLPPILSLFAGDQTRTLQAAAANRLYARRSTIVGISPTGGAATAPAARSLLEPPPSYTERAANQSQITAGPSNAPTVQSKFRRRFSVRPTALQIPPGQAPPPGASLMEQSSQTALQRRLSLRPSPLARELSPTSPPGGSGSALPAGAIDESGGTSAQRLLPLPAGTRPSTSSTHSPLSRIVQISQAQRKSSMPSAAATGSSGAPAEK | Function: Background potassium channel. Rectification is dependent on external potassium concentration. Acts as an outwardly rectifying channel but as external potassium levels increase, this is reversed.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 109290
Sequence Length: 1001
Subcellular Location: Membrane
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P53224 | MTELDYQGTAEAASTSYSRNQTDLKPFPSAGSASSSIKTTEPVKDHRRRRSSSIISHVEPETFEDENDQQLLPNMNATWVDQRGAWIIHVVIIILLKLFYNLFPGVTTEWSWTLTNMTYVIGSYVMFHLIKGTPFDFNGGAYDNLTMWEQIDDETLYTPSRKFLISVPIALFLVSTHYAHYDLKLFSWNCFLTTFGAVVPKLPVTHRLRISIPGITGRAQIS | Function: Component of the SPOTS complex that acts as a negative regulator of sphingolipid synthesis. Acts by inhibiting serine palmitoyltransferases (LCB1 and LCB2) activity.
PTM: Phosphorylated in case of disruption of sphingolipid synthesis. Phosphorylation regulates inhibitory activity of serine palmitoyltransferases (LCB1 and LCB2).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25245
Sequence Length: 222
Subcellular Location: Endoplasmic reticulum membrane
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Q06144 | MIDRTKNESPAFEESPLTPNVSNLKPFPSQSNKISTPVTDHRRRRSSSVISHVEQETFEDENDQQMLPNMNATWVDQRGAWLIHIVVIVLLRLFYSLFGSTPKWTWTLTNMTYIIGFYIMFHLVKGTPFDFNGGAYDNLTMWEQINDETLYTPTRKFLLIVPIVLFLISNQYYRNDMTLFLSNLAVTVLIGVVPKLGITHRLRISIPGITGRAQIS | Function: Component of the SPOTS complex that acts as a negative regulator of sphingolipid synthesis. Acts by inhibiting serine palmitoyltransferases (LCB1 and LCB2) activity.
PTM: Phosphorylated in case of disruption of sphingolipid synthesis. Phosphorylation regulates inhibitory activity of serine palmitoyltransferases (LCB1 and LCB2).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24855
Sequence Length: 216
Subcellular Location: Endoplasmic reticulum membrane
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Q9VP04 | MTSIAGGHGEANPNSSWLSARGFWLAYLLGLLSVHLLFLSVPFVSIPWAWTATNLLHNAAHLYFLHVIKGAPWLSTENDPSRRWTHWEQIDDGVQMTTTRKFLTAVPIVLFLLTCLYTRNNTEHFIPNFISLVVVTLPKLPQFHGVRLFNINKY | Function: Negative regulator of sphingolipid synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17570
Sequence Length: 154
Subcellular Location: Endoplasmic reticulum membrane
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Q29RQ9 | MNVGVAHSEVNPNTRVMNSRGMWLTYALGVGLLHIVLLSIPFFSVPVAWTLTNVIHNLGMYVFLHAVKGTPFETPDQGKARLLTHWEQLDYGVQFTSSRKFFTISPIILYFLASFYTKYDTTHFILNTASLLSVLIPKMPQLHGVRIFGINKY | Function: Negative regulator of sphingolipid synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17361
Sequence Length: 153
Subcellular Location: Endoplasmic reticulum membrane
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Q921I0 | MNVGVAHSEVNPNTRVMNSRGMWLTYALGVGLLHIVLLSIPFCSVPVAWTLTNIIHNLGMYVFLHAVKGTPFETPDQGRARLLTHWEQLDYGVQFTSSRKFFTISPIILYFLASFYTKYDPTHFILNTASLLSVLIPKMPQLHGVRIFGINKY | Function: Negative regulator of sphingolipid synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17355
Sequence Length: 153
Subcellular Location: Endoplasmic reticulum membrane
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Q756T2 | MWRWSTGVRTMLGYAMCFLALGSALTVRLHSTRTNLPQYLTREIGDDEFEELLRSSASAGHKWHVEQFVDGSRCYVPETEQNMAPVPDDLLERGIKLVEEATVGKKLEYLPISYWGYKFINSELNKTVIQHKDQHQVLLGSMVKADPQTVQHSLERDEDSYYISERFGDGDLCSLLEEDRTVEVQYRCKYDTPLEIILDLKEYETCRYTMLVSIPSLCELPEFGPYTRQTPANTIYCTAPATPEFNIATLVEAYKPTFLGHGFYHLAPHANLTHKETTAMLMYHQQPIPGNEEDDGTMDSAFIKHSTMAYMQLLEMGLLNGPDGLPFSEEGNFTVYAKVIGFDGGLITVTRFQISHGEVIIDHVVPEVLEDMEQGNSEDYEQQAPEQLDEEEAELTSQSDDPAIMRVHLQEFITPEYDAIE | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 47924
Sequence Length: 421
Subcellular Location: Endoplasmic reticulum membrane
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Q5ACR4 | MNWTSLVYLWFIFKSIFADLTSHQLKSKVVFLDTTISDEVARSYLGSEDGNVTHGNYEILSIANGANDGNITSYLCQLPRTKKMAPTKPKPTMSVHELKSRAIDLISESFVEGTSCVFSFNLHANYWTIGYCHGINVIQFHENLDDFISGIHKPHSPNHVYTLGNFSKQTSPLEFEFDTKERTISQRLLGEVCDLTGEPRTIDTIYRCDHILEIVELTEIRTCQYELHINVPKLCSLPEFKRTNLEEGVSEILCTRIE | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29429
Sequence Length: 258
Subcellular Location: Endoplasmic reticulum membrane
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Q6FV52 | MLVVAFASLLGAARAIMMPIDDPTTSDKFQITYANESLWDTLVMKNKTALESGELFDLGPDTKCFLPNMTRLHEQNVQSVNDPEYKQKLIDTLDMGAHIIDASLKNQCLVSQNGFWTYRYCGSGDFTQYHGVAPDPNDKLTYTLGRSSKQIENREFQLLYDDYGYYISEIIESGDICDVTGTPRAIEIQYTCGNVMRPGTLQWTRETKICHYEAQVIVPDLCQLELLSKNQDKKNAVPIICHMSNDVPDKHNIVDIVSNYDVSFVANQVYFLLPMNNSNVDRALLMYTGNATEDGLEMDPFPMEIYKKFIDVMNKMLGLGLLSPPDGKPFDVHDSYQWIGDIVDMHGNYLNRLRLDVDVNMEATLIIDKSINFTGPNNFQWYFRGSDRTKNSKSRFGSLTNDNMMLAGGSIINVDDISKENAQELLEKLVAAGKLSGVIEDNKITQGSPIEASKTKVTKASESTPVSEKNKKAKTVTKTIIRSRDKEEYFKENEKQGEENNAQVPFSAHNNEQHGTISKSERKEENTNQKQLANTQKGDTDTPPQSSQSSANDKLSRSGMGQKEPGVDEIGSELRGNSKKALGSNIDNSSGRSTLNDNSDRIAVENEAREIINSNAYDQSEASVDPNYRNDQQRLNSAKEHTFSQSKEKKSINSEEILETKILNSETLGNNDGVASDVKDEEVVESDRNGVIDDEL | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 77860
Sequence Length: 696
Subcellular Location: Endoplasmic reticulum membrane
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Q6BJ08 | MFSILNKLGIIWLALANISNCDNSKSGHKSIPKYNVKYYHANIPKDFANRFVELNDKIVENGSFEILGIDGQPSKNQYLCFTPNPNTAVNVSIESAQRNTRSKEIENEPKSEAEIIQRGVEMIEKSFSRKDCVFAYGSNGGYWTLGYCYGDKVVQFHENLQHFVATGKHKPEYPDYIYVLGRFKGSSKKPTNLDNQSPWASNNLDLSEFTIHESSIISDATAKNEQSRFLQHTLYDGEICDLTRKPRSIDIIYKCDPNHRGRIEILDQQEIKTCVYQMVIGVPKLCSLDEFRPNKVEDQIIDIDCKLIDQTNKVKADKLSYQDFFYYTDDIPSDNKIFPIPHSYKVSLNNYNLSPCGHGFYLGQSKLPINSPSVYFNFRHILVFNDQYHSSSDLLEKLGKMLKVCVGNKILSPHIENKRQSLLSWNDTFILWFELYDFYGSFISLVKVSRDGSKEELELKLRLINPETMLDQDGDLVKVPEFDAPNNAWNFQKFSKGKGSALDSTNNDKNNKATAENDKQYQSTSTDIVTVTVTESLETTSSEDGTEEVSNEMVILKKLADKLGMTDINELHQAIEDLDIELEVQHDEL | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 67260
Sequence Length: 589
Subcellular Location: Endoplasmic reticulum membrane
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Q5BDB9 | MRRQSRIVASLLVLACASSGAFAHRKFNVHDDLLAYPQFRIKFPDGFILESQARAFLEQAPYSSPDLNDISEQTPLKDESEESIRDGSSGEKAKFSYEELSLEGQRYLCQIPVVEDGDSNRTKVEVNEEEERKELARATDRGLELLREMEGKCLYYISGWWSYSFCYMNQIKQFHALPSGGGVPNYPPMEDHTTHSFILGRFPQEEGQDEGKGAKSGKSSTELAELQTKGGSRYLVQRLESGDQCDLTGKNRKIEVQFHCNPQSTDRIAWIKELYTCSYLMLIYTPRLCNDVAFLPPQQEEVHTIECREILTPEEVTGWQAMHEYQLSQQLVESAEAPKHQVIGGIEVGAQRLVGTEGKRIEKGRVASIGEEKVDVVAKRVNGEVQLLSAEELKKFDLDEAKIEELRKKLEEWAKGKDWTLEIVTGNGAYLRGVVDTDEDEEDGYENEEGETDKREQRENTQETTGQPGQPGHQEETESGQAGHPMDDRSEDGEDPDVDGSEEIFKDEL | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57548
Sequence Length: 509
Subcellular Location: Endoplasmic reticulum membrane
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Q4IEA7 | MRRFNLILLASLQLVGARSPGGFNIHEDLLTYPQFEVVFDNQYISEKDAHSLLDSQHPTYSADFAQSTLGQAREADARDNEAENKDQDGPSYKYELMKMPPNEYLCSIPILQSPEAENKTANELAKAEEARELTRATASGWELLSELQDSCLYFMSGWWSYSFCNNREIVQFHALPSIPNGQPPKRDPHTMEFTLGRVPAVPASAAHQAKMNGQEAPPPAELQVKGDQRYLVQRLEGGTICDLTGRERTIEVQYHCVPGMKADRIGWIKEVTICAYLMVVNTPRLCNDVAFLPPEETRANPITCKLILDKLNEPPSLDQTVPLAQDEAQVPLKQEDTGAKSGDAAPRDVGKEPINIGGVLVGARNVLSGADEAGKPPAKLPPPRSYFSNSNTDTERFLKVVASGKSKEDGGEMEVLGNEELEKLDLKPSVVKDMTERMRKLAGKYGWKLELVELPGGEKELRGYIDADEEELAKNKAKLKKEKEAAAKAKGDDEEEVVEGSEEQFFDKKDEL | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56835
Sequence Length: 512
Subcellular Location: Endoplasmic reticulum membrane
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Q13438 | MAAETLLSSLLGLLLLGLLLPASLTGGVGSLNLEELSEMRYGIEILPLPVMGGQSQSSDVVIVSSKYKQRYECRLPAGAIHFQREREEETPAYQGPGIPELLSPMRDAPCLLKTKDWWTYEFCYGRHIQQYHMEDSEIKGEVLYLGYYQSAFDWDDETAKASKQHRLKRYHSQTYGNGSKCDLNGRPREAEVRFLCDEGAGISGDYIDRVDEPLSCSYVLTIRTPRLCPHPLLRPPPSAAPQAILCHPSLQPEEYMAYVQRQADSKQYGDKIIEELQDLGPQVWSETKSGVAPQKMAGASPTKDDSKDSDFWKMLNEPEDQAPGGEEVPAEEQDPSPEAADSASGAPNDFQNNVQVKVIRSPADLIRFIEELKGGTKKGKPNIGQEQPVDDAAEVPQREPEKERGDPERQREMEEEEDEDEDEDEDEDERQLLGEFEKELEGILLPSDRDRLRSEVKAGMERELENIIQETEKELDPDGLKKESERDRAMLALTSTLNKLIKRLEEKQSPELVKKHKKKRVVPKKPPPSPQPTEEDPEHRVRVRVTKLRLGGPNQDLTVLEMKRENPQLKQIEGLVKELLEREGLTAAGKIEIKIVRPWAEGTEEGARWLTDEDTRNLKEIFFNILVPGAEEAQKERQRQKELESNYRRVWGSPGGEGTGDLDEFDF | Function: Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4.
PTM: Intramolecular disulfide bonds.
Sequence Mass (Da): 75562
Sequence Length: 667
Subcellular Location: Endoplasmic reticulum lumen
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Q6CNH1 | MIFLPVTSVVFAISWIYSGVSAFNPYSSTPYSLKYVDEQEFLSVIDNETLLQEGRLFRPYEGSDVLCYQRNTSSLIQHHEEDTFNSEGALIEAVNMVNAILAPNPIEMNTVPISYWTYIISSGETRTVVQKGYFGETYLLGNSSNYNSTIDYHFAKSKTGRVYLSETLVDGCTCDLTHKPREVEIQYICPKRPLSRPFHLEVREIQSCKYQLRLFLPQLCELSSFNPLLGQLSEHNIICHRSGSKLSPALDIFNRYSATVLDHGIYLLKPKNSAKDRRQLMYHAAEPLDSQTTLFELTVEERFIGDFISSLKKLIGSDFIQSPTGKSIKPGDLFLWRAPVVDETGNLLFLIDLELNSASEAIGKVNNDASLLNELPIHNMVYFDSMTVNQTDETSSNSLPEKSTGLVPDIFATDEIESPYKGGTAQELKDKLMEAFRDIGYPDIEVEILEEVVEEQN | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 51621
Sequence Length: 457
Subcellular Location: Endoplasmic reticulum membrane
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Q872S3 | MRRPSLALLALSSLPFGSARQPASFSIHQDLLAHPQFEVIFSDSYVFEADAFALLEAANKTPKPTPASDGAHDGSTTRTDLTSAIRESATANADTDNGDESIGGTSPLRETYELIAHPPMRYLCSIPIIAPPPALNKTATELAKAEEAREVTRAYNKGWELMRGLENQCLHFVSGWWSYQYCYGKSIVQYHAVPNPKGGPPLRDKNSQEYILGTSLPPSSHSQKGKQIEVPNNEQKQLSPPPNTELQAKDNQRYLVQRLDGGTICDLTGRPRTIEIQYHCNPALSGDRIGWIKEVTTCAYLMVIHTPRLCADVAFLPPKETKAHPITCRQIITSDEEALSFNQRRKNTIDSAAAAAAAVTTEDQKQGSESGSPEKLSYQGLTVAGIPIGARRILPSTHVLPLPRHLQQQRQEAQQGNLLEALTKAAFKADVFGDYGDDNNNNNNNHHPKAGKGRKAAGAGKGQSGQKEMKKMRISERDIDKLGLDQQTLDALREEIRAAGLDPDRNLNDEREAGGEIVWEFYADVSGDEDDGAVAEEGKEVFVWYEDEDEGGEPAEAGKDQKESKKGGNGEGSGSGSEEGSKEEYYRDEL | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 64567
Sequence Length: 590
Subcellular Location: Endoplasmic reticulum membrane
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Q9UTC8 | MFSSSMFPHLILPAIGSSKVRTMVLPFAFVGFFIFPICLASLLDWNDAYEYPKYSFEWSNVSILEGDIDSIKEKTEKTKLSSLFYAGKHEYFCVYPNASLIKQNSTTEPSYDLQELRIQGTEKINELANVFLIENRGYWTYDYVYGQHVRQYHLEPQQGSDKVLANPMYILGTAPNTQTKKNLEENWAIGFVEGKAYLQTTFRNGTMCDITKRPRHVILSYECSTNSDTPEITQYQEVSSCAYSMTIHVPGLCSLPAFKIQEDIPSEKIVCYNVIKEKSNEVDHKDSQHVVDEVAQTSPPEVKEVETQSS | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 35393
Sequence Length: 310
Subcellular Location: Endoplasmic reticulum membrane
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Q6C3U1 | MLLKSLALIASSSLAATFNIGDDLFADPQFTVQFHNRPLRQADVQNGLLPHRDPVYGHPLGYEMMQFNGTNHICGIPEVTTTKSSKSREEGELSPTEARDRALELMLPLLGDCLFYEQGFFSYRFCYGSGVVQYRRHGDNYFPRIYPPPQADDSPTFVLGSFEKDDTTNTVTSAGGIPFLAHRLRSGTHCPLTGANREIEVQFVCDKNVQHDHILWIKEKRTCNYVMQVGTPRLCKDMRFQPPPDESLPIMCYSVESEAPEFETIDGMFDGVAHVKEEQEAVSARAHQFVGSNVNKDKIDEIEVAWRFTKARALNYIGVWLGDCVNRQTLFKELGIATPSHDAPFIIQTRSMFVPAPINRHFEVRLMITRQQLLLSINDDDVTLEEKYAWWQEQGDMSNLEIQGLTMLDDAGIEDVLARATDEVMKQLNKEAKQSKKLAKKKEAASTKREEAKKQVEASVEEKAVDSAEDDGTDTVTSTQTFFRTQTLSTAEAESKQMPDKAEEDEDEDLIVTMYFEDGEFKIEGFEVADFEGVKSAMKDLADKEDDDDDYEDYGLSD | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 63074
Sequence Length: 558
Subcellular Location: Endoplasmic reticulum membrane
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Q99220 | MQAKIIYALSAISALIPLGSSLLAPIEDPIVSNKYLISYIDEDDWSDRILQNQSVMNSGYIVNMGDDLECFIQNASTQLNDVLEDSNEHSNSEKTALLTKTLNQGVKTIFDKLNERCIFYQAGFWIYEYCPGIEFVQFHGRVNTKTGEIVNRDESLVYRLGKPKANVEEREFELLYDDVGYYISEIIGSGDICDVTGAERMVEIQYVCGGSNSGPSTIQWVRETKICVYEAQVTIPELCNLELLAKNEDQKNASPILCRMPAKSKIGSNSIDLITKYEPIFLGSGIYFLRPFNTDERDKLMVTDNAMSNWDEITETYYQKFGNAINKMLSLRLVSLPNGHILQPGDSCVWLAEVVDMKDRFQTTLSLNILNSQRAEIFFNKTFTFNEDNGNFLSYKIGDHGESTELGQITHSNKADINTAEIRSDEYLINTDNELFLRISKEIAEVKELLNEIVSPHEMEVIFENMRNQPNNDFELALMNKLKSSLNDDNKVEQINNARMDDDESTSHTTRDIGEAGSQTTGNTESEVTNVAAGVFIEHDEL | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. The recognition of targets is N-glycan specific. Functions in recruiting misfolded protein substrates in conjunction with HRD3 .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 61258
Sequence Length: 542
Domain: The MRH (mannose 6-phosphate receptor homology) domain is required for the ERAD-L activity.
Subcellular Location: Endoplasmic reticulum membrane
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Q1EG28 | MKTLSVLVLCSLAVLCLTSDASFSSQPAVDTPAQEGLFVEQEQASSVVRQAPKELSLSQLESLREVCELNLACEDMMDTSGIIAAYTTYYGPIPF | Function: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein (By similarity). The carboxylated form binds strongly to apatite and calcium (By similarity).
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium.
Sequence Mass (Da): 10252
Sequence Length: 95
Subcellular Location: Secreted
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K7NTD0 | MKTLVLLSICALLSVCWSMGAVEPEVVVDTVADTTADAAPADPAAAAAPSSSSSESSESSESSESSESSESSESSESSESNSSSASDSNSSSDSSASDSNSSSDSSSSSSSSSSSSSSSSSSSESTESSESSESSSSSSSSSSSSSSSSSSSSSESSSSESNSADSSASDSPSSSSSSSSSSSSESASDEAAKVVVKRDLASVLLRRRRAAPGGDLTPLQLESLREVCELNIACDEMAETAGIVAAYVAYYGPVPF | Function: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein (By similarity). The carboxylated form binds strongly to apatite and calcium (By similarity).
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium.
Sequence Mass (Da): 25198
Sequence Length: 256
Subcellular Location: Secreted
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Q800Y1 | MKTLAILVLCSLAAICLTSSASAGAQPAGDSPVQGGLFMEKDQASAVVRQTRAAKELTLAQTESLREVCETNMACDEMADAQGIVAAYQAFYGPIPF | Function: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein (By similarity). The carboxylated form binds strongly to apatite and calcium (By similarity).
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium.
Sequence Mass (Da): 10115
Sequence Length: 97
Subcellular Location: Secreted
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P86314 | YLDHGLGAPAPYVDPLEPKREVCELNPDCDELADQMGFQEAYRRFYGTT | Function: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein: it acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly to apatite and calcium.
PTM: Gamma-carboxyglutamic acid residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium (By similarity).
Sequence Mass (Da): 5592
Sequence Length: 49
Subcellular Location: Secreted
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P86312 | YLDHGLGAPAPYVDPLEPKREVDELADQMGFQEAYRRFYGTT | Function: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein: it acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly to apatite and calcium.
PTM: Gamma-carboxyglutamic acid residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium (By similarity).
Sequence Mass (Da): 4817
Sequence Length: 42
Subcellular Location: Secreted
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P02822 | MKAAALLLLAALLTFSLCRSAPDGSDARSAKAFISHRQRAEMVRRQKRHYAQDSGVAGAPPNPLEAQREVCELSPDCDELADQIGFQEAYRRFYGPV | Function: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein . The carboxylated form binds strongly to apatite and calcium (By similarity).
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium.
Sequence Mass (Da): 10707
Sequence Length: 97
Subcellular Location: Secreted
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Q7LZI4 | AGTAPADLTVAQLESLKEVCEANLACEHMMDVSGIIAAYTAYYGPIPY | Function: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein . The carboxylated form binds strongly to apatite and calcium (By similarity).
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium.
Sequence Mass (Da): 5063
Sequence Length: 48
Subcellular Location: Secreted
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P83238 | AGTAXGDLTPFQLESLREVCEVNLACEHMADTXGIVAAYTAYYGY | Function: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein . The carboxylated form binds strongly to apatite and calcium (By similarity).
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium.
Sequence Mass (Da): 4838
Sequence Length: 45
Subcellular Location: Secreted
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Q9HIK9 | MSKRDILSVLDMEKDLSEIIDLSIELKKNRYRSYESLRNKVLGLIFEKPSTRTRTSLEVAIDQLGGHAVYLNPSEMQLGRGETISDTGHVLSRFLDAIAYRAYDHRNVVELARSTSIPVINALDDVEHPLQIVADFMTIKEKKGRFTNLKFSYIGDGNNMANSLMLGAAILGTDMYVASPKGFEPKQEFVEKARSIAKQHGSSITITNDPVEAARDADVIYTDVWISMGEESKKGEKEKAFKDFQINEKLVSNAKRDYIFMHCLPAHRGLEVTDGVADSINSVIFDEAENRLHSEKGVLYKLLSY | Function: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Catalytic Activity: carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate
Sequence Mass (Da): 34299
Sequence Length: 305
Pathway: Amino-acid degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.1.3.3
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Q01323 | KTSTRTRCAFEVAARDQGAGVTYLEPSASQIGHKESIKDTARVLGRMFDGIEYRGFGQDVVEELAKYAGVPVFNGLTNEFHPTQMLADGLTMREHSDKPLNQIAFAYVGDARYNMANSLLVLAAKLGMDVRISAPKSLWPSENIIEMVQAVAKETGGRILLTENVQEAVKGVDFIHTDVWVSMGEPKEAWQERIDLLKDYRVTPELMAAAENPQVKFMHCLPAFHNRETKVGEWIYETFGLNGVEVTEEVFESEASIVFDQA | Function: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Catalytic Activity: carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate
Sequence Mass (Da): 29205
Sequence Length: 262
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.1.3.3
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Q01324 | KTSTRTRCAFEVAARDQGAGVTYLESSASQIGHKESIKDTARVLGRMYDAIEYRGFGQETVEELAKYAGVPVFNGLTNEFHPTQMLADALTMREHGGKPLNQTSFAYVGDARYNMGNSLLILGAKLGMDVRIGAPEGLWPSEGIIAAANAVAEETGAKITLTANPQEAVKGVGFIHTDVWVSMGEPKEIWQERIDLLKDYRVTSELMAASGNPQVKFMHCLPAFHNRETKIGEWIYETFGLNGVEVTEEVFESPAGIVFDQA | Function: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Catalytic Activity: carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate
Sequence Mass (Da): 28665
Sequence Length: 262
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.1.3.3
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O86404 | DQGAGATYLEPSASQIGHKESIKDTARVLGRMYDAIEYRGFGQEIIEELAKYAGVPVFNGLTNEFHPTQMLADALTMREHSSKPLNQTAFAYVGDARYNMGNSLLILGAKLGMDVRIGAPESLWPSEGIIAAAHAVAKETGAKITLTENAHEAVNGVGFIHTDVWVSMGEPKEVWQERIDLLKDYRVTPELMAASGNPQVKFMHCLPAFHNRETKVGEWIYETFGLNGVEVT | Function: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Catalytic Activity: carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate
Sequence Mass (Da): 25480
Sequence Length: 232
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.1.3.3
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Q7RTS6 | MSEELAQGPKESPPAPRAGPREVWKKGGRLLSVLLAVNVLLLACTLISGGAFNKVAVYDTDVFALLTAMMLLATLWILFYLLRTVRCPCAVPYRDAHAGPIWLRGGLVLFGICTLIMDVFKTGYYSSFFECQSAIKILHPLIQAVFVIIQTYFLWVSAKDCVHVHLDLTWCGLMFTLTTNLAIWMAAVVDESVHQSHSYSSSHSNASHARLISDQHADNPVGGDSCLCSTAVCQIFQQGYFYLYPFNIEYSLFASTMLYVMWKNVGRFLASTPGHSHTPTPVSLFRETFFAGPVLGLLLFVVGLAVFIIYEVQVSGDGSRTRQALVIYYSFNIVCLGLTTLVSLSGSIIYRFDRRAMDHHKNPTRTLDVALLMGAALGQYAISYYSIVAVVAGTPQDLLAGLNLTHALLMIAQHTFQNMFIIESLHRGPPGAEPHSTHPKEPCQDLTFTNLDALHTLSACPPNPGLVSPSPSDQREAVAIVSTPRSQWRRQCLKDISLFLLLCNVILWIMPAFGARPHFSNTVEVDFYGYSLWAVIVNICLPFGIFYRMHAVSSLLEVYVLS | Function: Proton-selective channel that specifically transports protons into cells. Proton-selective channel activity is probably required in cell types that use changes in intracellular pH for cell signaling or to regulate biochemical or developmental processes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62236
Sequence Length: 562
Subcellular Location: Cell membrane
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Q80SX5 | MSEELVPHPNESLPGPRASPREVWKKGGRLLSVLLAVNVLLLACTLISGGAFNKVAVYDTDVFALLTTMMLLAALWIVFYLLRTARCPDAVPYRDAHAGPIWLRGGLVLFGICTLVMDVFKTGYYSSFFECQSAIKILHPIIQAVFVIVQTYFLWISAKDCIHTHLDLTRCGLMFTLATNLAIWMAAVVDESVHQAHSYSGSHGNTSHTRLNPDSKRAGGAAEEDPCLCSTAICQIFQQGYFYLYPFNIEYSLFASTMLYVMWKNVGRLLASTHGHGHTPSRVSLFRETFFAGPVLGLLLFVVGLAVFILYEVQVSGERGHTRQALVIYYSFNIVCLGLMTLVSLSGSVIYRFDRRAMDHHKNPTRTLDVALLMGAALGQYAISYYSIVAVVVGSPRDLQGALNLSHALLMIAQHTFQNVFIIESLHRGPPGAEPREMPPKEPCQGITFANLDAIRTLPSCPPTPRLVIPNLESPQEAVAIISAPRCHWRRRCLKDISLFLLLCNVILWIMPAFGARPHFSNTVEVDFYGYSLWAAIVNICLPFGIFYRMHAVSSLLEVYVLS | Function: Proton-selective channel that specifically transports protons into cells. Proton-selective channel activity is probably required in cell types that use changes in intracellular pH for cell signaling or to regulate biochemical or developmental processes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62582
Sequence Length: 563
Subcellular Location: Cell membrane
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Q7RTS5 | MGRGARAAAAQSRWGRASRASVSPGRTIRSAPAVGEAQETEAAPEKENRVDVGAEERAAATRPRQKSWLVRHFSLLLRRDRQAQKAGQLFSGLLALNVVFLGGAFICSMIFNKVAVTLGDVWILLATLKVLSLLWLLYYVASTTRRPHAVLYQDPHAGPLWVRGSLVLFGSCTFCLNIFRVGYDVSHIRCKSQLDLVFSVIEMVFIGVQTWVLWKHCKDCVRVQTNFTRCGLMLTLATNLLLWVLAVTNDSMHREIEAELGILMEKSTGNETNTCLCLNATACEAFRRGFLMLYPFSTEYCLICCAVLFVMWKNVGRHVAPHMGAHPATAPFHLHGAIFGPLLGLLVLLAGVCVFVLFQIEASGPAIACQYFTLYYAFYVAVLPTMSLACLAGTAIHGLEERELDTVKNPTRSLDVVLLMGAALGQMGIAYFSIVAIVAKRPHELLNRLILAYSLLLILQHIAQNLFIIEGLHRRPLWETVPEGLAGKQEAEPPRRGSLLELGQGLQRASLAYIHSYSHLNWKRRALKEISLFLILCNITLWMMPAFGIHPEFENGLEKDFYGYQIWFAIVNFGLPLGVFYRMHSVGGLVEVYLGA | Function: Proton-selective channel that specifically transports protons into cells. Proton-selective channel activity is probably required in cell types that use changes in intracellular pH for cell signaling or to regulate biochemical or developmental processes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66296
Sequence Length: 596
Subcellular Location: Cell membrane
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Q80UF9 | MASQTSAPAEPAPMPSPEAKTTEGASSYDQADMETKHAGSPCPPKQKSWLARHFSLLLRRDRQAQKAGQLFSGLLALNVVFLGGAFICSMIFNKVSVTLGDVWILLAALKVLSLLWLLYYTVGTTRKPHAVLYRDPHAGPIWVRGSLVLFGSCTVCLNIFRMGYDVSHIHCKSEVELIFPAIEIVFMIIQTWVLWRHCKDCVQVQTNFTRCGLMLTLATNLLMWVLAVTNDSMHREIEAELDALMEKFSGNGTNTCMCLNTTVCEVFRKGYLMLYPFSTEYCLICCAVLFVMWKNVSRSLAAHTGAHPNRSPFRLHGTIFGPLLGLLALVAGVCVFVLFQIEASGPDIARQYFTLYYAFYVAVLPTMSLACLAGTAIHGLEERELDTLKNPTRSLDVVLLMGAALGQMGIAYFSIVAIVATQPHELLNQLILAYSLLLILQHITQNLFIIEGLHRRPLWEPAVSGVMEKQDVELPRRGSLRELGQDLRRASRAYIHSFSHLNWKRRMLKEISLFLILCNITLWMMPAFGIHPEFENGLEKDFYGYRTWFTIVNFGLPLGVFYRMHSVGGLVEVYLGA | Function: Proton-selective channel that specifically transports protons into cells. Proton-selective channel activity is probably required in cell types that use changes in intracellular pH for cell signaling or to regulate biochemical or developmental processes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64743
Sequence Length: 577
Subcellular Location: Cell membrane
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Q47421 | MKLKRKRVKPIALDDVTIIDDGRLRKAITAAALGNAMEWFDFGVYGFVAYALGQVFFPGADPGVQMIAALATFSVPFLIRPLGGVFFGALGDKYGRQKILAITIIIMSISTFCIGLIPSYERIGIWAPILLLLAKMAQGFSVGGEYTGASIFVAEYSPDRKRGFMGSWLDFGSIAGFVLGAGVVVLISTLIGEQAFLAWGWRLPFFLALPLGLIGLYLRHALEETPAFRQHVEKLEQNDRDGLKAGPGVSFREIATHHWKSLLVCIGLVIATNVTYYMLLTYMPSYLSHSLHYSENHGVLIIIAIMIGMLFVQPVMGLLSDRFGRKPFVVIGSVAMFFLAVPSFMLINSDIIGLIFLGLLMLAVILNAFTGVMASTLPALFPTHIRYSALASAFNISVLIAGLTPTVAAWLVESSQNLYMPAYYLMVIAVIGLLTGLFMKETANKPLKGATPAASDLSEAKEILQEHHDNIEHKIEDITQQIAELEAKRQLLVAQHPRIND | Function: Involved in uptake and accumulation of various osmoprotectants. Allows the uptake of glycine betaine, proline, ectoine, and pipecolic acid . May be a contributory factor in the infection progression within the host .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54858
Sequence Length: 501
Subcellular Location: Cell inner membrane
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E0SCY1 | MAIKLEVTHLYKIFGEHPERAFRLLEQGLSKDQIFEKTGLTVGVKDASLAIEEGEIFVIMGLSGSGKSTLVRLLNRLIEPTRGQVLIDGEDISRLPDGALRAVRRKQISMVFQSFALMPHLNILDNTAFGMDLAGVPRAEREQKALNALQQVGLETYAHAYPDELSGGMRQRVGLARALANDPDILLMDEAFSALDPLIRTEMQDELIKLQARRQRTIVFISHDLDEAMRIGDRIAIMHSGEVIQVGTPDEILNNPANDYVRTFFRGVDISHVFTAKDIARRRPVAVIRKTPGVGPRSALRILQEEDREYGYVLERGRKFIGVVSIDSLKQALRGQQPLEQALLPAPAPVPASMSLNELISQVAQAPCAVPVVDENHEYLGIISKGMLLQALDKESTLND | Function: Part of the OusB ABC transporter complex involved in glycine betaine and choline uptake. May also transport several other osmoprotectants such as ectoine, DMSA, DMSP, proline and carnitine. Probably responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 44338
Sequence Length: 400
Subcellular Location: Cell inner membrane
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E0SCY2 | MTDTTQNPWEEDQAPDQAAAANHSHAAATSGEHAAAAGSSGTPAQTDPWAASSSAPAGNTPAPDNAADAWSNAPPPAASDVHQSAADWLNSTPTPTQEHFNLMDPFRHTLVPLDRWVTEGIDWLVLHFRPLFQGIRVPVDMILTSFQQLLTGLPAPVAILVFSLLAWQVSSFGMGVATLLSLVAIGAIGAWSQAMVTLALVLTALFFCVIIGLPLGIWLAHSDRAARIVRPLLDAMQTTPAFVYLIPIVMLFGIGNVPGVVVTIIFALPPIIRLTILGIRQVPADLVEAAQSFGASPRQMLFKVQLPLAMPTIMAGINQTLMLALSMVVIASMIAVGGLGQMVLRGIGRLDMGLASIGGVGIVILAIILDRLTQSLGRDARSRGNRHWYHHGPLGLLARPFIKSRA | Function: Part of the OusB ABC transporter complex involved in glycine betaine and choline uptake. May also transport several other osmoprotectants such as ectoine, DMSA, DMSP, proline and carnitine. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43060
Sequence Length: 406
Subcellular Location: Cell inner membrane
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Q01567 | MHVSSLKVVLFGVCCLSLAACQTPAPVKNTASRSAASVPANEQISQLASLVAASKYLRVQCERSDLPDDGTILKTAVNVAVQKGWDTGRYQSLPQLSENLYQGLLKDGTPKATQCSSFNRTMTPFLDAMRTVR | Function: Out proteins are required for the translocation of pectate lyases and cellulases across the outer membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 14334
Sequence Length: 133
Subcellular Location: Cell outer membrane
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P0DPS2 | MNVFFMFSLLFLAALGSCADDRNPLEECFRETDYEEFLEIARXXXXTSNPKHVVRVGAGMSGLSAAYVLAGAGHQVTVLEASERPGGRXXXXXXXXEGWYANLGPMRXXXXXXXXXXXXXKFGLNLNEFSQENDNAWYFIKXXXXXXXXXXDPGLLKYPVKPSEAGKSAGQLYEESLGKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFDEIVDGMDKLPTSMYQAIXXXXXXXXXXXXXXXXXXKVTVTYQTPAKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXIFLTCTKKFWEDDGIHGGKSTTDLPSRXXXXXXXXXXXXXXVIIAYGIGDDANFFQALDFKDCADIVFNDLSLIHQLPKEEIPSFCYPSMIQKXXXXXXXXXXITTFFTPYQFQHFSEAXXXXXXXIYFAGEYTAQAHGWIDSTIK | Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme . Shows activity on L-Leu . Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation (By similarity). When tested on SW480 and SW620 human colon cancer cells, shows inhibition of cell proliferation, and induction of apoptosis, which is probably a consequence of the increased caspase-3 activity and the decreased Bcl-2 expression .
PTM: N-glycosylated.
Catalytic Activity: an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+)
Sequence Mass (Da): 54544
Sequence Length: 488
Subcellular Location: Secreted
EC: 1.4.3.2
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P0C2D7 | ADDKNPLEECFREDDYEEFLEIAKNGLKKTSNPKHIVYPVKPSEQLYEESLRDQLPTSMHRYPSMIQKIFFAGEYTANAHGWIDSTIK | Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme . Is highly active on L-Met, L-Leu, L-Phe, L-Ile, and L-Arg, moderately active on L-His, L-Trp, L-Asn, L-Glu, and L-Val, and weakly or not active on L-Gln, L-Lys, L-Asp, L-Ala, L-Tyr, L-Ser, L-Pro, L-Gly, L-Thr, and L-Cys . Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities (By similarity). In addition, this protein has an ability to induce apoptosis in cultured HeLa and K562 cells, and inhibits ADP-induced platelet aggregation dose-dependently. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions.
PTM: N-glycosylated.
Catalytic Activity: an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+)
Sequence Mass (Da): 10295
Sequence Length: 88
Subcellular Location: Secreted
EC: 1.4.3.2
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Q51330 | MNNPQTGQSTGLLGNRWFYLVLAVLLMCMISGVQYSWTLYANPVKDNLGVSLAAVQTAFTLSQVIQAGSQPGGGYFVDKFGPRIPLMFGGAMVLAGWTFMGMVDSVPALYALYTLAGAGVGIVYGIAMNTANRWFPDKRGLASGFTAAGYGLGVLPFLPLISSVLKVEGVGAAFMYTGLIMGILIILIAFVIRFPGQQGAKKQIVVTDKDFNSGEMLRTPQFWVLWTAFFSVNFGGLLLVANSVPYGRSLGLAAGVLTIGVSIQNLFNGGCRPFWGFVSDKIGRYKTMSVVFGINAVVLALFPTIAALGDVAFIAMLAIAFFTWGGSYALFPSTNSDIFGTAYSARNYGFFWAAKATASIFGGGLGAAIATNFGWNTAFLITAITSFIAFALATFVIPRMGRPVKKMVKLSPEEKAVH | Function: Anion transporter that carries out the exchange of divalent oxalate with monovalent formate, the product of oxalate decarboxylation, at the plasma membrane, and in doing so catalyzes the vectorial portion of a proton-motive metabolic cycle that drives ATP synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44517
Sequence Length: 418
Domain: The protein has a two-fold symmetry axis, with a central cavity which may be associated with substrate transport. Residues contributed from seven transmembrane helices probably line the substrate transport pathway.
Subcellular Location: Cell inner membrane
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P45850 | SDPDPLQDFCVADLDGKAVSVNGHTCKPMSEAGDDFLFSSKLTKAGNTSTPNGSAVTELDVAEWPGTNTLGVSMNRVDFAPGGTNPPHIHPRATEIGMVMKGELLVGILGSLDSGNKLYSRVVRAGETFVIPRGLMHFQFNVGKTEAYMVVSFNSQNPGIVFVPLTLFGSDPPIPTPVLTKALRVEAGVVELLKSKFAGGS | Function: Releases hydrogen peroxide in the apoplast which may be important for cross-linking reactions in the cell wall biochemistry. May play an important role in several aspects of plant growth and defense mechanisms.
PTM: Glycosylated. A form called G contains antennary GlcNAc residues, whereas a form called G' lacks antennary GlcNAc residues in its otherwise identical glycans.
Catalytic Activity: 2 H(+) + O2 + oxalate = 2 CO2 + H2O2
Sequence Mass (Da): 21203
Sequence Length: 201
Subcellular Location: Secreted
EC: 1.2.3.4
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Q9I6Z0 | MSRTWIRNPLAIFTANGLDAAGGLVVEDGRIVELLGAGQQPAQPCASQFDASRHVVLPGLVNTHHHFYQTLTRAWAPVVNQPLFPWLKTLYPVWARLTPEKLELATKVALAELLLSGCTTAADHHYLFPGGLEQAIDVQAGVVEELGMRAMLTRGSMSLGEKDGGLPPQQTVQEAETILADSERLIARYHQRGDGARVQIALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLAETLDEEDFCLQRFGLRTVDYLDSVGWLGPRTWLAHGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASNMILEARQALYLQRLRYGAERITPELALGWATRGSARLLGRSDIGELAPGKQADLALFKLDELRFSGSHDPLSALLLCAADRADRVMVGGAWRVVDGAVEGLDLAALIARHRAAASALIAG | Cofactor: Binds 1 zinc ion per subunit.
Function: Specifically deaminates 8-Oxoguanine (8-oxoG) to uric acid. 8-oxoG is formed via the oxidation of guanine within DNA by reactive oxygen species and leads, if uncorrected, to the incorporation of 8-oxoG:A mismatches and eventually to G:C to T:A transversions.
Catalytic Activity: 8-oxoguanine + H(+) + H2O = NH4(+) + urate
Sequence Mass (Da): 48303
Sequence Length: 449
Pathway: Purine metabolism.
EC: 3.5.4.32
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Q84710 | MASFLKPVNSQGLWLSLLLAITYLFLLPSAGQSLDPSGIGLAAGCSQSQGGISSFAALPRPCNDSVCTLPDLGWSCQRTAQDTANQQQSPFNHTGHFLTTSGWTWPNWTCSPSQCQLLIHLPTWQIVKQDFLLLLKEWDLLTMCQRCSDLLTKTPGFILRFAGETLILVANLIEFVLVSWSLWLCSVLVYVAQAVPGKFLLYMAAFCTTFWAWPRETASSLIRIVTTPLTLIGFLNKTGIGLISHCLALTWNMFMTWSLLPWVTLMKMMKILITSSRVLTRSGRPKRTSSKSLKHKLKISRAIQKKQGKKTPVEERTIPGVQIKKLREDPPKGVILRCTDQFGDHVGYASAVKLEKGQTGIVLPIHVWTDTVYINGPNGKLKMADFTALYEVTNHDSLIMTSAMAGWGSILGVRPRPLTTIDAVKLKNYSLFTERDGKWYVQAAKCIAPAEGMFRVVSDTRPGDSGLPLFDMKMNVVAVHRGTWPSERFPENRAFAILPVPDLTSSSSPKFTGCETYSEAETAYEMADNFSDGEEILIRTKGQSYRTFIGSNKVALLSIRKLEEELSRGPIGLWADDTEDDESAPRRSGNGLFRSTPEKQSQAKTPSPKVEESAAPPPAPRAEKVRHVRRSEMTPEQKRADNLRRRKAKAAKKTPSTPPKKSKDKAPTLSQVAELVEKAVRAALTVQPRRSRASSKISIGGRNPGRKPQVSIQLDPVPSQSTSVPPKDSQAGESAWLGPRRSYRPVQKSTVGQKQEPRRN | Function: Precursor from which the VPg molecule is probably released at the onset of the RNA synthesis. Essential for virus replication (By similarity).
PTM: Specific enzymatic cleavages in vivo yield mature proteins. The protease probably cleaves itself and releases the VPg protein (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84187
Sequence Length: 760
Domain: The C-terminus part of protein P1 and P1-C25 displays RNA-binding properties.
Subcellular Location: Membrane
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P17519 | MNRFTAYAALFFMFSLCSTAKEAGFLHPAFNFRGTSTMSASSGDYSAAPTPLYKSWALPSSLNLTTQPPPPLTDRSYYELVQALTSKMRLDCQTVGDMTWRHLSEMLFASWNSVKEVSLKAASVTLWAIINIWFGLYWTLARLITLFLWTFSIEALCLILLGCITSLIYKGALSLSEHLPVFLFMSPLKIIWRAAFSKRNYKNERAVEGYKGFSVPQKPPKSAVIELQHENGSHLGYANCIRLYSGENALVTAEHCLEGAFATSLKTGNRIPMSTFFPIFKSARNDISILVGPPNWEGLLSVKGAHFITADKIGKGPASFYTLEKGEWMCHSATIDGAHHQFVSVLCNTGPGYSGTGFWSSKNLLGVLKGFPLEEECNYNVMSVIPSIPGITSPNYVFESTAVKGRVFSDEAVKELEREASEAVKKLARFKSLTDKNWADDYDSDEDYGLEREAATNAPAEKTAQTNSAEKTAPSTSAEKTALTNKPLNGQAAPSAKTNGNSDIPDAATSAPPMDKMVEQIITAMVGRINLSEIEEKIVSRVSQKALQKPKQKKRGRRGGKNKQNSLPPTSTQSTSGAPKKEAAPQASGSAGTSRATTTPAPEAKPSGGKNSAKFTPSWRIKQQDSAGQKPDLKLNSKA | Function: Precursor from which the VPg molecule is probably released at the onset of the RNA synthesis. Essential for virus replication. Participates, together with the proteins P0 and P7, in the inhibition of the induction of aphid-induced host phytohormones . This could play a role in the attraction to the infected plants by aphids .
PTM: Specific enzymatic cleavages in vivo yield mature proteins. The protease probably cleaves itself and releases the VPg protein. The VPg protein is probably further cleaved in its C-terminus.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69629
Sequence Length: 639
Domain: The C-terminus part of protein P1 and VPg/P1-C25 displays RNA-binding properties.
Subcellular Location: Membrane
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Q5NDN0 | MALLGIKLMTLVFAAWLSCCHSSSALPSSGLSGPCLNHSCLLRNSLNGASQWGTILHSPAVGSNCPPCPMMSIMGCSPPKPLQSNSYGVLCSTIASKAKQDLKLCWKEVQTRSEMYSKRISAALIDSLHQAVGMLLMIIIWIWSSIFLVVYHVLAYMTTYHLSSAVCVGFLIFCTICAFRLISWICGDLLAFNVSGLTPIWVNFSESSCPAGLSLRRYKNEKTVEGYKPFIIPQKSPKKSVIELSFSNGSHLGYATCVRLWDGSICLMTAKHCLVKEALLKGRVAGHSLPVKNFDLFLTCDEIDFSLLRGPKQWEAYLGVKGADLITSNRIGRSPVTFYNLSKDGEWLANSAQITGRHGKLCSVLSNTSPGDSGTPYYSGKNVVGIHKGTSELENYNLMIPIPNIPGLTSPDFKFETTNVRGNLYNDEGFRLSVGEDDKAEHWTDRLMKSITFKTKRWADWAEEESESDDERGKVVPPAKPSNYGEGCPPEHNQYLSDVGDLLTKVIGPEQNEKCVDILMGIMGVDKNEVAPHKEEKAEKGNEAVVSATVKTVKEPTTQCDEDIISEIVKRVVDKMNLKAIEKSVVEILAEKAMTKAPRGKRKNSKDTSRPSTPGSYIIPAKRTPDSGPVEKSLNSTGRAKEESPSGARTLPGNIPAWVR | Function: Precursor from which the VPg molecule is probably released at the onset of the RNA synthesis. Essential for virus replication (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72353
Sequence Length: 660
Subcellular Location: Host membrane
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P09506 | MYSKLMFFFALCSISFLFTSEAASTMLLESSYLPLNQSYAPGFLYKRDMLPPPLQAVLTYTCPEPRPLAEESYNDLLRAISQKSSSDFQNAYSLALSFSSDFYQHGLKTLKDVSFLAVEKFLWGLTRLWSSLILASFSALWWLVSNFTTPVFCLALLYTVTKYMVKTVSFLFGGLPIWIISIAFSLLKKSFSALRSTPKCLYEKAIDGFKSFTIPQSPPKSCVIPITHASGNHAGYASCIKLYNGENALMTATHVLRDCPNAVAVSAKGLKTRIPLAEFKTIAKSDKGDVTLLRGPPNWEGLLGCKAANVITAANLAKCKASIYSFDRDGWVSSYAEIVGSEGTDVMVLSHTEGGHSGSPYFNGKTILGVHSGASATGNYNLMAPIPSLPGLTSPTYVFETTAPQGRVFAQEDIAEIEGLYAQVMKRVQQAEDFKPKTGKYWGDMEDDEDIFFESKEDLSGNGVRGTVRGTNGEGSSTPKTSNVDGKEMMEKIISSLVGKINLENIERKVIEEISAKAMKTPKSRRRRAPKKQPESSKDTSPRSTTGKYQPPHVRSPASVTAANCPNTTTPSKKKNLAGGRPSSGTIPRWVRKQAASAGPSSAPKQN | Function: Precursor from which the VPg molecule is probably released at the onset of the RNA synthesis. Essential for virus replication (By similarity).
PTM: Specific enzymatic cleavages in vivo yield mature proteins. The protease probably cleaves itself and releases the VPg protein (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66211
Sequence Length: 607
Domain: The C-terminus part of protein P1 and VPg/P1-C25 displays RNA-binding properties.
Subcellular Location: Membrane
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Q10NB9 | MGNGITKNPCFSGDPYAAAVASDPLPDDSHGHSFTYVPSSAAAFDHSPRSAAASSETSYFSLSGAAISANPATSASMPSFRLYNELTWPPSTACTFESSRSFAAAPLIQAAPPRLSMSGPLHATSGRFSEASGSASTASDRFSDHPFMDGMLDRASSASSTARLMPSFSHLMSEPRVAQSGLSNERSLIRSLVRVASKLRFGVPLSGRRSNGPAEPTTKSDGDYRSTPKGNVEWAQGMAGEDRFHVAVSEEHGWVFVGIYDGFNGPDATDYLFANLYVAVHRELKGVLWDDIQGVDVVTDNLPDPALANATHLCFLDAGGVGGGGDDDPDAERKAKRGRIERNADDDGASSVHRDVLKALARALARTEEAFFAAAEERAAQSPELGLVGSCVLVMLMKGKDVYLMNVGDSRAVLARRREPDFKDIFFRPDQDLQLLKAEVMRELEAHDRNGLQCVQLTPEHSAAAEEEVRRIRSQHLTDRQAVVNGRVKGKLSVTRAFGAGYLKQPKWNDRLLEAFKVDYIGAEPYISCTPSLRHHRISSNDRFLVLSSDGLYQYFTNKEVVDQVAMFTAEQPDGDPAKHLVGELVLRAARKAGMDCRRLLEIPHGDRRNYHDDVSIIVMSFEGRIWRSSV | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 68745
Sequence Length: 631
EC: 3.1.3.16
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Q8RWN7 | MGNGTSRVVGCFVPSNDKNGVDLEFLEPLDEGLGHSFCYVRPSIFESPDITPSNSERFTIDSSTIDSETLTGSFRNDIVDDPSFLNRHNSKGLAETTFKAISGASVSANVSTARTGNQMALCSSDVLEPAASFESTSSFASIPLQPLPRGGSGPLNGFMSGPLERGFASGPLDRNNGFMSGPIEKGVMSGPLDVSDRSNFSAPLSFRRKKPRFQRFMRSVSGPMKSTLARTFSRRSGGLSWMHRFFLHPETRVSWAVGKDGKLHGEDPESCLESNRNLQWAHGKAGEDRVHVVLSEEQGWLFIGIYDGFSGPDAPDFVMSHLYKAIDKELEGLLWDYEEPSEDNQLQPDQEPPTEENMCDPESISEQHSKSVVAESEEVMIDDISSLGNTDTQIADGPPGDSAGPGKKSMRLYELLQLEQWEGEEIGLKRYGGNVALNNMTNQVENPSTSGGGAGNDPCTTDRSALDGIPNSGQRHGTKKSQISSKIRRMYQKQKSLRKKLFPWSYDWHREEGICVEEKIVESSGPIRRRWSGTVDHDAVLRAMARALESTEEAYMDMVEKSLDINPELALMGSCVLVMLMKDQDVYVMNVGDSRAILAQERLHDRHSNPGFGNDEGIGHKSRSRESLVRIELDRISEESPIHNQATPISVSNKNRDVTSYRLKMRAVQLSSDHSTSVEEEIWRIRSEHPEDDQSILKDRVKGQLKVTRAFGAGFLKKPNFNEALLEMFQVEYIGTDPYITCEPCTVHHRLTSSDRFMVLSSDGLYEYFSNEEVVAHVTWFIENVPEGDPAQYLIAELLSRAATKNGMEFHDLLDIPQGDRRKYHDDVSVMVVSLEGRIWRSSGQYYPERKQKFNR | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Involved in the regulation of pedicel length and of CLAVATA pathways controlling stem cell identity at shoot and flower meristems.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 95571
Sequence Length: 856
Domain: The N-terminal domain (1-233) has a regulatory function and inhibits phosphatase activity.
Subcellular Location: Nucleus
EC: 3.1.3.16
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Q10MX1 | MSCTVAIPSSPVFSPSRRPLSCKAASASASPESVSVAASSPAQAAPPAGSPLRPFALRAHLREEATPSPQPSAAAAAAVSAPAGSVLKRRRPAPLVVPVCGGAAAAAAAAAVAAVESDPRNEVEEDGEEFAVYCRRGKGRRRVEMEDRHVAKVALGGDPKVAFFGVFDGHGGKSAAEFVAENMPKFMAEEMCKVDGGDSGETEQAVKRCYLKTDEEFLKREESGGACCVTALLQKGGLVVSNAGDCRAVLSRAGKAEALTSDHRASREDERERIENLGGFVVNYRGTWRVQGSLAVSRGIGDAHLKQWVVSDPDTTTLGVDSQCEFLILASDGLWDKVENQEAVDIARPLYISNDKASRMTACRRLVETAVTRGSTDDISIVIIQLQQFSR | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 41315
Sequence Length: 391
Subcellular Location: Membrane
EC: 3.1.3.16
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Q9M8R7 | MGSCLSAESRSPRPGSPCSPAFSVRKRKNSKKRPGSRNSSFDYRREEPLNQVPGRMFLNGSTEVACIYTQQGKKGPNQDAMVVWENFGSRTDTIFCGVFDGHGPYGHMVAKRVRDNLPLKLSAYWEAKVPVEGVLKAITTDTVNNVTNINNPEDAAAAAAFVTAEEEPRTSADMEEENTETQPELFQTLKESFLKAFKVMDRELKFHGSVDCFCSGTTAVTLIKQGQYLVVGNVGDSRAVMGTRDSENTLVAVQLTVDLKPNLPAEAERIRKCRGRVFALRDEPEVCRVWLPNCDSPGLAMARAFGDFCLKDFGLISVPDVSFRQLTEKDEFIVLATDGIWDVLSNEDVVAIVASAPSRSSAARALVESAVRAWRYKYPTSKVDDCAAVCLYLDSSNTNAISTASSISKLEDGEEEELKATTEDDDASGPSGLGRSSTVRSGKEIALDESETEKLIKEADNLDSEPGTEYSALEGVARVNTLLNLPRFVPGK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 53715
Sequence Length: 492
EC: 3.1.3.16
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Q10MN6 | MESAAGEEGKAAPSLPLATLIGRELRGGGSERPLVRYGHFGFAKRGEDYFLVKPDCLRVPGDPSSAFSVFAVFDGHNGVSAAVFSKEHLLEHVMSAVPQGIGRDDWLQALPRALVAGFVKTDIDFQRKGEASGTTATLVVVDGFTVTVASVGDSRCILDTQGGVISLLTVDHRLEENVEERERVTASGGEVSRLNLCGGQEVGPLRCWPGGLCLSRSIGDTDVGEFIVPIPHVKQVKLSNAGGRLIIASDGIWDALSSEAAAQACRGLPAELAAKLVVKQALKTSGLKDDTTCVVVDIIPSDHSSTPPSLSPKKNQNKLRSLLFGRRSHSSVGKLGNKSASFDSVEELFEEGSAMLDERLGRNFPSKANSSPSRCAICQVDQAPFEDLVTDNGGGCCSAPSTPWVGPYLCSDCRKKKDAMEGKRSSRSTACR | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 45829
Sequence Length: 432
EC: 3.1.3.16
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Q9M9W9 | MGHFSSMFNGIARSFSIKKAKNINSSKSYAKEATDEMAREAKKKELILRSSGCINADGSNNLASVFSRRGEKGVNQDCAIVWEGYGCQEDMIFCGIFDGHGPWGHFVSKQVRNSMPISLLCNWKETLSQTTIAEPDKELQRFAIWKYSFLKTCEAVDLELEHHRKIDSFNSGTTALTIVRQGDVIYIANVGDSRAVLATVSDEGSLVAVQLTVDFKPNLPQEEERIIGCNGRVFCLQDEPGVHRVWQPVDESPGLAMSRAFGDYCIKDYGLVSVPEVTQRHISIRDQFIILATDGVWDVISNQEAIDIVSSTAERAKAAKRLVQQAVRAWNRKRRGIAMDDISAVCLFFHSSSSSPSL | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 39780
Sequence Length: 358
EC: 3.1.3.16
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Q5MFV5 | MLRAVARCCGHWPPGAAAADGMLWQTELRPHAAGEFSMAAAQANLAMEDQAQVLASPAATLVGVYDGHGGADASRFLRSRLFPHVQRFEKEQGGMSTEVIRRAFGAAEEEFLQQVRQAWRQRPKMAAVGSCCLLGAISGDTLYVANLGDSRAVLGRRVVGGGVAVAERLTDEHNAASEEVRRELTALNPDDAQIVVHARGAWRVKGIIQVSRTIGDVYLKKQEYSMDPVFRNVGPPIPLKRPALSAEPSIQVRKLKPNDLFLIFASDGLWEHLSDDAAVQIVFKNPRTGIANRLVKAALKEATRKREVSFRDLKTIEKGVRRHFHDDISVIVVYLDRHRGRRHTRVVDSSSNCTNAPVDIYSSNSGQSVETLQAHRGSGW | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 41754
Sequence Length: 380
EC: 3.1.3.16
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Q7XJ53 | MGCVQCKCCSRYPSSSSDGDSRGPLEANGVLKGKDQKPLGSIHVPSPNFDMVYSVLSQRGYYPDSPDKENQDTYCIKTELQGNPNVHFFGVFDGHGVLGTQCSNFVKERVVEMLSEDPTLLEDPEKAYKSAFLRVNEELHDSEIDDSMSGTTAITVLVVGDKIYVANVGDSRAVLAVKDRNRILAEDLSYDQTPFRKDECERVKACGARVLSVDQVEGLKDPNIQTWANEESEGGDPPRLWVQNGMYPGTAFTRSVGDFTAESIGVIAEPEVSMVHLSPNHLFFVVASDGIFEFLPSQAVVDMVGRYADPRDGCAAAAAESYKLWLEHENRTDDITIIIVQIKKLSNE | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 38330
Sequence Length: 348
EC: 3.1.3.16
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Q84T94 | MGNSLACFCCGGGAGGRGGRHVAPAALPSDPAYDEGLGHSFCYVRPDKFVVPFSADDLVADAKAAAAAEGEATTFRAISGAALSANVSTPLSTSVLLLMPEESSASATASSGFESSESFAAVPLQPVPRFSSGPISAPFSGGFMSGPLERGFQSGPLDAALLSGPLPGTATSGRMGGAVPALRRSLSHGGRRLRNFTRALLARTEKFQDSADLGSPDAAAAAVAACGGDPCGLQWAQGKAGEDRVHVVVSEERGWVFVGIYDGFNGPDATDFLVSNLYAAVHRELRGLLWDQREQNVQHDQRPDQPGSAPSTTASDNQDQWGRRRRTRRSRPPRGADDDQRRWKCEWEQERDCSNLKPPTQQRLRCNSENDHVAVLKALTRALHRTEEAYLDIADKMVGEFPELALMGSCVLAMLMKGEDMYIMNVGDSRAVLATMDSVDLEQISQGSFDGSVGDCPPCLSAVQLTSDHSTSVEEEVIRIRNEHPDDPSAISKDRVKGSLKVTRAFGAGFLKQPKWNDALLEMFRIDYVGSSPYISCNPSLFHHKLSTRDRFLILSSDGLYQYFTNEEAVAQVEMFIATTPEGDPAQHLVEEVLFRAANKAGMDFHELIEIPHGDRRRYHDDVSVIVISLEGRIWRSCV | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Protein phosphatase that acts on XA21 pathogen recognition receptor. Negatively regulates cell death and XA21-mediated innate immunity.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 69180
Sequence Length: 639
Subcellular Location: Cell membrane
EC: 3.1.3.16
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Q9SR24 | MGNGVASFSGCCAGTTAGEISGRYVTGVGLVQENLGHSFCYVRPVLTGSKSSFPPEPPLRPDPIPGTTTTFRSISGASVSANTSTALSTSLSTDTSGIASAFESSNRFASLPLQPVPRSPIKKSDHGSGLFERRFLSGPIESGLVSGKKTKEKAKLKKSGSKSFTKPKLKKSESKIFTFKNVFTNLSCSKKSVIKPINGFDSFDGSSDTDRYIPEINSLSTIVSSHEKPRIKEEEDKTESALEEPKIQWAQGKAGEDRVHVILSEENGWLFVGIYDGFSGPDPPDYLIKNLYTAVLRELKGLLWIDKGESYNRNGESNIEKQSTVEHASDSDQENCPVMNGNDVACGSRNITSDVKKLQWRCEWEHNSSNKSNNINHKDVLRALQQALEKTEESFDLMVNENPELALMGSCVLVTLMKGEDVYVMSVGDSRAVLARRPNVEKMKMQKELERVKEESPLETLFITERGLSLLVPVQLNKEHSTSVEEEVRRIKKEHPDDILAIENNRVKGYLKVTRAFGAGFLKQPKWNEALLEMFRIDYVGTSPYITCSPSLHHHRLSSRDKFLILSSDGLYEYFSNEEAIFEVDSFISAFPEGDPAQHLIQEVLLRAAKKYGMDFHELLEIPQGDRRRYHDDVSVIVISLEGRIWRSSM | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 72381
Sequence Length: 650
Domain: The conserved PP2C phosphatase domain (240-639) is interrupted by an insertion of approximately 100 amino acids.
Subcellular Location: Nucleus
EC: 3.1.3.16
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Q7Y138 | MLGALLRLLSACGGVWPTSPAPPARSSSSSSAAAAADQAAAEGRDGLLWWRDLARCHAGELSVAVVQGNHVLEDQCRVESGPPPLAATCIGVFDGHAGPDAARFACDHLLPNLREAASGPEGVTADAIRDAFLATEEGFLAVVSRMWEAQPDMATVGTCCLVGVVHQRTLFVANLGDSRAVLGKKVGRAGQITAEQLSSEHNANEEDVRQELMAQHPDDPQIVALKHGVWRVKGIIQVSRSLGDAYLKHSQYNTEQIKPKFRLPEPFSRPILSANPSIIARCLQPSDCFIIFASDGLWEHLSNQQAVEIVHNHQRAGSARRLIKAALHEAARKREMRYSDLMKIDKKVRRHFHDDITVIVLFINYDQLAKGHSQGQSLSIRCALDH | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 42019
Sequence Length: 386
EC: 3.1.3.16
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P49598 | MAGICCGVVGETEPAAPVDSTSRASLRRRLDLLPSIKIVADSAVAPPLENCRKRQKRETVVLSTLPGNLDLDSNVRSENKKARSAVTNSNSVTEAESFFSDVPKIGTTSVCGRRRDMEDAVSIHPSFLQRNSENHHFYGVFDGHGCSHVAEKCRERLHDIVKKEVEVMASDEWTETMVKSFQKMDKEVSQRECNLVVNGATRSMKNSCRCELQSPQCDAVGSTAVVSVVTPEKIIVSNCGDSRAVLCRNGVAIPLSVDHKPDRPDELIRIQQAGGRVIYWDGARVLGVLAMSRAIGDNYLKPYVIPDPEVTVTDRTDEDECLILASDGLWDVVPNETACGVARMCLRGAGAGDDSDAAHNACSDAALLLTKLALARQSSDNVSVVVVDLRKRRNNQASS | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Major negative regulator of abscisic acid (ABA) responses during seed germination and cold acclimation. Confers insensitivity to ABA. Modulates negatively the AKT2/3 activity, which mediates K(+) transport and membrane polarization during stress situations, probably by dephosphorylation. Prevents stomata closure by inactivating the S-type anion efflux channel SLAC1 and its activator SRK2E. Represses KIN10 activity by the specific dephosphorylation of its T-loop Thr-198, leading to a poststress inactivation of SnRK1 signaling .
PTM: Ubiquitinated by RGLG1 and RGLG5 in response to abscisic acid (ABA). Ubiquitination of PP2CA leads to its degradation by the proteasome.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 43350
Sequence Length: 399
Domain: The 'lock' site stabilizes the complex made of PP2C, ABA and PYR/PYL/RCAR receptor by keeping receptor 'gate' and 'latch' loops in closed positions.
EC: 3.1.3.16
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Q7XP01 | MVMASAGVNMPGGDGDHPPAAAQECHRLRRRRYVPAAAAASEDGDNSSNGGGEKRSLPASSASPSPSPTSSAASSDCSSDRDDDGCSSTAGAAARRLPLPSGASTAAAVWPVAFGSVSLAGRMRDMEDAVSLRPSFCTWLDGSPMHFFAVFDGHGGPHVSALCREQMHVIVAEEMVAEAAALRQRQPAAMEEEEEERAVAGGAVAELRPGGRAGGGGVRVRARHRAGVPCPLSGQTGAIIGSTAVVALLVRDRLVVSNCGDSRAVLCRAGDPLPLSSDHKGLNPSLSWRGTRVALARGTWGDKTGQSVGPAALLLSGGAHPDRPDEKARIEAVGGRVVYLNGPRVRGILAMSRALGDKYLKPEVICEPDITITVRTVDDECLILASDGMWDVISNETASDVARQCLEDGSPTSGRRAARSGEAASSSAGAPAAAVGQESEPRCYRAAALLARLALGRESSDNISVVVIDLKGRG | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 48836
Sequence Length: 474
EC: 3.1.3.16
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Q9LHJ9 | MVSSATILRMVAPCWRRPSVKGDHSTRDANGRCDGLLWYKDSGNHVAGEFSMSVIQANNLLEDHSKLESGPVSMFDSGPQATFVGVYDGHGGPEAARFVNKHLFDNIRKFTSENHGMSANVITKAFLATEEDFLSLVRRQWQIKPQIASVGACCLVGIICSGLLYIANAGDSRVVLGRLEKAFKIVKAVQLSSEHNASLESVREELRSLHPNDPQIVVLKHKVWRVKGIIQVSRSIGDAYLKKAEFNREPLLAKFRVPEVFHKPILRAEPAITVHKIHPEDQFLIFASDGLWEHLSNQEAVDIVNTCPRNGIARKLIKTALREAAKKREMRYSDLKKIDRGVRRHFHDDITVIVVFLDSHLVSRSTSRRPLLSISGGGDLAGPST | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: May dephosphorylate and repress plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), thus influencing negatively plant growth and fitness (By similarity). Involved in pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) signaling . Negatively regulates immune responses by controlling the phosphorylation and activation status of BIK1, a central rate-limiting kinase in PTI signaling . Impairs the phosphorylation of the NADPH oxidase RBOHD by BIK1 .
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
PTM: Phosphorylation at Ser-77 induces dissociation of PP2C38 from BIK1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42851
Sequence Length: 385
Subcellular Location: Cell membrane
EC: 3.1.3.16
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Q7XW27 | MVAVTGGRPPGLQDAPGAPPPAPAAEAVPSRPLARDATYGGRVYGGVGGGGCCLEFLDCVLRAMGVATPAEIMPPADFRWAARPMRRRRRGGSSSSSSSPRDREPRDGRIAANGASAAASLYTMRGNKGVNQDAMLVWENFCSKEDTIFCGVFDGHGPYGHLVSKRVRDLLPIKLSANLGRDGHKETSTNIVTSSMTEGGGTERMDRDTETPLGTEENGDYPEMFAALRTSLLRAFYVMDRDLKFHKTIDSVFSGTTAVTVIKQGHDLLIGNLGDSRAVLGTRDEYDQFFAVQLTVDLKPTIPSEAARIRERSGRIFSLPDEPDVARVWLPKYNMPGLAMARAFGDFCLKDYGLISMPDVSYHRITEKDEFVVLATDGVWDVLSNSEVVSIVSQAKSEASAARFVVESAQRAWRTRFPTSKIDDCAVVCLFLNTDARNKPPGSGIKDLANAIELGGGNLS | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 49687
Sequence Length: 460
EC: 3.1.3.16
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Q7XVF9 | MVDEELFDKSSNDHSISSEEEDMLVRSYSNLNVSFGYHCNSYQCFSLDTDEYDISPNKRLETNTMMTSQNGSFTCLSGAAISANFTLANTNICKGLIGEEILPELDSPNSFRKIVSSPSMSRLDLLSTSQGSPVSTESSIFEISKNIWRSSAPTTVSSNFLTSTEIKMAGGAAGEDRVQAVCSEKNGWLICGIYDGFNGRDAADFLAVTLYDNIVYYLYLLECRIKQENGLYGSPEGSLNGVKSELTLAMRFAENEDVKFSETFRAGVLKCLTTAVEQAENDFLCMVEQEMDDRPDLVSVGSCVLVVLLHGTDLCILNLGDSRAVLASVPSSGMDKLKAVQLTEIHSLENPLEYQKLLADHPNEPSVVMGNKIKGKLKVTRAFGVGYLKQKKLNDALMGILRVRNLCSPPYVYTNPHTVSHKVTEDDLFVVLGSDGLFDFFSNDEVVQLVYQFMHDNPIGDPAKYLIEQLLLKAAKEAALTAEELMRIPVGSRRKYHDDVTIIVIILGNAQRTMTASTSL | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 57320
Sequence Length: 520
EC: 3.1.3.16
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Q9LUS8 | MQEGTDPYGEIEISFGYQCNNKKIGIPEDKIADGREVLGGFRLQKTSSFSCLSGAALSGNPTLANTNICNGVIGSEILPSLDSPKSFRKVPSSPALSKLDILSPSLHGSMVSLSCSSSTSPSPPEPESCYLTSMSSPSSVNEGFLLSAMEVQVAGGAAGEDRVQAVCSEENGWLFCAIYDGFNGRDAADFLACTLYESIVFHLQLLDRQMKQTKSDDDGEKLELLSNISNVDYSSTDLFRQGVLDCLNRALFQAETDFLRMVEQEMEERPDLVSVGSCVLVTLLVGKDLYVLNLGDSRAVLATYNGNKKLQAVQLTEDHTVDNEVEEARLLSEHLDDPKIVIGGKIKGKLKVTRALGVGYLKKEKLNDALMGILRVRNLLSPPYVSVEPSMRVHKITESDHFVIVASDGLFDFFSNEEAIGLVHSFVSSNPSGDPAKFLLERLVAKAAARAGFTLEELTNVPAGRRRRYHDDVTIMVITLGTDQRTSKASTFV | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 53614
Sequence Length: 493
EC: 3.1.3.16
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P22895 | MGFLVLLLFSLLGLSSSSSISTHRSILDLDLTKFTTQKQVSSLFQLWKSEHGRVYHNHEEEAKRLEIFKNNSNYIRDMNANRKSPHSHRLGLNKFADITPQEFSKKYLQAPKDVSQQIKMANKKMKKEQYSCDHPPASWDWRKKGVITQVKYQGGCGRGWAFSATGAIEAAHAIATGDLVSLSEQELVDCVEESEGSYNGWQYQSFEWVLEHGGIATDDDYPYRAKEGRCKANKIQDKVTIDGYETLIMSDESTESETEQAFLSAILEQPISVSIDAKDFHLYTGGIYDGENCTSPYGINHFVLLVGYGSADGVDYWIAKNSWGFDWGEDGYIWIQRNTGNLLGVCGMNYFASYPTKEESETLVSARVKGHRRVDHSPL | Function: Probable thiol protease.
PTM: N-glycosylated on its propeptide.
Sequence Mass (Da): 42794
Sequence Length: 379
Subcellular Location: Vacuole
EC: 3.4.22.-
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P0DJ01 | MKIKKIKLLKALALTGAFGIVATVPVIVSSCSSTSENNGNGNGNGGTDGNTQQTEVTPAIKSEVSLTGALSKIYDTKTGTDRETTSQLIVKDIKANPENYFTNGEALKDVIASATVTVDGGFTESTFTGEAYSVWSAKADVKKGTYSQASKQLDIKSINDLQTVLGDSAAIKGICDLIPNLKLNNGTDYKVTNNGLSLSEDLLHINVTAKDGQTDVSMDLAIPVSDLNLKIDGLKISVSGTGIKTSELTTNYKFNIGIDNTVKTLTPAAVTLAEADRTNAEKVLEKLGYATVSGSTYTLDQDKLADALGLYNCKFEAVKSEKDSTNNNKYTVTLKATPNDGYFWEDGTNGAKEEISFVATFS | Function: Major M.penetrans antigen.
PTM: The N-terminus is blocked.
Location Topology: Lipid-anchor
Sequence Mass (Da): 38384
Sequence Length: 362
Subcellular Location: Cell membrane
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P15363 | MLKKLKNFILFSSIFSPIAFAISCSNTGVVKQEDVSVSQGQWDKSITFGVSEAWLNKKKGGEKVNKEVINTFLENFKKEFNKLKNANDKTKNFDDVDFKVTPIQDFTVLLNNLSTDNPELDFGINASGKLVEFLKNNPGIITPALETTTNSFVFDKEKDKFYVDGTDSDPLVKIAKEINKIFVETPYASWTDENHKWNGNVYQSVYDPTVQANFYRGMIWIKGNDETLAKIKKAWNDKDWNTFRNFGILHGKDNSFSKFKLEETILKNHFQNKFTTLNEDRSAHPNAYKQKSADTLGTLDDFHIAFSEEGSFAWTHNKSATKPFETKANEKMEALIVTNPIPYDVGVFRKSVNQLEQNLIVQTFINLAKNKQDTYGPLLGYNGYKKIDNFQKEIVEVYEKAIK | Function: P37 is part of a high-affinity transport system.
Location Topology: Lipid-anchor
Sequence Mass (Da): 46118
Sequence Length: 403
Subcellular Location: Cell membrane
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P75371 | MLKRKKLLQGFLKFLPLIIPATIFVSCARRESNHLIFNISLDHDADASISKFFELYSNNLSKKLDKKVTVSFNIIDDSFTKISNIQTAKADFAFVNSQSIKDNGIEEFNLILQTQTDAFKEDTNLDYYSDGQLKSKAEKMTTLFSKTPYKDWEDTAQQWTGSRYNFLYETNKLINFYRGMILITGSEEEIKKIKEAWDQKKWSDFMNYGIGHGSSGSAGKFQLPDLLLRKHFGSSYPGLQNAINQNPDKFANVRGREIGRDNKIKIVFDDANSFAWTHNDKNATNHFYTPTENNGKGDSEKSNNKNNKVEILTYTDPMLYDIGIVSDTLSDRYQKAIAEVFVELAKTKQDIYGPSYGYNGYNLITDPNKEILDVIHKTYG | Function: P37 is part of a high-affinity transport system.
Location Topology: Lipid-anchor
Sequence Mass (Da): 43495
Sequence Length: 380
Subcellular Location: Cell membrane
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P0DTK2 | MDYKFLAGFALGFSSAIPFSVAGLYFVYLKISSHVRSIVNEYGRG | Function: Together with movement protein P17, plays an essential role in virus long distance movement.
Sequence Mass (Da): 4980
Sequence Length: 45
Domain: The C-terminus regulates the targeting to host mitochondria.
Subcellular Location: Host cell junction
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Q96480 | METVDSTRAFVKNVKRLIVKVGTAVVTRADGRLALGRLGALCEQLQELNSQGYEVILVTSGAVGVGRQRLRYRKLLNSSFLDLQKPQTELDGKACAAVGQNGLMALYDSLFSQLDVTSAQLLVTDNDFRDPDFRRQLNDTVNSLLSLKVIPIFNENDAISTRRAPYEDSSGIFWDNDSLAALLALELKADLLVLLSDVDGLYSGPPRDPDSKLIYTYIKEIHERVITFGDKSRVGRGGMTAKVKAAMYAAYAGIPVVITSGFATDNIIKVLHGERIGTLFHCDANKWASIGETDAREMAVAARACSRRLQALSSQERSKILQDIADALEANEKAILAENEADVVAAQQAGYEKSLISRLALNPGKISSLANSVRVLSNMDEPLGHTLKRTEIADGFILEKSSSPLGVVLIIFESRPDALVQIASLAVRSGNGLMLKGGKEAKRSNAILHKVITSAIPVSVGERLIGLVTSREEIPELLKLDDVIDLVIPRGSNKLVSQIKASTKIPVLGHADGICHVYVDKSADMDMAKRITVDAKIDYPAACNAMETLLVHKDLAQNGGLNDLIVELQTKGVSLYGGPKASSLLMIPEARTFRHEYSSLACTVEVVEDVYAAIDHIHQHGSAHTDSIITEDQEVAEVFLRQVDSAAVFHNASTRFSDGFRFGLGAEVGISTGRIHARGPVGVEGLLTTKWLARGSGQIVDGDKSIVYSHKDLTQQG | Function: P5CS plays a key role in proline biosynthesis, leading to osmoregulation in plants.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 77590
Sequence Length: 717
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.
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Q8NBR0 | MAPPPPSPQLLLLAALARLLGPSEVMAGPAEEAGAHCPESLWPLPPQVSPRVTYTRVSPGQAEDVTFLYHPCAHPWLKLQLALLAYACMANPSLTPDFSLTQDRPLVLTAWGLALEMAWVEPAWAAHWLMRRRRRKQRKKKAWIYCESLSGPAPSEPTPGRGRLCRRGCVQALALAFALRSWRPPGTEVTSQGPRQPSSSGAKRRRLRAALGPQPTRSALRFPSASPGSLKAKQSMAGIPGRESNAPSVPTVSLLPGAPGGNASSRTEAQVPNGQGSPGGCVCSSQASPAPRAAAPPRAARGPTPRTEEAAWAAMALTFLLVLLTLATLCTRLHRNFRRGESIYWGPTADSQDTVAAVLKRRLLQPSRRVKRSRRRPLLPPTPDSGPEGESSE | Function: May act as a tumor suppressor. Inhibits tumor cell growth, when overexpressed.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 42238
Sequence Length: 393
Subcellular Location: Cell membrane
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Q5F267 | MVHPPPPPPRLLLVALVGLLSLREVVAEPAEEAGTPCPEGLWPVPPQVLPRVTYTQVSQGQAEGIAFFYHPCAHPWLKLQLALLAHLYVAKPTLIPDFSLTWDRPLVLTAWGTALELAWIEPAWVAHWLKRQRRRKQRKSVWFLSDNLFGPTPTMPASRRGKLCGRRCVQAPTLAFALRSWRPPGAQVTSRGSGRSSISVVKRRGLRAALGLQSTPPGLRVSLASSQSLKAQQLTLGTSSVAPVSLTTGGPGGNGRSRTEAQMPSGQGNHGGCACPGQVSPAPRAAGPPRVARGPTPRTEEAAWAAMALTFLLVLLTLATLCTRLHRNFRRSESIYWGPTADSQDTVAALLKRRLPLPSRRIKRSRRRPLLPPTPDSGPDSESSD | Function: May act as a tumor suppressor. Inhibits tumor cell growth, when overexpressed (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 41766
Sequence Length: 385
Subcellular Location: Cell membrane
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P0DQP9 | SLWEFGQMILKETGKLPFPYYGAYGCYCGWGGRRGPKDATDRCCYVHDCKQICECDKAAAVCFRERKYMAYLRVLCKK | Cofactor: Binds 1 Ca(2+) ion.
Function: Snake venom phospholipase A2 (PLA2) that exhibits myotoxin and anticoagulant activity . Displays edema-inducing activities in mouse paw . Also displays cytotoxic activity against some cell lines and myotubes, and antimicrobial activities against E.coli, C.albicans and Leishmania . PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Mass (Da): 9051
Sequence Length: 78
Subcellular Location: Secreted
EC: 3.1.1.4
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P0DM51 | DLWQFGKMILKVAGKLPFPYYGAYGCYCGWGGRGKPKDPTDRCCFVHDCC | Cofactor: Binds 1 Ca(2+) ion.
Function: Snake venom phospholipase A2 (PLA2). In vitro, shows anticoagulant activity and induces cytotoxicity when tested on C2C12 myoblasts/myotubes. In vivo, when tested on mice, induces myotoxicity (intramuscular injection), edema (injection in the subplantar region) and lethality. Also induces neurotoxic effect on mouse neuromuscular preparations and has bactericidal activity on the Gram-negative bacteria E.coli (ATCC29648) and the Gram-positive S.aureus (ATCC 25923). The catalytic and anticoagulant activities of BnpTX-I are higher than those of BnpTX-II. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
PTM: Contains 7 disulfide bonds.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Mass (Da): 5653
Sequence Length: 50
Subcellular Location: Secreted
EC: 3.1.1.4
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P0C942 | HLLKFNKMIKFETRKNAIPFYAFYGCYCGWGGRXXXXXXXXXCCFVHDCCYGKXXXXXXXWDLYRYSLKSGYLTCGKGTWCEEQICECDRVAAECLRRSLSTYKYGYMFYPDSRCRGPSETC | Cofactor: Binds 1 Ca(2+) ion.
Function: Snake venom phospholipase A2 (PLA2) that displays neurotoxic and myotoxic activities. Induces inflammatory edema by mechanisms involving mast cell activation and arachidonic acid metabolites. Increases plasma creatine kinase activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Mass (Da): 14284
Sequence Length: 122
Subcellular Location: Secreted
EC: 3.1.1.4
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P28305 | MFLINGHKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDFWPQLEQEMKTLAAEQQNGVLKVVISRGSGGRGYSTLNSGPATRILSVTAYPAHYDRLRNEGITLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMPVMPVCACGDVSFSSATLYEYLAPLCERPN | Function: Involved in the biosynthesis of p-aminobenzoate (PABA), a precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate.
Catalytic Activity: 4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate
Sequence Mass (Da): 29715
Sequence Length: 269
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-aminobenzoate from chorismate: step 2/2.
EC: 4.1.3.38
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O42951 | MEESNLFETTLYDGELFLLPSHLQRMKASAKSLGYSWPGEQYIENKLREAVQDTSMARVRWELSKAGDVTVQIVPIQTLEKAPYTLILDKQPSSTEKNPSCINKMTNRAIYIEAMNRNDAQYSKAQDVLLYNHQGFVTEATIFNVAFHRNGQWITPSLKHGLLSGTMRKNLLENGSIHEDDKGLLQKDNLKNGEQVLLFNSFRKVCKGVLIIQPEKACELLKKKDSSEKLS | Function: Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate.
Catalytic Activity: 4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate
Sequence Mass (Da): 26264
Sequence Length: 231
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-aminobenzoate from chorismate: step 2/2.
Subcellular Location: Cytoplasm
EC: 4.1.3.38
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Q9KQI0 | MYWVNGQRRNEVPIHDRSFQYGDGCFTTILTKEGQVQQWSSHKARLQACLDILHIPEPNWDRVWQGLQSMILPQEKAGLKIHISRGLGGRGYSPTQVSESIVTISAFAFPAHYQAWRDKGLAVGICQQRMGLNPLLAGHKHNNRLEQILLKREMDNAGWDDGVCLDINGKVIETTAANIFWCRDGTMFTPCLRHAGVAGVARRQILELAQQQEIPIVIDEFTLEDLLSAEEVFITNALLEVAPVTQIGQQRLTIGSMTRRFQESSNS | Function: Involved in the biosynthesis of p-aminobenzoate (PABA), a precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate (By similarity).
Catalytic Activity: 4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate
Sequence Mass (Da): 30063
Sequence Length: 267
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-aminobenzoate from chorismate: step 2/2.
EC: 4.1.3.38
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Q03266 | MSLMDNWKTDMESYDEGGLVANPNFEVLATFRYDPGFARQSASKKEIFETPDPRLGLRDEDIRQQIINEDYSSYLRVREVNSGGDLLENIQHPDAWKHDCKTIVCQRVEDMLQVIYERFFLLDEQYQRIRIALSYFKIDFSTSLNDLLKLLVENLINCKEGNSEYHEKIQKMINERQCYKMRVLVSKTGDIRIEAIPMPMEPILKLTTDYDSVSTYFIKTMLNGFLIDSTINWDVVVSSEPLNASAFTSFKTTSRDHYARARVRMQTAINNLRGSEPTSSVSQCEILFSNKSGLLMEGSITNVAVIQKDPNGSKKYVTPRLATGCLCGTMRHYLLRLGLIEEGDIDIGSLTVGNEVLLFNGVMGCIKGTVKTKY | Function: Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate.
Catalytic Activity: 4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate
Sequence Mass (Da): 42640
Sequence Length: 374
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-aminobenzoate from chorismate: step 2/2.
Subcellular Location: Cytoplasm
EC: 4.1.3.38
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Q93VI4 | MPVHDEQEHEVYGGEIPEEEEGEMDTEEYEEHGGEEGAAAGDEELEPGSSSRDLEDMKKRIKEIEEEAGALREMQAKAEKDMGASQDPSGGVSAAEKEEVDSRSIYVGNVDYACTPEEVQQHFQSCGTVNRVTILTDKFGQPKGFAYVEFVEVEAVQNSLILNESELHGRQIKVSAKRTNVPGMRQFRGRGRPFRPMRGFMPGVPFYPPYAYGRVPRFRRPMRYRPY | Function: Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length. Increases the affinity of poly(A) polymerase for RNA. Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation.
Sequence Mass (Da): 25671
Sequence Length: 227
Domain: The RRM domain is essential for the recognition of specific adenine bases in the poly(A) tail, but not sufficient for poly(A) binding.
Subcellular Location: Nucleus speckle
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Q9FJN9 | MEEEEHEVYGGEIPDVGEMDGDMEALNPDLDMAAADDDAVKELDEMKKRLKEMEDEAAALREMQAKVEKEMGAQDPASIAANQAGKEEVDARSVFVGNVDYACTPEEVQQHFQTCGTVHRVTILTDKFGQPKGFAYVEFVEVEAVQEALQLNESELHGRQLKVLQKRTNVPGLKQFRGRRFNPYMGYRFRRPFMSPYMYSPYGYGKAPRFRRPMRYMPYQ | Function: Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length. Increases the affinity of poly(A) polymerase for RNA. Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation.
Sequence Mass (Da): 25250
Sequence Length: 220
Domain: The RRM domain is essential for the recognition of specific adenine bases in the poly(A) tail, but not sufficient for poly(A) binding.
Subcellular Location: Nucleus speckle
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Q9LX90 | MEEEEHEVYGGEIPEVGDTDVPDPDIDMSAADEDAVTELAEMKRRLKEMEEEAAALREMQAKVEKEMGATQDPASMAANQEGKEEVDARSVYVGNVDYACTPEEVQLHFQTCGTVNRVTILMDKFGQPKGFAYVEFVEVEAVQEALQLNESELHGRQLKVSPKRTNVPGMKQYHPGRFNPSMGYRFRRPFVPPYFYSPYGYGKAPRFRRPMRYMPYQ | Function: Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length. Increases the affinity of poly(A) polymerase for RNA. Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation.
Sequence Mass (Da): 24804
Sequence Length: 217
Domain: The RRM domain is essential for the recognition of specific adenine bases in the poly(A) tail, but not sufficient for poly(A) binding.
Subcellular Location: Nucleus speckle
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P11940 | MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAAAAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV | Function: Binds the poly(A) tail of mRNA, including that of its own transcript, and regulates processes of mRNA metabolism such as pre-mRNA splicing and mRNA stability . Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2 . Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs . Involved in translationally coupled mRNA turnover . Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain . Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed . By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability .
PTM: Phosphorylated by MAPKAPK2.
Sequence Mass (Da): 70671
Sequence Length: 636
Domain: The RNA-binding domains RRM1 and RRM2 and the C-terminus (last 138 amino acids) regions interact with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1, respectively.
Subcellular Location: Cytoplasm
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P29341 | MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKELFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAAAAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPSLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV | Function: Binds the poly(A) tail of mRNA, including that of its own transcript, and regulates processes of mRNA metabolism such as pre-mRNA splicing and mRNA stability. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability.
PTM: Phosphorylated by MAPKAPK2.
Sequence Mass (Da): 70671
Sequence Length: 636
Domain: The RNA-binding domains RRM1 and RRM2 and the C-terminus (last 138 amino acids) regions interact respectively with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1, respectively.
Subcellular Location: Cytoplasm
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Q5R8F7 | MNPSAPSYPMASLYVGDLHPDATEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAAAAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV | Function: Binds the poly(A) tail of mRNA, including that of its own transcript, and regulates processes of mRNA metabolism such as pre-mRNA splicing and mRNA stability. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability.
PTM: Phosphorylated by MAPKAPK2.
Sequence Mass (Da): 70643
Sequence Length: 636
Domain: The RNA-binding domains RRM1 and RRM2 and the C-terminus (last 138 amino acids) regions interact respectively with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1, respectively.
Subcellular Location: Cytoplasm
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Q7KNF2 | MADEDITLNEDQLLESLEETNGEQETEIATEVEEEGSMQIDPELEAIKARVKEMEEEAEKIKQMQSEVDKQMAGGSTTGLATVPLSLEEKQEIDTRSVYVGNVDYGASAEELEAHFHGCGTINRVTILCNKADGHPKGFAYIEFGSKEFVETALAMNETLFRGRQIKVMSKRTNRPGLSTTNRFARGSFRGRGARVSRACCHSTFRGARRAMGYRGRANYYAPY | Function: Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product . Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length (By similarity). Increases the affinity of poly(A) polymerase for RNA (By similarity). Binds to poly(A) and to poly(G) with high affinity . May protect the poly(A) tail from degradation (By similarity). Plays a role in the positive regulation of alpha-1,3 fucosylation, possibly by cooperating with swm which regulates nuclear export of fucosyltransferase FucTA .
Sequence Mass (Da): 24978
Sequence Length: 224
Domain: The RRM domain is essential for specific adenine bases recognition in the poly(A) tail but not sufficient for poly(A) binding.
Subcellular Location: Nucleus
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A1SK16 | MDRRIFGIENEYGVTCTFKGQRRLSPDEVARYLFRKVVSWGRSSNVFLRNGARLYLDVGSHPEYATPECDDVVELVTHDKAGERVLEGLLLDAEQRLHDEGIAGEIYLFKNNTDSAGNSYGCHENYLVSRAGEFSRLADVLIPFLVTRQIIVGAGKITQTPRGASYSVSQRAEHIWEGVSSATTRSRPIINTRDEPHADAEKYRRLHVIVGDSNMSETTTMLKVASCDLVLRMIEEGVVMRDLTMENPIRAIREISHDVTGRRKVRLANGREASALDIQQEYLTKARDFVDRRELSTPLIEQALDLWERGLKAVEADDLGLVDREIDWVIKWKLIERYRAKHGLPLGHPRIAQLDLAYHDIHRGRGLYYLLEKRGAVARVTTDLKIFEAKSVPPQTTRARLRGEFIRRAQERRRDFTVDWVHLKLNDQAQRTVLCKDPFRAHDERVQRLIDGM | Function: Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side-chain amino group of a substrate lysine.
Catalytic Activity: ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N(6)-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine.
Sequence Mass (Da): 51939
Sequence Length: 453
Pathway: Protein degradation; proteasomal Pup-dependent pathway.
EC: 6.3.1.19
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