ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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P07602 | MYALFLLASLLGAALAGPVLGLKECTRGSAVWCQNVKTASDCGAVKHCLQTVWNKPTVKSLPCDICKDVVTAAGDMLKDNATEEEILVYLEKTCDWLPKPNMSASCKEIVDSYLPVILDIIKGEMSRPGEVCSALNLCESLQKHLAELNHQKQLESNKIPELDMTEVVAPFMANIPLLLYPQDGPRSKPQPKDNGDVCQDCIQMVTDIQTAVRTNSTFVQALVEHVKEECDRLGPGMADICKNYISQYSEIAIQMMMHMQPKEICALVGFCDEVKEMPMQTLVPAKVASKNVIPALELVEPIKKHEVPAKSDVYCEVCEF... | Function: Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the... |
O07802 | MWSTVLVLALSVICEPVRIGLVVLMLNRRRPLLHLLTFLCGGYTMAGGVAMVTLVVLGATPLAGHFSVAEVQIGTGLIALLIAFALTTNVIGKHVRRATHARVGDDGGRVLRESVPPSGAHKLAVRARCFLQGDSLYVAGVSGLGAALPSANYMGAMAAILASGATPATQALAVVTFNVVAFTVAEVPLVSYLAAPRKTRAFMAALQSWLRSRSRRDAALLVAAGGCLMLTLGLSNL | Function: Required for the transport across the inner membrane of sulfolipid-1 (SL-1), which is a major cell wall lipid of pathogenic mycobacteria. Could also transport SL1278 (2-palmitoyl-3-(C43)-phthioceranyl-alpha, alpha'-D-trehalose-2'-sulfate), which is the precursor of SL-1. May potentiate SL-1 levels and confer ... |
P08635 | METAVNAKSPRNEKVLNCLYQNPDAVFKLICFPWAGGGSIHFAKWGQKINDSLEVHAVRLAGRETRLGEPFANDIYQIADEIVTALLPIIQDKAFAFFGHSFGSYIALITALLLKEKYKMEPLHIFVSGASAPHSTSRPQVPDLNELTEEQVRHHLLDFGGTPKHLIEDQDVLRMFIPLLKADAGVVKKFIFDKPSKALLSLDITGFLGSEDTIKDIEGWQDLTSGKFDVHMLPGDHFYLMKPDNENFIKNYIAKCLELSSLT | Function: Contributes to the release of free fatty acids from fatty acid synthase (FASN). Has broad substrate specificity, giving rise to a range of free fatty acids with chain lengths between 10 and 16 carbon atoms (C10 - C16).
Catalytic Activity: (9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP]
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A0A084API2 | MLDDDCSPTSSSEMSNASSREASITSRSSSTSGNNSLPEDRGAVVQLPTLNPSDYRWHPFPGDSSVLQRKAIGVEALVGIRDANSRGEYDFYNNIVLRVGNALELTLTRLKRAFVKAMLDARFENPSIACYGVWGQNKEQYLPHIQYKSFKSQSEALAWANNCIIIQATSLTGSELRAERLKKRRAQAVPQPSNPLDIIIYADVANQRNRLEPGTEVNILFLFNHLIWDGKGRYFTSELVQRATTILDQEKENIMPTHRWGEEKSRLDPPILDVMLVNLDKMGPDYDLAHRKLLNSQLQVGLSWGLPLTRNPGEPLQIRH... | Function: Putative 15-O-acetyltransferase; part of the satratoxin SC2 cluster involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings . Satratoxins are suggested to be made by products of multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins in al... |
A0A084API4 | MATIPIRLQALATDQTVLKLPHPYKTEFAVRKASKASTKLPVYNLVPKPFPTRPLPFELHNDHLVFTDAIHLKSSELPPDSNNGAWARARRAPCVTLYWDGVEVPTLKQAWLVVYAFFTMRPGMDSFRLELDGNSAANLARQIKDVLLGIDHPIKARQQQEPCAKTKENTLLILRSTFWQGAGCPFGPRPVWCPQESPSSLLPSTCLSSFPLAPFHRTSTISLAGDPEDFDRCQQSWHPIRPAKPAPGSIIYSRWIPYLGEMFSMVALDPEDSEHVRLFHEWQSDPRVLQGWTETKTLDQHRRYLEALHKDPHQLTVLAK... | Function: Putative O-acetyltransferase; part of the satratoxin SC2 cluster involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings . Satratoxins are suggested to be made by products of multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins in all, ... |
A0A084API6 | MVELNPVTITNDNATPRGHVLKLILVESRDIIRAVKTRLCPQYTISYLAQAATVIAMLDTYSSKSELSKPDFFVALTVVNGRRYLREDLESNYLAGYVTGAPIKIEKLRSLLVSLDDSKDIIVSALEKAAKDAKRRLDMWIYDQSQLATGFRIHSFKGAMSSENPELFKKTAVPYLSSYGINEV | Function: Trichothecene 15-O-acetyltransferase; part of the satratoxin SC2 cluster involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings . Satratoxins are suggested to be made by products of multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins ... |
A0A084AFG6 | MAASPVLATTSHPIGHEAAVVTDADLDRHYAVKLAGKLNDEMAWVGQQFTGEEDFVVCLSEADVAEVNAALTAFQDTGLKPGYLSPETFKLPKLGPKLRLLSQRIHEQEGFIVLRGLQPWRYRRLENTIVFTGIASYIGNRRGVQCADGPVMTHIFDYSTEVEEKEKLNDGYLGHANRTSYLPFHTDDGHIISLYCLQAADIGGRTLLASSHAIYNHLLETRPDVIETLKEEWIWDSFIPEKPSFIRPLLLEQDGKLICNYRIRPFLGTPGYPRNAALGPLPAHQEEALNTVAEIAEKLSLKFEFKTGDIQFLNNLSILH... | Function: Taurine hydroxylase-like protein; part of the satratoxin SC3 cluster involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings . Satratoxins are suggested to be made by products of multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins in a... |
A0A084AFG7 | MKLVEIAEDILSKANAYTNNTGLTSSQRFQLREEIRYQANGILSAIDGPEQTMKAIARSYTTCTALKVCVDLKLASHLPLSDARSLSQLAQICGCDSLVLRPMLRLLAKNGIFEQVDAETWQHTELSAVMAQPPFQALEEKYRSVAHLPRLLQAVSHQFPTPGRTAFNQVYCTSLDFYTYSNELDHAAARNFAFSMKELARNQIPFVQQSYPLETIDPESHFIDVAGGVGYLSFFLAGSFPKATFEVQDHPFIIEEAHSVCPSELRDRITFRAHNILHPQPEIAKEINGRLVFLVKIILHDHGDDDCRLMLRNLVSVMKQ... | Function: O-methyltransferase; part of the satratoxin SC3 cluster involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings . Satratoxins are suggested to be made by products of multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins in all, including... |
A0A084AFG8 | MATATPPPQDFPPYPPFTSLRLAAARDVAQMANLSVQGFKDSEIFRYERPGHDQYPEDAVAYFANLYRDRLEDPRAVVIVAEDWDGAERVVVGVGCWILPQDSPRTGQFVVPCVGDREPALDRDLCCRRLELFNAVTKATEERYLDGKVICDKFVVHPSYQRRGHGTAMLRWSLRLCTQDTVDQGVIPSHVGEPVYLSLGFEVIGEMHVPDEGDTQGFTQRVAVYKARQT | Function: Acetyltransferase; part of the satratoxin SC3 cluster involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings . Satratoxins are suggested to be made by products of multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins in all, including p... |
Q42588 | MATCIDTCRTGNTQDDDSRFCCIKNFFRPGFSVNRKIHHTQIEDDDDVWIKMLEEAKSDVKQEPILSNYYYASITSHRSLESALAHILSVKLSNLNLPSNTLFELFISVLEESPEIIESTKQDLIAVKERDPACISYVHCFLGFKGFLACQAHRIAHTLWKQNRKIVALLIQNRVSESFAVDIHPGAKIGKGILLDHATGVVIGETAVVGDNVSILHGVTLGGTGKQSGDRHPKIGDGVLIGAGSCILGNITIGEGAKIGSGSVVVKDVPARTTAVGNPARLIGGKENPRKHDKIPCLTMDQTSYLTEWSDYVI | Function: Serine acetyltransferase which catalyzes the formation of O-acetyl-L-serine from acetyl-CoA and L-serine . Also displays O-acetylserine (thio1)-lyase activity in vitro . May be involved in detoxification process by mediating the production of glutathione.
Catalytic Activity: acetyl-CoA + L-serine = CoA + O-ac... |
O34764 | MSLAPHGGTLVNRVDESYDVSGIQKEIELDLISFADLELIGIGAYSPIEGFFNEKDYVSVVENMRLSSGVVWSLPITLPVDAQKAAELSLGETVKLTYEGETYGVIQIEDLYVPDKQKEAVNVYKTDEQEHPGVKKLFSRGNTYVGGPITLIKKASKQFPEFTFEPSETRRQFAEKGWETIVGFQTRNPVHRAHEYIQKTALETVDGLFLNPLVGETKSDDIPADVRMESYQVLLDHYYPKDRVFLGVFLAAMRYAGPREAIFHALVRKNYGCTHFIVGRDHAGVGDYYGTYEAQELFDTFKPEELGITPLKFEHSFFCK... | Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Mass (Da): 42884
Sequence Length: 382
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
EC: 2.7.7.4
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Q3T0Q0 | MAKFVIRPATAADCSDILRLIKELAKYEYMEEQVMLTEKDLLEDGFGEHPFYHCLVAEVPKEHLTPEGHSIVGFAMYYFTYDPWIGKLLYLEDFFVMSDYRGFGIGSEILKKLSQVAMKCRCSSMHFLVAEWNEPSINFYKRRGASDLSSEEGWRLFKIDKEYLLKMAAEE | Function: Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine = spermidine >> spermine > N(1)-acetylspermine. This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines. Also involved in the regulation of polyamine transport out of cell... |
Q8AXL1 | MASFSIRAARPEDCSDLLRLIKELAKYEDMEDQVVLTEKELLEDGFGEHPFYHCLVAEVPKEQWSSEGHSIVGFAMYYFTYDPWIGKLLYLEDFYVMAEYRGLGIGSEILKNLSQVAVKCRCSSMHFLVAEWNEPSIRFYKRRGASDLSTEEGWRLFKIDKEYLLKMATEE | Function: Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine = spermidine >> spermine > N(1)-acetylspermine. This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines. Also involved in the regulation of polyamine transport out of cell... |
Q9LR00 | MAMKKANKLTQTAMIKQILKRCSSLGKKQSNVYGEDENGSPLNVPKGHFVVYVGENRVRYVVPISFLTRPEFQLLLQQAEEEFGFDHDMGLTIPCEEVVFRSLTSMLR | Function: Provide a mechanistic link between auxin and plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), and triggers PM H(+)-ATPases activity by promoting phosphorylation of their C-terminal autoinhibitory domain as a result of PP2C-D subfamily of type 2C phosphatases inhibition, thus leading to the ... |
Q9FXI0 | MAIINRSKLTQTTMIKQILKRCSSLGKKQSSEYNDTHEHDGDSLPLDVPKGHFVVYVGGNRVRYVLPISFLTRPEFQLLLQQAEEEFGFDHNMGLTIPCEEVAFKSLITSMLQPTYI | Function: Provide a mechanistic link between auxin and plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), and triggers PM H(+)-ATPases activity by promoting phosphorylation of their C-terminal autoinhibitory domain as a result of PP2C-D subfamily of type 2C phosphatases inhibition, thus leading to the ... |
Q9C7Q8 | MMINAKKLMKLAKKWQQRAALKRKRISFQRSSITTSSQTAVEKGCFVVYTADKIRFSFPLSYLSNTIVQELLKISEEEFGLPTEGPITLPFDSAFLEYLINLIQRRMDEDTEKALLLSISSARSSFQPQQHCSATQQLLVF | Function: May promote auxin-stimulated organ elongation, such as hypocotyls, stamen filaments and petals.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16142
Sequence Length: 141
Subcellular Location: Cell membrane
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Q0V7Z5 | MMNTKKLIKMAKKWQQRAALHRKRISFQRSSSATSSTAAEKGCFVVYTTDSTRFAFPLSYLSNSVFQELLKISEEEFGLPTGGPITSPFDSVFLEYLIKLVQRRMDADTEKALLMSISSARCSSQCSLKLQERSTQQLLVF | Function: May promote auxin-stimulated organ elongation, such as hypocotyls, stamen filaments and petals.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15976
Sequence Length: 141
Subcellular Location: Cell membrane
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Q0WPR6 | MINTKKLLKMAKKWQQRAALKRKRISFQRSTTTTTTTTTTTSSSTAVEKGCFVVYTVDKIRFAFPLSYLNNSVFEELLKISEEEFGLRAGGPITLPFDSVFLEYLIKFIERRMDGDTEKALLMSISSARCSMQPQEQQSGYTQQLLVF | Function: May promote auxin-stimulated organ elongation, such as hypocotyls, stamen filaments and petals.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16916
Sequence Length: 148
Subcellular Location: Cell membrane
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Q9C7Q1 | MMNTKKLIKMFRKWQQRAALHRKRISFQRPSTRSTTVEKGCFVVYTADNTRFAFPISYLSNSVFQEILEISEEEFGLPTGGPITLPFDSVFLEYLIKLIKRRMDGDTEKALLMSISSARCSLQKQEQSTQQLLVF | Function: May promote auxin-stimulated organ elongation, such as hypocotyls, stamen filaments and petals.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15664
Sequence Length: 135
Subcellular Location: Cell membrane
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Q29Q96 | MMNTKKLMKMAKKWQQRAALRRKRISFQRSNSTTSSSSAVEKGCFVVYTADQVRFAFPISYLSNSVIQELLKISEEEFGIPTEGPITLPFDSIRFSWSISSN | Function: May promote auxin-stimulated organ elongation, such as hypocotyls, stamen filaments and petals.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 11661
Sequence Length: 102
Subcellular Location: Cell membrane
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Q29PU2 | MAKGGNKLMKLKSVLKKLNSFNTKPNQPPAQTNHSRSSAVSAFPSEDLQTVYVGRTRRTYHVSSDVVSHPLFQQLAAVDGGCGSEDGSISVSCEVVLFEHLLWMLENADADESRPESVYELVEFYAC | Function: May be involved in the regulation of ethylene receptor signaling. Promotes cell expansion and plant growth (Probable). Involved in the regulation of cell elongation .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13981
Sequence Length: 127
Subcellular Location: Nucleus
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O65648 | MAIKKSNKAALSQAASLKQILKRCSSLGKKNQGNCYFNDVPKGHFPVYVGQHRSRYVVPISWLDHHEFQSLLQLAEEEFGFEHEMGLTIPCDEVVFRSLISMFR | Function: Provide a mechanistic link between auxin and plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), and triggers PM H(+)-ATPases activity by promoting phosphorylation of their C-terminal autoinhibitory domain as a result of PP2C-D subfamily of type 2C phosphatases inhibition, thus leading to the ... |
A9QY39 | MTKVVQFSLLLALILVLSVSLASAASQNLEFTELEDEDQSNLSTYIVHVRKPQVIQSDDLHTFYYSLLPESTKTTNQRIVFTYRNVVNGFAVKLTPEEAKALQQNEEVVSARPEKILSLHTTHTPSFLGLQQGLGLWKGSNSGKGVIIGILDTGISPFHPSFSDEGMPSPPAKWNGICEFTGKRTCNNKIIGARNFVKTKNLTLPFDDVGHGTHTASTAAGRPVQGANVYGNANGTAVGMAPDAHIAMYKVCGLVGCSESAILAGMDTAVDDGVDVLSLSLGGPSGPFFEDPIALGAFGAIQKGIFVSCSAANSGPAYSS... | Function: Required for arbuscular mycorrhiza (AM) development during AM symbiosis with AM fungi (e.g. Glomeromycota intraradices).
Sequence Mass (Da): 79452
Sequence Length: 750
Subcellular Location: Secreted
EC: 3.4.21.-
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O82777 | MELLHLLLFSWALSAHLFLALAQRSTYIVHLDKSLMPNVFTDHHHWHSSTIDSIKASVPSSVDRFHSAPKLVYSYDNVLHGFSAVLSKDELAALKKLPGFISAYKDRTVEPHTTHTSDFLKLNPSSGLWPASGLGQDVIVAVLDSGIWPESASFQDDGMPEIPKRWKGICKPGTQFNASMCNRKLIGANYFNKGILANDPTVNITMNSARDTDGHGTHCASITAGNFAKGVSHFGYAPGTARGVAPRARLAVYKFSFNEGTFTSDLIAAMDQAVADGVDMISISYGYRFIPLYEDAISIASFGAMMKGVLVSASAGNRGP... | Function: Serine protease . Has preference for Gln in the P1 position and Lys in the P2 position of oligopeptide substrates. Active also with His in the P1 position . Involved in resistance against insects partly by regulating expression of systemic wound response genes and possibly by its post-ingestive activity in th... |
F4IG09 | MAIAFHTFLLQLLLFFFASFAEANDSRKTYLVQMKVGGHRYGSSSGHQELLGEVLDDDSTLADAFIYSYKESFTGFSASLTPRERQKLMRRREVLEVSRSRNLKLQTTRSWDFMNLTLKAERNPENESDLVVAVIDSGIWPYSELFGSDSPPPPGWENKCENITCNNKIVGARSYYPKKEKYKWVEEKSVIDVTGHGTHVASIVAGRKVEKAGYFGLAEGTMRGGVPNAKIAVYKTCWRVIRKNGREDSVCREDNILKAIDDAIADKVDIISYSQGFQFTPLQKDKVSWAFLRALKNGILTSAAAGNYANNGKFYYTVAN... | PTM: The C-terminal propeptide is autocleaved.
Sequence Mass (Da): 87920
Sequence Length: 775
Subcellular Location: Secreted
EC: 3.4.21.-
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O23357 | MASLGLFLCLSSVLLMSLCQVPTAIEDERKASHVYIAYMGALPSKISYSPMSHHQNILQEVIESSSVEDYLVRSYGRSFNGFAAKLTESEKDKLIGMEGVVSVFPSTVYKLFTTRSYEFMGLGDKSNNVPEVESNVIVGVIDGGIWPESKSFSDEGIGPIPKKWKGTCAGGTNFTCNRKVIGARHYVHDSARDSDAHGSHTASTAAGNKVKGVSVNGVAEGTARGGVPLGRIAVYKVCEPLGCNGERILAAFDDAIADGVDVLTISLGGGVTKVDIDPIAIGSFHAMTKGIVTTVAVGNAGTALAKADNLAPWLISVAAG... | PTM: The C-terminal propeptide is autocleaved.
Sequence Mass (Da): 76561
Sequence Length: 725
Subcellular Location: Secreted
EC: 3.4.21.-
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Q9FIF8 | MAKLSTPLYLICLAFIFTRDVSANDYRQASSVYIVYMGTLPEIKYSPPSHHLSILQKLVGTIAASHLLVRSYKRSFNGFAANLSQAESQKLQNMKEVVSVFPSKSHELTTTRSWDFVGFGEKARRESVKESDVIVGVIDSGIWPESESFDDEGFGPPPKKWKGSCKGGLKFACNNKLIGARFYNKFADSARDEEGHGTHTASTAAGNAVQAASFYGLAQGTARGGVPSARIAAYKVCFNRCNDVDILAAFDDAIADGVDVISISISADYVSNLLNASVAIGSFHAMMRGIITAGSAGNNGPDQGSVANVSPWMITVAASG... | PTM: The C-terminal propeptide is autocleaved.
Sequence Mass (Da): 78489
Sequence Length: 729
Subcellular Location: Secreted
EC: 3.4.21.-
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Q870W0 | MSSLRFLDLVKPFVPFLPEVQQPETKIPFNQKLMWTGLTLLIFLVMSQMPLYGIVSSDTSDPLYWLRMMMASNRGTLMELGITPIISSGMVFQLLAGTHMIDVNLDLKADRELYQTAQKLFAVILSIGTATVYVFTGLYGPPSDLGAGIVFLLILQLVVAGMIVILLDELLQKGYGLGSGISLFIATNICESIMWKAFSPTSINTGRGPEYEGAVIALFHLLMTWDNKQRALYEAFYRQNLPNIMNLLATLVVFAAVIYLQGFRVEIPVKSSRQRGARGSYPIRLFYTSNMPIMLQSALSSNVFLISQMLYSRFSENLLV... | Function: Appears to play a crucial role in the insertion of secretory and membrane polypeptides into the ER. It is required for assembly of membrane and secretory proteins and is essential for cell growth. It interacts with other membrane proteins required for protein translocation. Upon binding to SEC62/63 complex, s... |
P32915 | MSSNRVLDLFKPFESFLPEVIAPERKVPYNQKLIWTGVSLLIFLILGQIPLYGIVSSETSDPLYWLRAMLASNRGTLLELGVSPIITSSMIFQFLQGTQLLQIRPESKQDRELFQIAQKVCAIILILGQALVVVMTGNYGAPSDLGLPICLLLIFQLMFASLIVMLLDELLSKGYGLGSGISLFTATNIAEQIFWRAFAPTTVNSGRGKEFEGAVIAFFHLLAVRKDKKRALVEAFYRTNLPNMFQVLMTVAIFLFVLYLQGFRYELPIRSTKVRGQIGIYPIKLFYTSNTPIMLQSALTSNIFLISQILFQKYPTNPLI... | Function: Part of the Sec61 complex, which is the major component of a channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). The functional states of the translocon complex include co- and post-translational ER import, cotranslational membrane protein integration ... |
P38389 | MVGSGAPQRGSAAATASMRRRKPTSGAGGGGASGGAAGSMLQFYTDDAPGLKISPNVVLIMSIGFIAFVAVLHVMGKLYFVK | Function: Necessary for protein translocation in the endoplasmic reticulum.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8217
Sequence Length: 82
Subcellular Location: Endoplasmic reticulum membrane
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A8I6P9 | MAGSQSQASTLVARGGRSSSNAPTGAAGALRRRPVRGSGGSGTTKAQQAAMNFYTDDTPGWKMSPVVVITMSLSFIAFVTILHVVGKFQ | Function: Necessary for protein translocation in the endoplasmic reticulum.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9188
Sequence Length: 89
Subcellular Location: Endoplasmic reticulum membrane
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Q54YR4 | MKRPSTQRAPATVNKGGNSMMKFYSEDAIGLKVGPTAVLFMSLIFIAFVIILHIMGKYTRS | Function: Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypepti... |
P60468 | MPGPTPSGTNVGSSGRSPSKAVAARAAGSTVRQRKNASCGTRSAGRTTSAGTGGMWRFYTEDSPGLKVGPVPVLVMSLLFIASVFMLHIWGKYTRS | Function: Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER) . Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypept... |
Q9CQS8 | MPGPTPSGTNVGSSGRSPSKAVAARAAGSTVRQRKNASCGTRSAGRTTSAGTGGMWRFYTEDSPGLKVGPVPVLVMSLLFIAAVFMLHIWGKYTRS | Function: Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER) (By similarity). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of n... |
O43002 | MSSTKASGSVKNSAASAPGGPKSQIRRRAAVEKNTKESNSGPAGARAAGAPGSTPTLLKLYTDEASGFKVDPVVVMVLSVGFIASVFLLHIVARILKKFASE | Function: Necessary for protein translocation in the endoplasmic reticulum.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 10444
Sequence Length: 102
Subcellular Location: Endoplasmic reticulum membrane
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P24433 | MSKVWVGGFLCVYGEEPSEECLALPRDTVQKELGSGNIPLPLNINHNEKATIGMVRGLFDLEHGLFCVAQIQSQTFMDIIRNIAGKSKLITAGSVIEPLPPDPEIECLSSSFPGLSLSSKVLQDENLDGKPFFHHVSVCGVGRRPGTIAIFGREISWILDRFSCISESEKRQVLEGVNVYSQGFDENLFSADLYDLLADSLDTSYIRKRFPKLQLDKQLCGLSKCTYIKASEPPVEIIVAATKVAGDQVQLTTEPGSELAVETCDVPVVHGNYDAVESATATTAMSNQNLPNTTPLLSSPPFSDCVFLPKDAFFSLLNVT... | Function: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interact... |
Q2HRB6 | MAQGLYVGGFVDVVSCPKLEQELYLDPDQVTDYLPVTEPLPITIEHLPETEVGWTLGLFQVSHGIFCTGAITSPAFLELASRLADTSHVARAPVKNLPKEPLLEILHTWLPGLSLSSIHPRELSQTPSGPVFQHVSLCALGRRRGTVAVYGHDAEWVVSRFSSVSKSERAHILQHVSSCRLEDLSTPNFVSPLETLMAKAIDASFIRDRLDLLKTDRGVASILSPAYLKASQFPVGIQAVTPPRPAMNSSGQEDIISIPKSAFLSMLQSSIDGMKTTAAKMSHTLSGPGLMGCGGQMFPTDHHLPSYVSNPAPPYGYAYK... | Function: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interact... |
P23984 | MSENVDIKYIFVAGYLVVYDHQESAGREYELTREQSKSALPVLPGTIPINIDHESSCVVGTVLTILDLPRGLFCLGVVSTALAPIFLSYVQDDALFANAEEGMVLTETEKFLYLLSNILPSLSLSSRRLEKNEVPGKDFFAHVALCELGRREGTVAIYGATASEAIGAFDDLSAPIKEQLYEIATREKCAEVPRELSRPEITRVLMKKFIHGAFLMDRGTCLKTRREMAAVYNPKYLQANEVITIGIKEHSEETPENAIKDRSVSTQTAPSFDISESQQPSGQTHVPAMESATCSGQFLQTKNGASPSASREDMVYVPFE... | Function: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interact... |
P03711 | MTAELRNLPHIASMAFNEPLMLEPAYARVFFCALAGQLGISSLTDAVSGDSLTAQEALATLALSGDDDGPRQARSYQVMNGIAVLPVSGTLVSRTRALQPYSGMTGYNGIIARLQQAASDPMVDGILLDMDTPGGMVAGAFDCADIIARVRDIKPVWALANDMNCSAGQLLASAASRRLVTQTARTGSIGVMMAHSNYGAALEKQGVEITLIYSGSHKVDGNPYSHLPDDVRETLQSRMDATRQMFAQKVSAYTGLSVQVVLDTEAAVYSGQEAIDAGLADELVNSTDAITVMRDALDARKSRLSGGRMTKETQSTTVSA... | Function: Assembly protease promotes icosahedral procapsid assembly. Autocatalytic cleavage may release the capsid scaffolding protein. The protease domain catalyzes the cleavage of the capsid scaffolding protein after complete procapsid formation. Assembly protease and cleavages products are evicted from the capsid be... |
Q6UDK6 | MVVAEQLEDVFVGGYLVIYASQDGAGEEYRLPKEVVARALPVEPGRVPVNINHDASCRVGSVISIVDVEKGLFFLGVVSGSLALAMFKYVARDLFRADDGDSPGGGAESETRSDEALPANTLSEREKFLYLLSNVLPSLSLSSARLADGYSPADDFFAHVALCELGKRDGTIAIYGSSPPEVLDAFSGLDDAAKRELARSAEEWTTSSRREEPVDEAMVSECLLRKFMNNAFLMDRGEYLRARRHLADVRRPKYLQAAETTCLSSANPRSSGKAAFSCEARGLDEAGAGAIGRAPESGMAASADQHAQDGIKIRLERSRS... | Function: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interact... |
Q01002 | MSIVYVAGFVDVVAYPKVDPVLYLNLDDVSKCLPLTKPIPLNIEHLPESTIGHTIGLYAVTHGVFCVGVIHSEKFLHLTENLFSNSCVAQATSKFLPYQPLLEMLHTWLPALSLSSLCPTAQNAANTNMFQHVSLCALGRRRGTVAVYSMNLEDAISQFCSISQAEVENIYQDSKNVDINSLPKPVFNIDPHILMAKAIDAGFIKDRLQLLKTDKGVAKIKKLTYLKASEIGKPVTEDISEDMNQHGIVPQGSDDLISVPKSTFLSMLQNNLDNFKQHPRPACFPQYFSPQGAYMPYELYPPQPYSGDNIGYMLPSGSYV... | Function: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interact... |
P09286 | MAAEADEENCEALYVAGYLALYSKDEGELNITPEIVRSALPPTSKIPINIDHRKDCVVGEVIAIIEDIRGPFFLGIVRCPQLHAVLFEAAHSNFFGNRDSVLSPLERALYLVTNYLPSVSLSSKRLSPNEIPDGNFFTHVALCVVGRRVGTVVNYDCTPESSIEPFRVLSMESKARLLSLVKDYAGLNKVWKVSEDKLAKVLLSTAVNNMLLRDRWDVVAKRRREAGIMGHVYLQASTGYGLARITNVNGVESKLPNAGVINATFHPGGPIYDLALGVGESNEDCEKTVPHLKVTQLCRNDSDMASVAGNASNISPQPPS... | Function: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interact... |
Q8N9R8 | MVRGARQPQQPRSRLAPRLTGTVEKPPRKRRSRTEFALKEIMSSGGAEDDIPQGERKTVTDFCYLLDKSKQLFNGLRDLPQYGQKQWQSYFGRTFDVYTKLWKFQQQHRQVLDNRYGLKRWQIGEIASKIGQLYYHYYLRTSETSYLNEAFSFYSAIRQRSYYSQVNKEDRPELVVKKLRYYARFIVVCLLLNKMDVVKDLVKELSDEIEDYTHRFNTEDQVEWNLVLQEVAAFIEADPVMVLNDDNTIVITSNRLAETGAPLLEQGMIVGQLSLADALIIGNCNNQVKFSELTVDMFRMLQALEREPMNLASQMNKPGM... | Function: Tumor suppressor which functions to suppress MRTFA-induced SRF transcriptional activity. May function in the RHOA-DIAPH1 signal transduction pathway and regulate cell migration through transcriptional regulation of ITGB1.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 70399
Sequence Lengt... |
Q8C8N2 | MVRGARQSQQPRSRLAPRLSGTVEKPPRKRKSRTEFTLKETMSSGGAEDDIPQGERKTVTDFCYLLDKSKQLFNGLRDLPQYGQKQWQSYFGRTFDVYTKLWKFQQQHRQVLDNRYGLKRWQIGEIASKIGQLYYHYYLRTSETSYLNEAFSFYSAIRQRSYYSQVNKEDRPELVVKKLRYYARFIVVCLLLNKMDVVKDLVKELSDEIEDYTHRFNTEDQVEWNLVLQEVAAFIEADPVMVLNDDNTIVITSNRLAETGAPLLEQGMIVGQLSLADALIIGNCNNQVKFSELTVDMFRMLQALEREPMNLASQMNKPGI... | Function: Tumor suppressor which functions to suppress MRTFA-induced SRF transcriptional activity. May function in the RHOA-DIAPH1 signal transduction pathway and regulate cell migration through transcriptional regulation of ITGB1.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 70275
Sequence Lengt... |
Q9SKT3 | MSRYQSHSFDDGEINPFANPTSVPAATSKLSPLPPEPYDRGATMDIPLDSGKDLKAKEKELREKEAELKRREQEIKRKEDAIAQAGIVIEEKNWPPFFPLIHHDISNEIPIHLQRIQYVAFTSMLGLVVCLLWNIVAVTTAWIKGEGPTIWFLAIIYFISGVPGAYVMWYRPLYRAMRTDSALKFGWFFFTYLFHIAFCVFAAVAPPIIFKGKSLTGILPAIDVLSGNILVGIFYFIGFGFFCLESLVSIWVIQQVYMYFRGSGKAAEMKQEATRRAMMAAL | Function: Probably involved in membrane trafficking.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31963
Sequence Length: 282
Subcellular Location: Cell membrane
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Q64420 | MPGHLLQEEMTSSYTTTTTTITEPPSESLQKTVPLYLEEDIRPEMKEDIYDPSYQDEEGPPPKLEYVWRNIILMALLHLGALYGLVLVPSSKVYTLLWAFVYYVISIEGIGAGVHRLWSHRTYKARLPLRIFLIIANTMAFQNDVYEWARDHRAHHKFSETYADPHDSRRGFFFSHVGWLLVRKHPAVKEKGGKLDMSDLKAEKLVMFQRRYYKPAILLMCFILPTFVPWYFWGEAFVNSLCVSTFLRYTLVLNATWLVNSAAHLYGYRPYDKNIDPRENALVSLGCLGEGFHNYHHAFPYDYSASEYRWHINFTTFFID... | Cofactor: Expected to bind 2 Fe(2+) ions per subunit.
Function: Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substr... |
O02858 | MPAHLLQEEISSSYTTTTTITAPSSRVLQNGGGKLEKTPQYVEEDIRPEMKDDIYDPTYQDKEGPRPKLEYVWRNIILMSLLHLGALYGIILIPTCKIYTLLWAFAYYLLSAVGVTAGAHRLWSHRTYKARLPLRVFLIIANTMAFQNDVYEWARDHRAHHKFSETDADPHNSRRGFFFSHVGWLLVRKHPAVKEKGGLLNMSDLKAEKLVMFQRRYYKPGILLMCFILPTIVPWYCWGEAFPQSLFVATFLRYAIVLNATWLVNSAAHLYGYRPYDKTISPRENILVSLGAVGEGFHNYHHTFPYDYSASEYRWHINLT... | Cofactor: Expected to bind 2 Fe(2+) ions per subunit.
Function: Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substr... |
Q42551 | MASGIARGRLAEERKSWRKNHPHGFVAKPETGQDGTVNLMVWHCTIPGKAGTDWEGGFFPLTMHFSEDYPSKPPKCKFPQGFFHPNVYPSGTVCLSILNEDYGWRPAITVKQILVGIQDLLDTPNPADPAQTDGYHLFCQDPVEYKKRVKLQSKQYPALV | Function: SUMO-conjugating enzyme that accepts the SUMO proteins from the E1 SUMO-activating heterodimer SAE1/SAE2 and catalyzes its covalent attachment to other proteins with the E3 SUMO ligases SIZ1 and MMS21. Associates with SIZ1 for sumoylation of the transcription factor GTE3.
Sequence Mass (Da): 17986
Sequence Le... |
P03882 | MKNIKKNQVMNLGPNSKLLKEYKSQLIELNIEQFEAGIGLILGDAYIRSRDEGKTYCMQFEWKNKAYMDHVCLLYDQWVLSPPHKKERVNHLGNLVITWGAQTFKHQAFNKLANLFIVNNKKTIPNNLVENYLTPMSLAYWFMDDGGKWDYNKNSTNKSIVLNTQSFTFEEVEYLVKGLRNKFQLNCYVKINKNKPIIYIDSMSYLIFYNLIKPYLIPQMMYKLPNTISSETFLK | Function: Mitochondrial DNA endonuclease involved in intron homing. It introduces a specific double-strand break in the DNA of the 21S rRNA gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Specifically recognizes and cleaves the sequence 5'... |
P03878 | MVQRWLYSTNAKDIAVLYFMLAIFSGMAGTAMSLIIRLELAAPGSQYLHGNSQLFNVLVVGHAVLMIFFLVMPALIGGFGNYLLPLMIGATDTAFPRINNIAFWVLPMGLVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAINFIVTTLNMRTNGMTMHKLPLFVWSIFITAFLLLLSLPVLSAGITMLLLDRNFNTSFFEVSGGGDPILYEHLFWFFGQTVATIIMLMMYNDMHFSKCWKLLKKWITNIMSTLFKALFVKMFMSYNNQQDKMMNNTMLKKDNIKRSSETTRKMLNNSM... | Function: Mitochondrial DNA endonuclease involved in intron homing. It introduces a specific double-strand break at the junction of the two exons a4-a5 of the COX1 gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Recognizes with limited spe... |
Q3ZFI4 | MASSLKKLITSFLLFFFYTIIVASSEPSCRRYKSIISFGDSIADTGNYLHLSDVNHPPQAAFLPYGETFFSVPTGRDSDGRLIIDFIAEFLGLPYVPPYFGSQNVSFEQGVNFAVYGATALDRAFFIEKGIVSDFTNVSLSVQLNTFKQILPTLCASSSRDCREMLGDSLILMGESGGNDYNYPFFEDKSINEIKELTPLIIKAISDAIVDLIDLGGKTFLVPGSFPVGCSAAYLTLFQTAKEKDYDPLTGCLPWLNDFGKHHDEQLKTEIRRLRKLYPHVNIMYADYYNSLYRLYQKPTKYGFKNRPLAACCGVGGQYN... | Function: Sinapine esterase that catalyzes that hydrolysis of sinapine, releasing choline and sinapate. Sinapine (O-sinapoylcholine) is the predominant phenolic compound in a complex group of sinapate esters in seeds of oilseed rape (B.napus). Sinapine has antinutritive activity and prevents the use of seed protein for... |
P03877 | MVQRWLYSTNAKDIAVLYFMLAIFSGMAGTAMSLIIRLELAAPGSQYLHGNSQLFNVLVVGHAVLMIFFLVMPALIGGFGNQKRYESNNNNNQVMENKEYNLKLNYDKLGPYLAGLIEGDGTITVQNSSSMKKSKYRPLIVVVFKLEDLELANYLCNLTKCGKVYKKINRNYVLWTIHDLKGVYTLLNIINGYMRTPKYEAFVRGAEFMNNYINSTTITHNKLKNMDNIKIKPLDTSDIGSNAWLAGMTDADGNFSINLMNGKNRSSRAMPYYCLELRQNYQKNSNNNNINFSYFYIMSAIATYFNVNLYSRERNLNLLV... | Function: Mitochondrial DNA endonuclease involved in intron homing. It introduces a specific double-strand break in the DNA of the COX1 gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Recognizes with high specificity and cleaves the sequen... |
Q9ZZX1 | MVQRWLYSTNAKDIAVLYFMLAIFSGMAGTAMSLIIRLELAAPGSQYLHGNSQLFNVLVVGHAVLMIFFLVMPALIGGFGNYLLPLMIGATDTAFPRINNIAFWVLPMGLVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAINFIVTTLNMRTNGMTMHKLPLFVWSIFITAFLLLLSLPVLSAGITMLLLDRNFNTSFFEVSGGGDPILYEHLFWFFGHPEVYILIIPGFGIISHVVSTYSKKPVFGEISMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKI... | Function: Mitochondrial DNA endonuclease involved in intron homing. It introduces a specific double-strand break in the DNA of the COX1 gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Recognizes with limited specificity and cleaves the seq... |
Q5HEA4 | MKKTLLASSLAVGLGIVAGNAGHEAHASEADLNKASLAQMAQSNDQTLNQKPIEAGAYNYTFDYEGFTYHFESDGTHFAWNYHATGTNGADMSAQAPTTNNVAPSAVQANQVQSQEVEAPQNAQTQQPQASTSNNSQVTATPTESKSSEGSSVNVNAHLKQIAQRESGGNIHAVNPTSGAAGKYQFLQSTWDSVAPAKYKGVSPANAPESVQDAAAVKLYNTGGAGHWVTA | Function: Is able to cleave peptidoglycan and affects clumping and separation of bacterial cells.
Sequence Mass (Da): 24096
Sequence Length: 231
Subcellular Location: Secreted
EC: 3.2.-.-
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P51172 | MRAVLSQKTTPLPRYLWPGHLSGPRRLTWSWCSDHRTPTCRELGSPHPTPCTGPARGWPRRGGGPCGFTSAGHVLCGYPLCLLSGPIQGCGTGLGDSSMAFLSRTSPVAAASFQSRQEARGSILLQSCQLPPQWLSTEAWTGEWKQPHGGALTSRSPGPVAPQRPCHLKGWQHRPTQHNAACKQGQAAAQTPPRPGPPSAPPPPPKEGHQEGLVELPASFRELLTFFCTNATIHGAIRLVCSRGNRLKTTSWGLLSLGALVALCWQLGLLFERHWHRPVLMAVSVHSERKLLPLVTLCDGNPRRPSPVLRHLELLDEFAR... | Function: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also ... |
P51170 | MAPGEKIKAKIKKNLPVTGPQAPTIKELMRWYCLNTNTHGCRRIVVSRGRLRRLLWIGFTLTAVALILWQCALLVFSFYTVSVSIKVHFRKLDFPAVTICNINPYKYSTVRHLLADLEQETREALKSLYGFPESRKRREAESWNSVSEGKQPRFSHRIPLLIFDQDEKGKARDFFTGRKRKVGGSIIHKASNVMHIESKQVVGFQLCSNDTSDCATYTFSSGINAIQEWYKLHYMNIMAQVPLEKKINMSYSAEELLVTCFFDGVSCDARNFTLFHHPMHGNCYTFNNRENETILSTSMGGSEYGLQVILYINEEEYNPF... | Function: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in... |
Q9WU39 | MAPGEKIKAKIKKNLPVRGPQAPTIKDLMHWYCLNTNTHGCRRIVVSRGRLRRLLWIAFTLTAVALIIWQCALLVFSFYTVSVSIKVHFQKLDFPAVTICNINPYKYSAVSDLLTDLDSETKQALLSLYGVKDVLDSTPRKRREAGSMRSTWEGTPPRFLNLIPLLVFNENEKGKARDFFTGRKRKISGKIIHKASNVMHVHESKKLVGFQLCSNDTSDCATYTFSSGINAIQEWYKLHYMNIMAQVPLEKKINMSYSAEELLVTCFFDGMSCDARNFTLFHHPMYGNCYTFNNRENATILSTSMGGSEYGLQVILYINE... | Function: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in... |
H1AFJ7 | MGHGRRISESIKKQLPVTGPEAPTVKNLMDWYLNNTNTHGCRRIAVSRGYLRRWIWICFTVSSVGMIFWQWTLLLMSYYTVSVSVTVQFQTLPFPAVTICNINPYRKNATSALLEELDKQTKLILKELYTSCTGCSNRKLRSVLLNEAPEEDSGVAKLLQDMPLMKFEVIKEDHVIVSELSSNRQYRINNTFITRMYNNMDLATVGEQVGFKICDANKSNCIIYTFNSGVTAILEWYRLNYLNIMAQIPNEKKLEMGYSADDLIVTCMYDGQSCDSRNFTLFQHPLHGNCYTFNSGDDGNILQTLTGGSEYGLKLTLYLE... | Function: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in... |
K7FSQ4 | MAPPYHGDTREFSMAPAKKIKAKIKKTLPVTGPQAPTVSELMHWYCMNTNTHGCRRIVVSRGRLRKFIWILLTLSAVGLILWQCAELIMSYYTASVSVTVQFQKLPFPAVTICNINPYKYSAMKEHLSELDKETKNALETLYGFSEGKSKVRRDAADWNSTGRNMQSKLLEKIPLLKFDDLFKKTATEILSGHKRKIEGSAFHQGSSMVNIGEPQDVVGFQLCDPNNSSDCAVYIFSSGVNAIQEWYKLHYMNIMAQIPLEMKVNMGYSAEDLLLTCFFDGISCDSRNFTPFHHPLYGNCYTFNSGENGTILTTSTGGSE... | Function: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in... |
Q8VYP0 | MASALCRTASRLRSVQLFRRIRVSSDLLSASSPSPACISDALRHGDFSLPRSFFSLNCGIEMLKMDQRCLLSTSASDTTSKHDSGKPETKSSEKNEKSGGSESSDGGSDHKNERASGKDVRGGPVSWMSFFLLFATGAGLVYYYDTQKKRHIEDINKNSIAVKEGPSAGKAAIGGPFSLIRDDGKRVTEKNLMGKWTILYFGFTHCPDICPDELIKLAAAIDKIKENSGVDVVPVFISVDPERDTVQQVHEYVKEFHPKLIGLTGSPEEIKSVARSYRVYYMKTEEEDSDYLVDHSIVMYLMSPEMNFVKFYGKNHDVDS... | Function: Thought to play a role in cellular copper homeostasis, mitochondrial redox signaling or insertion of copper into the active site of COX. Plays an essential role in embryo development.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 37195
Sequence Length: 334
Subcellular Location: Mitochond... |
Q8LAL0 | MLPCRRLVLSCKNQAASFLRRCGPSKRIQSVNYCKSTRQGHEIPDVKPLFPTGGGTQAPSRSRARYAVPAILLGFAGFVGFLHYNDERRAVPRGQASSNSGCGCGSNTTVKGPIIGGPFTLVSTENKIVTENDFCGKWVLLYFGYSFSPDVGPEQLKMMSKAVDKLESKHNEKILPVFVTLDPQRDTPSHLHAYLKEFDSRILGLTGTASAMRQMAQEYRVYFKKVQEDGEDYLVDTSHNMYLINPKMEIVRCFGVEYNPDELSQELLKEVASVSQ | Function: Thought to play a role in cellular copper homeostasis, mitochondrial redox signaling or insertion of copper into the active site of COX (By similarity). Participates in copper and redox homeostasis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 30771
Sequence Length: 276
Subcellular Loca... |
P54178 | MKVIKGLTAGLIFLFLCACGGQQIKDPLNYEVEPFTFQNQDGKNVSLESLKGEVWLADFIFTNCETICPPMTAHMTDLQKKLKAENIDVRIISFSVDPENDKPKQLKKFAANYPLSFDNWDFLTGYSQSEIEEFALKSFKAIVKKPEGEDQVIHQSSFYLVGPDGKVLKDYNGVENTPYDDIISDVKSASTLK | Function: Necessary for insertion of copper into the active site of cytochrome c oxidase. May play a role in copper homeostasis or redox signaling.
Location Topology: Lipid-anchor
Sequence Mass (Da): 21718
Sequence Length: 193
Subcellular Location: Cell membrane
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Q9FH05 | MASVSWRAVAVAMVVVLLSLQWFAKGYPEEDLVVRLPGQPTVGFKQYAGYVDVDVKAGRSLFYYYVEAVKQPDSKPLTLWLNGGPGCSSIGGGAFTELGPFYPTGDGRGLRVNSMSWNKASHLLFVESPAGVGWSYSNKSSDYNTGDKSTANDMLVFLLRWFEKFPKLKSRDLFLTGESYAGHYIPQLADAILSYNSHSSGFKFNIKGVAIGNPLLKLDRDSPATYEFFWSHGMISDELKLTITSQCDFDDYTFASPHNVSTACNEAISETENIITEYVNNYDVLLDVCYPSIVQQELRLKKMATKMSMGVDVCMTYERR... | Function: Probable carboxypeptidase.
Sequence Mass (Da): 52874
Sequence Length: 473
Subcellular Location: Secreted
EC: 3.4.16.-
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Q84W27 | MVSSRAVVMAIMVLVTVQWLVFAEGYPEEDLVARLPGQPNVGFRQFAGYVDVDSENGRSLFYYYVEAVKEPDTKPLTLWLNGGPGCSSVGGGAFTELGPFYPTGDGRGLRLNSMSWNKASNLLFVESPAGVGWSYSNRSSDYNTGDKSTVNDMLVFLLRWFNKFPELKSRDLFLTGESYAGHYIPQLADVILSYNSRSSGFKFNVKGIAIGNPLLKLDRDFAAAYEYFWSHGMISDEVRLTIMNQCDFANPKNMSNACIYAIVESSVLTEYINSYHILLDVCYPSIVQQELRLKKMNALHANRTRLPYEWTMCSNRLNYS... | Function: Probable carboxypeptidase.
Sequence Mass (Da): 49774
Sequence Length: 442
Subcellular Location: Secreted
EC: 3.4.16.-
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Q8VY01 | MPRLQCLTMATSLILLLQALSLVSSTILSRADRITRLPGQPRVGFQQYSGYVTIDEKKQRALFYYLAEAETKPISKPLVLWLNGGPGCSSLGVGAFSENGPFRPKGSILVRNQHSWNQEANMLYLETPVGVGFSYANESSSYEGVNDKITAKDNLVFLQKWFLKFPQYLNRSLFITGESYAGHYVPQLAQLMIQYNKKHNLFNLKGIAIGNPVMEFATDFNSRAEYFWSHGLISDPTYKLFTSSCNYSRFLSEYHRGSVSSMCTKVLSQVGIETSRFIDKYDVTLDVCIPSVLSQSKVVSPQPQQVGETVDVCLEDETVN... | Function: Probable carboxypeptidase.
Sequence Mass (Da): 51883
Sequence Length: 465
Subcellular Location: Secreted
EC: 3.4.16.-
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Q9M9Q6 | MEQATTLFILLSTLLLAVSVESPQPPLFPDEALPTKSGYLPVKPAPGSSMFYAFYEAQEPTTPLPDTPLLVWLQGGPGCSSMIGNFYELGPWRVVSRATDLERNPGAWNRLFGLLFVDNPIGVGFSIAASQQDIPTNQRQVAEHLYAALVEFLEQNPSFENRPVYFTGESYAGKYVPAIGYYILKEKPNGKVNLKGLAIGNGLTDPVTQVQTHAVNVYYSGLVNAKQRVELQKAQEISVALVKSQKWREAADARTELLTLLSNMTGLATLYNTARAIPYRTDLVVDLLNQREAKRVLGVSETVRFEECSDEVEDVLRADV... | Function: Probable carboxypeptidase.
Sequence Mass (Da): 49222
Sequence Length: 444
Subcellular Location: Secreted
EC: 3.4.16.-
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Q67Y83 | MKTTVVYLVILCLIVSCTNGETKHVRKINSDGSEAWGYVEVRPKAHMFWWHYKSPYRVENPSKPWPIILWLQGGPGASGVGIGNFQEVGPLDTFLKPRNSTWLKKADLLFVDSPVGAGYSFVEGNQKDLYVKSDEEAAQDLTKLLQQLFNKNQTLNQSPLFIVAESYGGKIAVKLGLSVIDAVQSGKLKLHLGGVILGDSWISPEDFVFSWGPLLKHVSRLDDNGLDSSNSLAEKIKTQIKNGEYVGATQTWMDLENLISSKSNFVDFYNFLLDTGMDPVSLTTSLKIKKEEKIKKYSRYLNDMRSLSDVEDVEGDLDKL... | Function: Probable carboxypeptidase.
Sequence Mass (Da): 51752
Sequence Length: 461
Subcellular Location: Secreted
EC: 3.4.16.-
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Q9CAU2 | MANYISSVLKSLLLLLHLVFLIQQHVDSASIVKFLPGFEGSLPFELETGYIGIGEEEEVQLFYYFIKSERNPKEDPLLLWLSGGPGCSSISGLLFENGPLAMKLDVYNGTLPSLVPTTYSWTKTSSMIFLDQPVGTGFSYSRTQQYNKPSDSGEAKRIHEFLQKWLSKHQEFSSNPFYVAGDSYSGMVVPATVQEISKGNYQCCSPPINLQGYVLGNPITEHAIDYNYRIPFAHGMALISDELYESLKRVCKGEYVDPRDTECLKLVEEFSKCTKGVCQEVVIKPLCVTETPNCYIYRYLLTTYWVNDVNVRKALQINKE... | Function: Probable carboxypeptidase.
Sequence Mass (Da): 49938
Sequence Length: 438
Subcellular Location: Secreted
EC: 3.4.16.-
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Q9SQX6 | MANDYVSTVLLLLSLLIFLSQRTDSASIVKSLPGFDGPLPFELETGYIGVGEEEEVQLFYYFIKSERNPQEDPLLLWLSGGPGCSSISGLLYENGPVNVKIEVYNGTLPSLVSTTYSWTKVSSIIYLDQPVGTGFSYSRTKLVNKPSDSGEAKRIHEFLHKWLGKHQEFSSNPFYVGGDSYCGMVIPALVQEISKGNYVCCKPPINLQGYILGNPSTENEVDINYRIPYAHGMALISDELYESMKRICKGKYENVDPRNTKCLKLVGEYQKCTKRINKALIITPECVDTSPDCYMYRYLLTTYWANDENVQRALHVNKGS... | Function: Probable carboxypeptidase.
Sequence Mass (Da): 49565
Sequence Length: 437
Subcellular Location: Secreted
EC: 3.4.16.-
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Q8RUW5 | MSLKIKFLLLLVLYHHVDSASIVKFLPGFEGPLPFELETGYIGIGEDENVQFFYYFIKSENNPKEDPLLIWLNGGPGCSCLGGIIFENGPVGLKFEVFNGSAPSLFSTTYSWTKMANIIFLDQPVGSGFSYSKTPIDKTGDISEVKRTHEFLQKWLSRHPQYFSNPLYVVGDSYSGMIVPALVQEISQGNYICCEPPINLQGYMLGNPVTYMDFEQNFRIPYAYGMGLISDEIYEPMKRICNGNYYNVDPSNTQCLKLTEEYHKCTAKINIHHILTPDCDVTNVTSPDCYYYPYHLIECWANDESVREALHIEKGSKGKW... | Function: Involved in plants secondary metabolism. Functions as acyltransferase to form the sinapate ester sinapoylmalate. Also capable of catalyzing the formation of 1,2-bis-O-sinapoyl beta-D-glucoside.
PTM: N-glycosylated.
Catalytic Activity: (S)-malate + 1-O-(trans-sinapoyl)-beta-D-glucose = D-glucose + sinapoyl (S)... |
O64811 | MSLILKFMLLILLVSSHHVRSGSIVKFLPGFKGPLPFELETGYIGIGEEENVQFFYYFIKSDKNPQEDPLIIWLNGGPGCSCLSGLFFENGPLALKNKVYNGSVPSLVSTTYSWTKTANIIFLDQPVGSGFSYSKTPIERTSDTSEVKKIHEFLQKWLIKHPQFLSNPFYVVGDSYSGMIVPALVHEISKGNYICCNPPINLQGYVLGNPITHIEFEQNFRIPYAHGMSLISDELYESLKRICKGNYFSVDPSNKKCLKLVEEYHKCTDNINSHHTLIANCDDSNTQHISPDCYYYPYHLVECWANNESVREALHVDKGS... | Function: Catalyzes the formation of 1,2-bis-O-sinapoyl beta-D-glucoside and an unidentified compound 1.
Catalytic Activity: 2 1-O-(trans-sinapoyl)-beta-D-glucose = 1,2-di-O-sinapoyl beta-D-glucose + D-glucose
Sequence Mass (Da): 49756
Sequence Length: 437
Subcellular Location: Secreted
|
Q10484 | MALECDSTIVFPRPLTRLVKCDLELRNTAPYPIGFKVKTTAPKQYCVRPNGGRIEANSAVSVEVILQPLDHEPAPGTKCRDKFLVQSTELKPELQGMDIADIWTQVSKANISERKIRCVYSEGPSTANAHANAHHQPAQTTTTSIPTSATDNYTTVNGNVNQSYSKGIDGTALPSTHANPVAAPSTATTQHTQLPKTSAVSHQKPHEAPSTAVKAPTATVAENEPYPKPQSVPTTTSPNNENNALRSTANVINNTRQSTATSPSMFAGNSGNQIGLARVSSSFGRPTSGAKVVPQIHNTVTVQTAFLLAIICFLIGLLF | Function: Vesicle-associated membrane protein-associated protein (VAP) implicated in maintaining the cortical endoplasmic reticulum (ER)-plasma membrane (PM) attachment . ER-PM contacts function to modulate the distribution of contractile ring components to ensure robust ring assembly . ER-PM contacts function also in ... |
Q6Q595 | MRIVPEKLVFKAPLNKQSTEYIKLENDGEKRVIFKVRTSAPTKYCVRPNVAIIGAHESVNVQIVFLGLPKSTADDEMDQKRDKFLIVTLPIPAAYQNVEDGELLSDWPNLEEQYKDDIVFKKIKIFHSVLPKRKPSGNHDAESARAPSAGNGQSLSSRALLIITVIALLVGWIYY | Function: Targets proteins containing a FFAT motif to membranes (By similarity). Involved in regulation of phospholipid metabolism.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 19678
Sequence Length: 175
Domain: The MSP domain is required for binding to the FFAT motif of target proteins.
... |
O60119 | MSVECSGELFFYPPFTTMSKELISVHNPNPEPVIFKVKTTAPKHYCVRPNSGKIEPKSTVNVQVLLQAMKEEPAPDFKCRDKFLIQSMAIGDADTSNVENYHEFWTEMEKQGRSIFDRKIRCVYSTKQPPQSADKQVENTSTSNPPVSVEGSENLASSVGGPTAVGVSLDEAQNDFNGAKDHLSNGVNTVVPDSTFRSTFESAQIPDASVVQTVVTDADNGAASVKDTIVTAESASSKGADVARSKVQDIIDNEIPKPSESPRRSVSSTPPVHPPPPVPQNLSAVNEEFDTKKNDFDSKLPESTPAVEKVSENLGSETRE... | Function: Vesicle-associated membrane protein-associated protein (VAP) implicated in maintaining the cortical endoplasmic reticulum (ER)-plasma membrane (PM) attachment . ER-PM contacts function to modulate the distribution of contractile ring components to ensure robust ring assembly . ER-PM contacts function also in ... |
P40075 | MSAVEISPDVLVYKSPLTEQSTEYASISNNSDQTIAFKVKTTAPKFYCVRPNAAVVAPGETIQVQVIFLGLTEEPAADFKCRDKFLVITLPSPYDLNGKAVADVWSDLEAEFKQQAISKKIKVKYLISPDVHPAQNQNIQENKETVEPVVQDSEPKEVPAVVNEKEVPAEPETQPPVQVKKEEVPPVVQKTVPHENEKQTSNSTPAPQNQIKEAATVPAENESSSMGIFILVALLILVLGWFYR | Function: Targets proteins containing a FFAT motif to endoplasmic reticulum membranes. Regulates phospholipid biosynthesis by modulating the subcellular localization of the transcriptional repressor OPI1.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 26926
Sequence Length: 244
Domain: The ... |
Q9HGM4 | MTEKTASHYWNEETSILKLRRKDILLFEIYATTLLLGSIYSIYVDKWSITSYFGNSKNLINLIFVKRGWFWTSLVYFYHAWDQKRNKIDFKFISRYIVATLWWMFVTQWFIGPGLIDRTFALSGGSCKNFDGDSSVFIPLTASTCKGLNGSWSGGHDLSGHVFLLTHSSLFMLSENFSFILNNGIKATSTKVLFGLLGLWWWMLFVTASFYHTTFEKCTGFFSGILEWSIVYVFSSRMPAVADLLGSSDY | Function: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (By similarity). Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen (By similarity). This catalytic activity i... |
P53012 | MSSKWFNAIHLLVCPLTVLVGYLMNAYGYGAALQATLNKDGLVNAMLVKKGWFWTSLVGWWCIIRYRAVPGATGRDRRHIVQSFKRYAILTVWWYVFTQGIWFGVGPIMDLVFVYTGGHCHYDVFDDAGHVNEDFQGSVTRTNRALALIHNVLTLHGHHQEHRQQQLWDRSIGSIQGALQATQPKTPKNVTASAAAAINTFIHDQMHRWQGPLTTSAQCRRFGGHWAGGHDPSGHVFLATLMCMFLLGELRVFGRRALAHLYAQKWQLVRLVTRLFDTGPLWTWRRCGGGSMTCGARLWRAIVEPPVTCAAALLRLTRCI... | Function: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate. Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen (By similarity). This catalytic activity is required for m... |
O13846 | MASVTSEKCVILSDGTEYDVTNYLVANKDAADLLRRYHRQEVADILNATSKSKHSEAVVEILKSAKVPLKNKEFSDLVDQNIGVGYGNEFIVKPTDLDKDFEKNHFLDLKKPLLPQILFGNIKKDVYLDQVHRPRHYRGSGSAPLFGNFLEPLTKTPWYMIPLIWVPCVTYGFLYACTGIPFSVAITFFIIGLFTWTLVEYTMHRFLFHLDEYTPDHPIFLTMHFAFHGCHHFLPADKYRLVMPPALFLIFATPWYHFIQLVLPHYIGVAGFSGAILGYVFYDLTHYFLHHRRMPNAYLTDLKTWHLDHHYKDYKSAYGI... | Cofactor: Binds 2 Zn(2+) ions per subunit that likely form a catalytic dimetal center.
Function: Ceramide hydroxylase involved in the hydroxylation of sphingolipid-associated very long chain fatty acids. Postulated to hydroxylate the very long chain fatty acid of dihydroceramides and phytoceramides at C-2.
Location Top... |
Q03529 | MSTNTSKTLELFSKKTVQEHNTANDCWVTYQNRKIYDVTRFLSEHPGGDESILDYAGKDITEIMKDSDVHEHSDSAYEILEDEYLIGYLATDEEAARLLTNKNHKVEVQLSADGTEFDSTTFVKELPAEEKLSIATDYSNDYKKHKFLDLNRPLLMQILRSDFKKDFYVDQIHRPRHYGKGSAPLFGNFLEPLTKTAWWVVPVAWLPVVVYHMGVALKNMNQLFACFLFCVGVFVWTLIEYGLHRFLFHFDDWLPESNIAFATHFLLHGCHHYLPMDKYRLVMPPTLFVILCAPFYKLVFALLPLYWAYAGFAGGLFGYV... | Cofactor: Binds 2 Zn(2+) ions per subunit that likely form a catalytic dimetal center.
Function: Ceramide hydroxylase involved in the hydroxylation of sphingolipid-associated very long chain fatty acids . Postulated to hydroxylate the very long chain fatty acid of dihydroceramides and phytoceramides at C-2 .
Catalytic ... |
Q9JL59 | MLAYSVTSSGLFPRMLWALLLLAASLNAHNDVWDEPCCTEHEVSVNRGSRVVMACNISNNLRDVTIELVTSEKTSIIFNHTPPGNYSKDSWQLHIQGVQAQLVITDAQDKHSGNYSWKLHGFQAEFKNFNLTVNAADRQKTEDLPVTKVPDKPPTAVRTEVIIIIAIATTIIITGIGVFVWYKQFPVAPQIQMSVPCLIHGSPGIPYLTLPP | Function: May be involved in thymocyte signaling.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 23477
Sequence Length: 212
Subcellular Location: Cell membrane
|
Q56135 | MLISNVGINPAAYLNNHSVENSSQTASQSVSAKDILNSIGISSSKVSDLGLSPTLSAPAPGVLTQTPGTITSFLKASIQNTDMNQDLNALANNVTTKANEVVQTQLREQQAEVGKFFDISGMSSSAVALLAAANTLMLTLNQADSKLSGKLSLVSFDAAKTTASSMMREGMNALSGSISQSALQLGITGVGAKLEYKGLQNERGALKHNAAKIDKLTTESHSIKNVLNGQNSVKLGAEGVDSLKSLNMKKTGTDATKNLNDATLKSNAGTSATESLGIKNSNKQISPEHQAILSKRLESVESDIRLEQNTMDMTRIDARK... | Function: Component of the type III secretion system 1 (SPI-1 T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (By similarity). SipB/SctE1 and SipC/SctB1 are inserted into the host membrane where they form a pore and allow the translocation of effector prote... |
Q9R803 | MEASNVALVLPAPSLLTPSSTPSPSGEGMGTESMLLLFDDIWMKLMELAKKLRDIMRSYNVEKQRLAWELQVNVLQTQMKTIDEAFRASMITAGGAMLSGVLTIGLGAVGGETGLIAGQAVGHTAGGVMGLGAGVAQRQSDQDKAIADLQQNGAQSYNKSLTEIMEKATEIMQQIIGVGSSLVTVLAEILRALTR | Function: Component of the type III secretion system 2 (SPI-2 T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (Probable). SseC/SctE2 and SseD/SctB2 are inserted into the host membrane where they form a pore and allow the translocation of effector proteins i... |
Q05129 | MNTIDNNNAAIAVNSVLSSTTDSTSSTTTSTSSISSSLLTDGRVDISKLLLEVQKLLREMVTTLQDYLQKQLAQSYDIQKAVFESQNKAIDEKKAGATAALIGGAISSVLGILGSFAAINSATKGASDVAQQAASTSAKSIGTVSEASTKALAKASEGIADAADDAAGAMQQTIATAAKAASRTSGITDDVATSAQKASQVAEEAADAAQELAQKAGLLSRFTAAAGRISGSTPFIVVTSLAEGTKTLPTTISESVKSNHDINEQRAKSVENLQASNLDTYKQDVRRAQDDISSRLRDMTTTARDLTDLINRMGQAARLA... | Function: Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (By similarity). EspD and EspB are inserted into the host membrane where they form a pore and allow the translocation of effector proteins into the cytosol... |
P15221 | ADGYVKGKSGCKISCFLDNDLCNADCKYYGGKLNSWCIPDKSGYCWCPNKGWNSIKSETNTC | Function: Binds to sodium channels (Nav) and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active on insects.
Sequence Mass (Da): 6855
Sequence Length: 62
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulf... |
P56609 | KEGYAMDHEGCKFSCFPRPAGFCDGYCKTHLKASSGYCAWPACYCYGVPSNIKVWDYATNKC | Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is active on mammals (By similarity).
Sequence Mass (Da): 6931
S... |
P68410 | MKGFLLFISILMMIGTIVVGKEGYAMDHEGCKFSCFIRPAGFCDGYCKTHLKASSGYCAWPACYCYGVPDHIKVWDYATNKCGK | Function: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin acts on Nav1.2/SCN2A, Nav1.3/SCN3A, Nav1.5/SCN5A, Nav1.6/SCN8A and Nav1.7/SCN9A voltage-gated sodium channels, with the highest ... |
E7CLP1 | KEGYPMGRDGCKISCVINNNFCKVECQAKWRQSDGYCYFWGLSCYCTIYQKTPRFGILAPINVEDNVTVTQCLGHLINVMYSH | Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing.
Sequence Mass (Da): 9524
Sequence Length: 83
Domain: Has the structural arr... |
A0A7S8MVA6 | MKTAFFILLIFSIFYGKAKGAEDREGFPVNRFGCTYPCYYGEDTEKCRRLCRETLGADYGYCFWYACYCENLPENVRRIKSQGFFGCSNGWWVVSTTTRKPK | Function: Putative sodium channel toxin.
Sequence Mass (Da): 11929
Sequence Length: 102
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
|
A0A7S8MU85 | QDEVGLGSCSVIFVVGNEEGEAKDGYAVGGDRCRVRCSPLGKNKDCETACRKKAGSYYGYCYLWFCYCENVSESAVVWGNPTLGPCLSDG | Function: Putative sodium channel toxin.
Sequence Mass (Da): 9693
Sequence Length: 90
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
|
A0A7S8RFI7 | MAGEWACLLVSLVLLWGAAGSRDGFLLDRNFCRIKCSFLGSNSMCADRCTVLGASAGHCNNYACFCTDLRDRVKIWGDSVRCRKP | Function: Putative sodium channel toxin.
Sequence Mass (Da): 9354
Sequence Length: 85
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
|
O81833 | MREIHSLFSLSLFLISSSLSVALDYNVITPKEFLKDGDTLSSPDQVFQLGFFSLDQEEQPQHRFLGLWYMEPFAVVWVANRNNPLYGTSGFLNLSSLGDLQLFDGEHKALWSSSSSSTKASKTANNPLLKISCSGNLISSDGEEAVLWQSFDYPMNTILAGMKLGKNFKTQMEWSLSSWKTLKDPSPGDFTLSLDTRGLPQLILRKNGDSSYSYRLGSWNGLSFTGAPAMGRENSLFDYKFTSSAQEVNYSWTPRHRIVSRLVLNNTGKLHRFIQSKQNQWILANTAPEDECDYYSICGAYAVCGINSKNTPSCSCLQGF... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 91875
Sequence Length: 815
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
O64782 | MGMVLFACLLLLIIFPTCGYAAINTSSPLSIRQTLSSPGGFYELGFFSPNNTQNQYVGIWFKKIVPRVVVWVANRDTPVTSSAANLTISSNGSLILLDGKQDVIWSTGKAFTSNKCHAELLDTGNFVVIDDVSGNKLWQSFEHLGNTMLPQSSLMYDTSNGKKRVLTTWKSNSDPSPGEFSLEITPQIPTQGLIRRGSVPYWRCGPWAKTRFSGISGIDASYVSPFSVVQDTAAGTGSFSYSTLRNYNLSYVTLTPEGKMKILWDDGNNWKLHLSLPENPCDLYGRCGPYGLCVRSDPPKCECLKGFVPKSDEEWGKGNW... | Function: S-domain receptor protein kinase involved in lipopolysaccharide (LPS) sensing . Specifically detects LPS of Pseudomonas and Xanthomonas species . LPS are major components of the outer membrane of Gram-negative bacteria and are important microbe-associated molecular patterns (MAMPs) that trigger biphasic produ... |
Q39086 | MRSVPNYHHSFFIFLILILFLAFSVSPNTLSATESLTISSNKTIISPSQIFELGFFNPASSSRWYLGIWYKIIPIRTYVWVANRDNPLSSSNGTLKISGNNLVIFDQSDRPVWSTNITGGDVRSPVAAELLDNGNFLLRDSNNRLLWQSFDFPTDTLLAEMKLGWDQKTGFNRILRSWKTTDDPSSGEFSTKLETSEFPEFYICSKESILYRSGPWNGMRFSSVPGTIQVDYMVYNFTASKEEVTYSYRINKTNLYSRLYLNSAGLLQRLTWFETTQSWKQLWYSPKDLCDNYKVCGNFGYCDSNSLPNCYCIKGFKPVN... | Function: Involved in the regulation of cellular expansion and differentiation. Mediates subcellular relocalization of PUB9 from nucleus to plasma membrane in a protein-phosphorylation-dependent manner. May be involved in the abscisic acid-mediated signaling pathway, at least during germination.
PTM: Autophosphorylated... |
Q39203 | MPCTTYLPLLLLLFLLPPPSVQSKVIIKGNQTILSFKAIFRLGFFSTTNGSSNWYLGISYASMPTPTHVWVANRIRPVSDPDSSTLELTSTGYLIVSNLRDGVVWQTDNKQPGTDFRFSETGNLILINDDGSPVWQSFDNPTDTWLPGMNVTGLTAMTSWRSLFDPSPGFYSLRLSPSFNEFQLVYKGTTPYWSTGNWTGEAFVGVPEMTIPYIYRFHFVNPYTPTASFWYIVPPLDSVSEPRLTRFMVGANGQLKQYTWDPQTQSWNMFWLQPEDPCRVYNLCGQLGFCSSELLKPCACIRGFRPRNDAAWRSDDYSDG... | Function: Serine/threonine-protein kinase.
PTM: Autophosphorylated.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 88493
Sequence Length: 797
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q8RWZ5 | MRGVFIVIVTCLVFLPDPLRAGVASIGSITPGFGGSQMNYINNDGIFLESNNSAFGFGFVTTQDSVTLFTLSIIHKSSTKLIWSANRASPVSNSDKFVFDDNGNVVMEGTEVWRLDNSGKNASRIELRDSGNLVVVSVDGTSIWESFDHPTDTLITNQAFKEGMKLTSSPSSSNMTYALEIKSGDMVLSVNSLTPQVYWSMANARERIINKDGGVVTSSSLLGNSWRFFDQKQVLLWQFVFSDNKDDNTTWIAVLGNNGVISFSNLGSGASAADSSTKIPSDLCGTPEPCGPYYVCSGSKVCGCVSGLSRARSDCKTGIT... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 89740
Sequence Length: 821
Subcellular Location: Membrane
EC: 2.7.11.1
|
P93756 | MKMLRALLLCLSLVFFLAFQIVVSEIQLGSKLVVGENTLWVSNNGDFALGFFNPPGLLNRFSIGIWFNSNSIPYDQRKVVWVAGAGVVVSDNSSYFELTRNGELVLFDSLLGVPVWNSKTNRFSVSSALLRDDGNLVLLKDREEIVWQSFGTPTDTLLPNQKFPAFEMLRAASENSRSSYYSLHLEDSGRLELRWESNITFWSSGNEVVKKKKKKKNIGAVLTSEGALFLEDQDLMRPVWSVFGEDHNDTVKFRFLRLDRDGNLRMYSWNEDSRIWKPVWQAVENQCRVFATCGSQVCSFNSSGYTECNCPFNAFVSVSD... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 85857
Sequence Length: 764
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q9UTJ7 | MLRFRKVAPSLKNGGNLKLFSTSSTLKKIASSQPLRAKQVSTSESVKYPVIDHTYDAIVVGAGGAGLRATFGLAEAGFNTACITKLFPTRSHTVAAQGGINAALGNMTKDDWRWHFYDTVKGSDWLGDQDAIHYMTKEAPKAVLELEHFGVPFSRTKEGKIYQRAFGGQSLEYGKGGQAYRCAAVADRTGHSILHTLYGQSLKHNTNFFIEYFAMDLIMEGGECRGVIAMNLEDGSIHRFRAHKTILATGGYGRAYFSCTSAHTCTGDGNAMVSRAGLPLQDLEFVQFHPTGIYGAGCLITEGCRGEGGYLLNSKGERFM... | Function: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Catalytic Activity: a quinone + succinate = a quinol + fumarate
Location Topology: Pe... |
G4V4G6 | MNLPVREFDAVVIGAGGAGMRAALQISQMGLSCALLSKVFPTRSHTVSAQGGITVALGNTHEDNWEWHMYDTVKGSDYIGDQDAIEYMCKTGPEAVLELEHMGLPFSRLDDGSIYQRPFGGQSRNFGGEQAARTAAAADRTGHALLHTLYQQNLKNHTTIFSEWYALDLVKNQDGAVMGCTAICIETGEVVYFKARATVLATGGAGRIYQSTTNAHINTGDGVGMALRAGVPVQDMEMWQFHPTGIAGAGVLVTEGCRGEGGYLLNKHGERFMERYAPNAKDLAGRDVVARSIMIEIREGRGCDGPWGPHAKLKLDHLGK... | Cofactor: Flavinylated by SdhE, flavinylation occurs at a very low level in the absence of SdhE.
Function: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase... |
Q00711 | MLSLKKSALSKLTLLRNTRTFTSSALVRQTQGSVNGSASRSADGKYHIIDHEYDCVVIGAGGAGLRAAFGLAEAGYKTACISKLFPTRSHTVAAQGGINAALGNMHKDNWKWHMYDTVKGSDWLGDQDSIHYMTREAPKSIIELEHYGVPFSRTENGKIYQRAFGGQTKEYGKGAQAYRTCAVADRTGHALLHTLYGQALRHDTHFFIEYFALDLLTHNGEVVGVIAYNQEDGTIHRFRAHKTIIATGGYGRAYFSCTSAHTCTGDGNAMVSRAGFPLQDLEFVQFHPSGIYGSGCLITEGARGEGGFLVNSEGERFMER... | Function: Catalytic subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH1 and SDH2 form the catalytic dimer. Electrons flow from succinate to the FAD bound to SDH... |
Q8LB02 | MAFGLIGRVVGTKSSRLSTAARLIPARWTSTGSEAQSKASTGGGGASLKTFQIYRWNPDNPGKPELQDYKIDLKDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIESGSKETTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKNPASVPGKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPESYLGPAALLHANRWISDSRDEYTKERLEAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIKQLQKSG | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Catalytic Activity: a quinone + succinate ... |
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