ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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O43761 | MEGASFGAGRAGAALDPVSFARRPQTLLRVASWVFSIAVFGPIVNEGYVNTDSGPELRCVFNGNAGACRFGVALGLGAFLACAAFLLLDVRFQQISSVRDRRRAVLLDLGFSGLWSFLWFVGFCFLTNQWQRTAPGPATTQAGDAARAAIAFSFFSILSWVALTVKALQRFRLGTDMSLFATEQLSTGASQAYPGYPVGSGVEGTETYQSPPFTETLDTSPKGYQVPAY | Function: May play a role in regulated exocytosis. May indirectly regulate the activity of the plasma membrane dopamine transporter SLC6A3 and thereby regulate dopamine transport back from the synaptic cleft into the presynaptic terminal.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24555
Sequence Length: 229
Subcellular Location: Cytoplasmic vesicle
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Q8R191 | MEGASFGAGRAGAAFDPVSFARRPQTLLRVVSWVFSIAVFGPIVNEGYVNSDSGPELRCVFNGNAGACRFGVVLGLGAFIACVAFLLLDVRFQQISSVRDRRRAVLLDLGFSGVWSFLWFVGFCFLTNQWQRTTPGPGTAQAGDAARAAIAFSFFSILSWVALTVKALQRFRLGTDMSLFATDQLGTGAAQAYPGYPVGSGVEGTETYQSPPFTETLDTSSKGYQVPAY | Function: May play a role in regulated exocytosis . May indirectly regulate the activity of the plasma membrane dopamine transporter SLC6A3 and thereby regulate dopamine transport back from the synaptic cleft into the presynaptic terminal .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24561
Sequence Length: 229
Subcellular Location: Cytoplasmic vesicle
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Q7JYV2 | MDMLNQILSINNGGAYGGGKAGGAFDPLTFAMKPQVVIRALCWLFSVVVFGCISSEGWTEKDGKEYCLYNGDGMACKYGNMVGVFGFLASMGFMGGEFLFERMSSVKSRKRYVMADMGFSALWTFMYFVAFLYLWSQWSSSAPPPLGIGAGSMKTAIWFCLFSIVSWALCALMAYKRFLIGAGDEFTSAFETDPANVVHQQAYGYSMDNDNDQYSASPFGQPQQGGMEQQQSGMEYQQPTY | Function: Required for the correct formation of synaptic vesicles at nerve terminals and has a role in the regulation of the synaptic vesicle exo-endocytic cycle.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26610
Sequence Length: 241
Subcellular Location: Cytoplasmic vesicle membrane
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Q08826 | MPREFKSFGSTEKSLLSKGHGEPSYSEIYAEPENFLEIEVHNPKTHIPNGMDSKGMFTDYEIICRTNLPSFHKRVSKVRRRYSDFEFFRKCLIKEISMLNHPKVMVPHLPGKILLSNRFSNEVIEERRQGLNTWMQSVAGHPLLQSGSKVLVRFIEAEKFVG | Function: Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18770
Sequence Length: 162
Subcellular Location: Cytoplasm
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Q759T1 | MNSFRESDEEDNNPFSGTNHLYASGIGAVPEGDDDFLSAEVDTADETVQETREQMMSRLFGECEGPRESSAGGWTSGSMGSIGAPDGHSDEVTEFGIDTVLVEGEVRTPGRARVPASYPDAEGSLGALRIVDAGQYKDTFGNYAIGYTIAYEGRQVTRRYSEFDSLRQALARLLPTVIIPPIPSKHPLIRYFLNPLNAENDIRIIEKRRRLLSRFLNNCHDITDIREHTVFQKFLNPEYIWSEVLLTPPVSILPTNNLLAPPLNPTKPSPLHLLLPTPPRRTTSYGSPKTNNPEYDIRFTELESLLLRYHKCLQPVLASSRQKKIHFKQLASSLADLGAYYNAFSLEDNVINLPHQMDQIRDLSRAIEKIGQAVDVNYVSSELLVENIMILLEEPIGEMLQFVQEGREVLRFRMQKQQQFHIIDTTIKKRRGRIEELRNFQAQLARLEAALKQNAEESPTIARAVQRLDAQHLHKQRKSPSGELQWTGLFKSRSGSVRTHDSLTTRPVTGDVDVDLLSDEERAREIARLEGDLEKLNECYKLIQRDMLQVNESMARSFDWFIMYLHDTWALVLRNYTRTLLNWLKDCLTAWKNARVTIDTIAV | Function: May be required for cytoplasm to vacuole transport (Cvt) and pexophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 68638
Sequence Length: 603
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctate structures.
Subcellular Location: Endosome membrane
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Q5AD73 | MSTDNLFEDIEQDNNPSFYGNPSILNDPYRPIQPPPPQQQQQQHQENESKQSHTKSPKPPLQSIHSGTSNAHPQSQPQHKHKHKHNTSLNNGYPNELVNSTIGLSNRILELLNDSQLQVDIINSEKLVNSSVIVYTIELSSPTTKIVVKRRYSEFKSLRDNLLKLFPTLIIPPIPEKHSILSYLLNTINHSHEISIIEMRKRYFKMFLDDLIFQSDYKLKNCPLLHKFFDPNYELCWYNALNEPPVSLIPDNLLLANPINPADQNGLYSLLPIVNGFDFNSHIDNLSNLKKINEDLYKLNDQVKLYELKGFEQDLEFSIPEELIQFEIKFHQTIKILTDLNKLNSKTTKNYKSMVDTLIDLGGNLNNFSLQVYQQKSGSNNELSEAIEKFGSTMDQSFLNFESFILNQLVPQWQEPVDQLILYLQNSLGLIKFYKYKIVQFKILYKLKFNKFQQLINLTNIGGVSSSGSGGGGLLASRISTDNDSNNSNNSGNNNNDGDLDTENFDHLKELNSPTINNALKNLSTKKISKKSSWYGLFGGNNQTKKFNFQLPIEEPTTATGSTEQQSQQQSAPNSPQREQQQQQSQSQSHHSHQTSIRFKLNHIEKELNKLNQLIELCNQDMHKLTEALVNTFEEFLSKIERKWLQLMITYIQNCKNMFEANLTNWKEFKESLVNETREVN | Function: May be required for cytoplasm to vacuole transport (Cvt) and pexophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 78368
Sequence Length: 681
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctate structures.
Subcellular Location: Endosome membrane
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P0CR64 | MDSDTSPNPFASSPPSSPSPRPSLPPPVPRKPSSLVSAASGSPPPTHRASFPDPARHPKMGATVPGPKPKTGYCCSIDKDISAGEQVHIVDALKTTEGGTASYITYVIRLGTHTVRRRYSAFLSLHQSLTGLYPVLIIPPIPSKQSLTDYAVKGQSKAREDATIIARRKRLLEDFLQRLIRHPILGGEHVLHRFLEEDVSWSEVLHSPPISLLSKNPLHAPSHNPTFQPTTPTSPSEAPATTSYIAHHLLPTPSPSHPLRQPDQRFMDSEAFTEKFQSHFSGTMEKVNRRVTKRWGERAHDMSELGGIWNGFSLVEQGKLGDAIEKVGRAVDAEYLATAALLQSWEKTTTEPLHIYSQFATLIRARLSFRHQKHVQYELVQEALETQRDKLEILENAEREARRLEEALERGGSVLASPQLEPEAARDERERAQRRARASQGFGLLSAVKHSLSGMIDMDPEATRRANIAKTRDNISQLEDSYQAAAQDLKYASMTLQADLDRFQRQKVADLREMAINLSQVHRDWCKQNLEAWKAAQAAVREIDPHPNRPAQTQTQVQSQQSHAGPSTLHAQTEDDVSKLGVDAMKNEIERVEIEIADKPLPKPSLAETGGDGVVPSPQPRQENDTEEQEGHGPLGPL | Function: May be required for cytoplasm to vacuole transport (Cvt) and pexophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 70714
Sequence Length: 638
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctate structures.
Subcellular Location: Endosome membrane
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Q6CWX3 | MNVFDGSDEEDNNPFSGTTHLYASGIAAVTDGPDDYDFTEPSINGSSDENAQSNAVAEPIEETDEPAEEIDDDTLQTWRFASAELSRSSAFETSYTNLLGQGKNPEVIRIVDAGQYRDIYGKYAIGYKIEFGGIVVTRRYSEFDSLRQSLCRLLPTIIIPPIPSKHPIIKYLFNPLHAKKDIKIIERRQRLLSRFLNNCHKVREIRNHIVFQKFLNPEYFWKEVLNTPPISILPMNNLLAPPLNPTKPSPIHLLLPTPTVLTMRKHEQLIGRNDVMEIKFADYDSDLIRYKAILQPLNKTVRSIRSNIQTYSAVLSELGAYFNAFSLENSVFQVSALFEQMNRLSMGIEKTGQAIDVNYVSAEIFSEAIMISLEEGSKEMLQFIHEAQRVLHFRNFKQEQFYTIETTIKKRKDRIRELKEADLQAVRLGEALKLNAEESPTVAQVMDSMTRKSANKNHTDKQIMGLFRSSASPNNKSGSDSISSEVEPHLLTKDERVVQVNKLEKELEKLNECFKLIEKDLQQVNESMDNSLNNLEKYFHEKWFLIFRELAHNITSWLKDCSESWKNAKQSIDSI | Function: May be required for cytoplasm to vacuole transport (Cvt) and pexophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65900
Sequence Length: 575
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctate structures.
Subcellular Location: Endosome membrane
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O60107 | MDFFEDNNPFSGSDNRSASSAVNVEPKVEPSQHQGSSSVKENAISQPNESFQSRNMFFQKDVDSVVDSALDPNGIVITGAMKAESGSHIVYIIKLQDSEIHHRYSEFASLRVQLSRLYPTCLVPPLPDKHKIMDYLINVTKNQRMSRMLEERKRLLQLFLRRVAQHPILGLSEVFRKFLSRHVSWKEVLHSPPISCLPKDLLKAPPADPSSKENAELYKELPIPSKTLVPRDNYDDVGKNFLMLEDTLQQYSIVAQEESNLFNQIVLSNSKYCLAHSTLGAMFNALSLSESGKLLTALEKVGQANDHTCLASIDFMHNFVIAVIEPLQELSKDAKNMRHIFIFRKMKFIQQVMVEELLTRKKSFLHLLERRERHAARLQQAIGEVDGDVILNRESEATLGVNNAQTSRSTIPEEDPLFNDEESKEPSVPLMGTDQPLENYHDGNGEQTEECLRDLRHNQSQDFETVSQDTSLTSVTVLPRTIRDVFDRIRFVLNGLTDNNVEVSRHNNIGRTAESVTHLTDMLLITTKDVAFVTDRVNFEFQRYQDTHRQDLNRILNRLTDSHIDWANRNLRIWNSVQESLKTYVS | Function: May be required for cytoplasm to vacuole transport (Cvt) and pexophagy (By similarity). Has a role in meiosis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 67002
Sequence Length: 586
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctate structures.
Subcellular Location: Cytoplasm
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Q6C9X0 | MSDFEDNNPFAGADRRDSVSSDATDDGPSASFLATNTTNDFGGASFMAGGGSFYGAASQIGGLGGMGMSAYDPESALANPFDDGSNSFSATPTASITNQNDTAHEATNERTTTASQSNIPPIEIIEANKNHEGTSRGFITYTIRVGDVSVRRRYSEFESLRTTLTRMFPTLIVPPIPEKHSITDYAVAPTKAREDKDMIEHRQRMLQVFLNRCRNLPQISNCIVFQRFLDPHASWSEVLNSPPVSTLPRYSLRAPPVDPSNNVTEAHSYLPIPSANGVVRNRGGDEEGKQEAFFAEAEKTAKEYEAVIGGGLEKVARRILKRYTDIAGDYAELGGRFNALSLEESDSRMAATVEKVGQAIDSNYLATNHLVRELGRQFGEPLAESAQFSGVVRSVLKYRKQKALQLELTSDSLEAKRVTLASLESAEADSQRINDALGRTRSNNGPSTTNSGEQPSASPAPKKSSGFKIPGLSSLNSAFNNMMDADPEASRRQGIGKTREQIGQLEQALEVAQKDIVVANESVEKDLERFRAEREADLKCMIRAFLKCHIDWAKQNLDTWQSAQAEVESM | Function: May be required for cytoplasm to vacuole transport (Cvt) and pexophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 62244
Sequence Length: 570
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctate structures.
Subcellular Location: Endosome membrane
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Q04053 | MDYNIFEAVHEQQSSTSDMDLSEEDNNPFVGTHHLYASGIGTTIGEARPENENSPPSSSSLPSSPAHSSSAGSSRASTSSSTSSHAVVEADAETEPFVSLSMSTTATISKFTPHDMNGTQQIQIIDAGDFKDPWGKHAIGYVILYENNKIIRRYSEFHSLRQSLTRLLPTIIIPPIPSKHSLLKYIWSPINAANDSKIISTRKKMLNSFLSNCLNIQEISNDIVFQKFLNPEFNWKDVLSSSPIIILPLNNLLAPPLSPTKPSPLHSILPIPSNSSLRNYNSIWQQHITVKSHNEISNLPTEILQNESQFTHIENLFQNYKRIITHLLKNIRSNKSHFHSLSTYFAELGAYYNAFSLENDITMPNSLRESENNSNNPMMEIISHIEKTGHSFDVIYISSEILIEKYTSILEDPINELLQFLNESFKVLNFKKLKFLQFKILERLIIEKETKLSSLTEIENQLQKINESLTRSTILTDENYKDTKAADLTFVKKDVRSLSKSSSNSSSSGHQNEIHIGASKLNYKTSTPTMNLNKLEIKQLTEQERSKQIKQLNQDLSKLKDCLSICISDMLEINNSSYNSLMHTYNHINLTIGKILKLFAASFKAWIKECLKNWKLAKLQIDEAL | Function: Involved in proper sorting of the v-SNARE protein SNC1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 70741
Sequence Length: 625
Domain: The PX domain binds to phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the punctate structures.
Subcellular Location: Prevacuolar compartment
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Q4WQI6 | MDQHDDFDSVSWRQDPESDISRPTTSGTDADESLEYNRDTNGKRRMSSVHEDPPQAGPLADAVDLAGIGDGVLECRVDSPLKENDGTKDAYISYLVTTHTDFKSFQKPDFAVRRRFTDFYFLYKTLYREYPACAVPPLPEKHKMEYVTGDRFGPEFTSRRAWSLHRFLKRLTLHPVLRRAPLLAIFLESPDWNAHMRLHSTRTSTGNSDGSGTGIFDNFTDTFVNAFTKVHKPDRRFIEVKEKADKLDEDLNHVEKIVARVARRESDLEADYNDLATQFRKLVPLEPDVEVPLQIFAASVEETARGFKMLKDHTDQNYLGSLRDMEAYIVSVKALLKTREQKQLDFEALVDYRNKAVAERDSLAANPSSYYASNPLTSSPASFIRSKMEDMRGVDHEQSRRERVRKLELRIDELTREVESAKTTSEMFDEEVVREVADFERIKAVEFRDTLGALAEKHIDFFQGAINTWERFVAEMEGDLDNDPEMSEHGRGGGVAA | Function: Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56858
Sequence Length: 497
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctate structures.
Subcellular Location: Cytoplasm
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Q5AD77 | MSSEDQFTSIQWDRDDGENTNNTPTDTTIKSKSSKSKKSKKSSSKKKNGNKISPSSTTETSDADDTMKEVTDQLESTQINDDNHEVDDGNKEQNVDANQIGNSDEDPTNSLLLPVNPQPKEPQEEKEDLQQQLQQPQQQLASIQQEPAPIQPPFNAVVNDESLSIQQQQQQQQPTGYVDISYYEKYSIKTTVTHPNRDLDTASKPFISYLVTTTTDNPSILKLTKEKKPKQGEEYLTFSVRRRYGDFRYLYESLSNDFPTVMIPPLPSKSNFKYLTGDTFSSEFVHKRLHSLDRFIRFILQHKILSQSSIFHLFISNSNDWATFTTSLKLKDSSSDESGIVGRVVNEDLITETVMNFLTPSKHKKETNKDILEINDKLKKLYENLIKLDKIFTKLKKKNHELGNDYDQFSNQILKLSSVQKGEDSIMTTNFKIFSDSLNYFSKSYNEMYRYIDENFLISLQDLAKFCLRFIQLIKLKNDKSTDLAVLQDFLNKELANNSGGSGSGSGSGGSGLHQPPNPVISSYQGGIVNNTTQLIKDTLSTSNTTISNTIKSDKIKNLEQEIAKETKILTDLTNKIINEEYPNWEKFNKIEIKNSMLGLCDQNIKFYNDLLEKFGEVEMKLIKRLDEDM | Function: Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 71842
Sequence Length: 630
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctate structures.
Subcellular Location: Cytoplasm
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Q6FPT9 | MDSASADASVTGSGNAKGSSAERVNGGGKFYKLEILVSDPQKRAGEAGLGPYVSYQISTRTDNPSYHGNQKASFDDIIVVHRRYNDVVLLHDILQNDHPTCIIPPLPDKKVLQYIAGDRFGRRFTQRRCHSLQNFLRRVSQHPILSTSKVLEIFLVGNEWDTYRKNIAGTLQNAQKEDVTDAVMNAFKKVHNQNEEFTEIRDRSDKLDNSVNRINKVFHRVVKKNEAIIEDYSKLGLTLQELQELVSSDNDKLADSLKVFIEGVTQFSYGLQDLNMFIDYEYLIDLKDLSHYIGSMKQTMRLKDQKQIDYEELSDYLTKSIKEKNNLISGYGGGNFLTSKLEELAGYNQEASRRDKINKLESTISSLTTELETAKKVADTFEQETLKEVKKFEEIKNDELKISLNNLADENIKFYERMLETWEKVDQSLR | Function: Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 49222
Sequence Length: 430
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctate structures.
Subcellular Location: Cytoplasm
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P0CR63 | MDQDGFHSIAWDDAPSSNPPLSAPSPSQSPFEEGFESISPSSAQPPASDQYEGYDNSKAGEAGDVGVTLDRRERLGGHEVDGSVWNGKWMDVQVREPAKEHEGSKDMYVSYAVKTETSLPTFRKPLTVVRRRFQDFVFLREHLVKNFPACVVPPIPDKHRLEYIKGDRFSPEFVERRRLDLQRFADRIARHPVLQRSQLVNDFLQSTEWSVAKHHHISHPPPESHASLIDSLSDTFINAFSRVRKPDARFVEMTEELERFEEGLTGVERVVGRGKSRVDDLAADYQDMAAAYQGLGYLESGITEPLNRFAEKMLDFSTLLKHMNNTTIEPFLSSSHSLLSYSATHRNVIKLRDQKQLDFEELSAYLSAIVSERDRLAALSSGHTAAPVGLGTYLRDQMDKLRGTDDIHTRRERMRKMDGKIKELQDAVTLAHETSNAFSEEVIKEHAYFELEKKQEMKDALQAYTDGQVEMLQQAMDDWDRIIPLLQRIRVDV | Function: Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56177
Sequence Length: 493
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctate structures.
Subcellular Location: Cytoplasm
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Q6BZE9 | MSSDDQFTSIQWDRDELGPNKETKVNKQETITEDDEHHNNDNEDKDNDTTKSNEPENIQEDDETKDDNEPTDSLILSKTGDENISNIESQNEGDHIVGEPDVNQEPSSDSQTEAYEINVVVTSPLRDLDSSSKPYISYLLTTATNHPSVMKLSTVKKEQGKEVVEITARRRYGDFRFLFDCLSNDHPEVMMPPLPSKSNFKYLTGDTFSTEFVHKRLHSLDRFVRFITCHKVLSQSSIFHLFVSDSADWSTFQKNLKISKVGVQESDADKGNSSMTSNVVNKVVNEDLLTETIMNFLTPSKHKRETNKEILEISDKLKKLYENLIKLDKIFTKLNKKNHDLSVDYEQFSQQIMKLSVIQNSSDETNEPTTPEINEQKQFATNFKVFASSLSYFSDNWSNLHKYIDESFLVSLKDCAKYIISLTNLIELQHNKKIDLQVLQDYLNKAKSELQGLGGSHNAPPNPIITHNNGGIVNNTTQLIRDTLSTSATPNIGSSVTESKVTKLQNRITELENEISVQSQLVLDLTNKIINEEYPNWDKFNKIELKESLLGLCNEEISFYKGLVDNWSDIELKLLKRLDELK | Function: Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 66454
Sequence Length: 582
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctate structures.
Subcellular Location: Cytoplasm
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O75908 | MEPGGARLRLQRTEGLGGERERQPCGDGNTETHRAPDLVQWTRHMEAVKAQLLEQAQGQLRELLDRAMREAIQSYPSQDKPLPPPPPGSLSRTQEPSLGKQKVFIIRKSLLDELMEVQHFRTIYHMFIAGLCVFIISTLAIDFIDEGRLLLEFDLLIFSFGQLPLALVTWVPMFLSTLLAPYQALRLWARGTWTQATGLGCALLAAHAVVLCALPVHVAVEHQLPPASRCVLVFEQVRFLMKSYSFLREAVPGTLRARRGEGIQAPSFSSYLYFLFCPTLIYRETYPRTPYVRWNYVAKNFAQALGCVLYACFILGRLCVPVFANMSREPFSTRALVLSILHATLPGIFMLLLIFFAFLHCWLNAFAEMLRFGDRMFYRDWWNSTSFSNYYRTWNVVVHDWLYSYVYQDGLRLLGARARGVAMLGVFLVSAVAHEYIFCFVLGFFYPVMLILFLVIGGMLNFMMHDQRTGPAWNVLMWTMLFLGQGIQVSLYCQEWYARRHCPLPQATFWGLVTPRSWSCHT | Function: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol . Plays a role in lipoprotein assembly and dietary cholesterol absorption . Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) and linolenoyl-CoA ((9Z,12Z,15Z)-octadecatrienoyl-CoA) as substrates . May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa .
PTM: Polyubiquitinated by AMFR/gp78 at Cys-277, leading to its degradation when the lipid levels are low . Association with AMFR/gp78 is mediated via interaction with INSIG1 . High concentration of cholesterol and fatty acid results in Cys-277 oxidation, preventing ubiquitination at the same site, resulting in protein stabilization .
Location Topology: Multi-pass membrane protein
Catalytic Activity: a long-chain fatty acyl-CoA + a sterol = a sterol ester + CoA
Sequence Mass (Da): 59896
Sequence Length: 522
Domain: Each protomer consists of 9 transmembrane segments, which enclose a cytosolic tunnel and a transmembrane tunnel that converge at the predicted catalytic site: acyl-CoA enters the active site through the cytosolic tunnel, whereas cholesterol enters from the side through the transmembrane tunnel.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.26
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O88908 | MQPKVPQLRRREGLGEEQEKGARGGEGNARTHGTPDLVQWTRHMEAVKTQFLEQAQRELAELLDRALWEAMQAYPKQDRPLPSAAPDSTSKTQELHPGKRKVFITRKSLIDELMEVQHFRTIYHMFIAGLCVLIISTLAIDFIDEGRLMLEFDLLLFSFGQLPLALMTWVPMFLSTLLVPYQTLWLWARPRAGGAWMLGASLGCVLLAAHAVVLCVLPVHVSVRHELPPASRCVLVFEQVRLLMKSYSFLRETVPGIFCVRGGKGISPPSFSSYLYFLFCPTLIYRETYPRTPSIRWNYVAKNFAQVLGCLLYACFILGRLCVPVFANMSREPFSTRALLLSILHATGPGIFMLLLIFFAFLHCWLNAFAEMLRFGDRMFYRDWWNSTSFSNYYRTWNVVVHDWLYSYVYQDGLWLLGRRARGVAMLGVFLVSAVVHEYIFCFVLGFFYPVMLMLFLVFGGLLNFTMNDRHTGPAWNILMWTFLFMGQGIQVSLYCQEWYARRHCPLPQTTFWGMVTPRSWSCHP | Function: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) and linolenoyl-CoA ((9Z,12Z,15Z)-octadecatrienoyl-CoA) as substrates. May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa.
PTM: Polyubiquitinated by AMFR/gp78 at Cys-280, leading to its degradation when the lipid levels are low. Association with AMFR/gp78 is mediated via interaction with INSIG1. High concentration of cholesterol and fatty acid results in Cys-280 oxidation, preventing ubiquitination at the same site, resulting in protein stabilization.
Location Topology: Multi-pass membrane protein
Catalytic Activity: a long-chain fatty acyl-CoA + a sterol = a sterol ester + CoA
Sequence Mass (Da): 60597
Sequence Length: 525
Domain: Each protomer consists of 9 transmembrane segments, which enclose a cytosolic tunnel and a transmembrane tunnel that converge at the predicted catalytic site: acyl-CoA enters the active site through the cytosolic tunnel, whereas cholesterol enters from the side through the transmembrane tunnel.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.26
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A6QP84 | MRANCSSGLACPANSSEEELPEGLKAFGNLDLVFTVVSALMIGLLMFSLGCSVEVQKLWGHIRRPWGIAVGMLCQFGLMPLIAYLLIISFSLKPLQAIAVLIMGCCPGGTVSNIFTFWVDGDMDLSISMTTCSTMAALGMMPLCLYLYTLSWNLEQNLTIPYQNIGITLVCLIIPVAFGIYVNYRWPKQSKIILKIGAIAGGLLFLVVTGAGMVLMKEFWSSDIILLMISFIFPLIGHATGFLLALLTHQSWQRCRTISLETGTQNVQMCFTMLQLSFTAEQLVQIFGFVLAYGLFQMLNGFFMVAAYKMYKRRLKNKHGNEKPSCQEARHRKKSTSPKETTAFLEVNEEATLSPGPSGPVDPHGAPTPTGDIARAK | Function: Transports sulfoconjugated steroid hormones from the extracellular compartment into the cytosol in a sodium-dependent manner without hydrolysis. Steroid sulfate hormones are commonly considered to be biologically inactive metabolites, that may be activated by steroid sulfatases into free steroids (By similarity). May play an important role by delivering sulfoconjugated steroids to specific target cells in reproductive organs (By similarity). May play a role transporting the estriol precursor 16alpha-hydroxydehydroepiandrosterone 3-sulfate (16a-OH-DHEAS) at the fetal blood vessel endothelium (By similarity). Can also transport other sulfoconjugated molecules such as taurolithocholic acid-3-sulfate and sulfoconjugated pyrenes (By similarity).
PTM: Glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: estrone 3-sulfate(out) + 2 Na(+)(out) = estrone 3-sulfate(in) + 2 Na(+)(in)
Sequence Mass (Da): 41438
Sequence Length: 377
Subcellular Location: Membrane
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Q3KNW5 | MRANCSSSSACPANSSEEELPVGLEVHGNLELVFTVVSTVMMGLLMFSLGCSVEIRKLWSHIRRPWGIAVGLLCQFGLMPFTAYLLAISFSLKPVQAIAVLIMGCCPGGTISNIFTFWVDGDMDLSISMTTCSTVAALGMMPLCIYLYTWSWSLQQNLTIPYQNIGITLVCLTIPVAFGVYVNYRWPKQSKIILKIGAVVGGVLLLVVAVAGVVLAKGSWNSDITLLTISFIFPLIGHVTGFLLALFTHQSWQRCRTISLETGAQNIQMCITMLQLSFTAEHLVQMLSFPLAYGLFQLIDGFLIVAAYQTYKRRLKNKHGKKNSGCTEVCHTRKSTSSRETNAFLEVNEEGAITPGPPGPMDCHRALEPVGHITSCE | Function: Transports sulfoconjugated steroid hormones from the extracellular compartment into the cytosol in a sodium-dependent manner without hydrolysis . Steroid sulfate hormones are commonly considered to be biologically inactive metabolites, that may be activated by steroid sulfatases into free steroids . May play an important role by delivering sulfoconjugated steroids to specific target cells in reproductive organs (By similarity). May play a role transporting the estriol precursor 16alpha-hydroxydehydroepiandrosterone 3-sulfate (16a-OH-DHEAS) at the fetal blood vessel endothelium . Can also transport other sulfoconjugated molecules such as taurolithocholic acid-3-sulfate and sulfoconjugated pyrenes .
PTM: Glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: estrone 3-sulfate(out) + 2 Na(+)(out) = estrone 3-sulfate(in) + 2 Na(+)(in)
Sequence Mass (Da): 41259
Sequence Length: 377
Subcellular Location: Membrane
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Q9CXB2 | MSTDCAGNSTCPVNSTEEDPPVGMEGHANLKLLFTVLSAVMVGLVMFSFGCSVESQKLWLHLRRPWGIAVGLLSQFGLMPLTAYLLAIGFGLKPFQAIAVLMMGSCPGGTISNVLTFWVDGDMDLSISMTTCSTVAALGMMPLCLYIYTRSWTLTQNLVIPYQSIGITLVSLVVPVASGVYVNYRWPKQATVILKVGAILGGMLLLVVAVTGMVLAKGWNTDVTLLVISCIFPLVGHVTGFLLAFLTHQSWQRCRTISIETGAQNIQLCIAMLQLSFSAEYLVQLLNFALAYGLFQVLHGLLIVAAYQAYKRRQKSKCRRQHPDCPDVCYEKQPRETSAFLDKGDEAAVTLGPVQPEQHHRAAELTSHIPSCE | Function: Transports sulfoconjugated steroid hormones from the extracellular compartment into the cytosol in a sodium-dependent manner without hydrolysis . Steroid sulfate hormones are commonly considered to be biologically inactive metabolites, that may be activated by steroid sulfatases into free steroids (By similarity). May play an important role by delivering sulfoconjugated steroids to specific target cells in reproductive organs . May play a role transporting the estriol precursor 16alpha-hydroxydehydroepiandrosterone 3-sulfate (16a-OH-DHEAS) at the fetal blood vessel endothelium (By similarity). Can also transport other sulfoconjugated molecules such as taurolithocholic acid-3-sulfate and sulfoconjugated pyrenes (By similarity).
PTM: Glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: estrone 3-sulfate(out) + 2 Na(+)(out) = estrone 3-sulfate(in) + 2 Na(+)(in)
Sequence Mass (Da): 40681
Sequence Length: 373
Subcellular Location: Membrane
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Q9LEZ1 | MESANIFGSDEDCRSCESGWTMYLASQSHDRDDDCYYGDDDEEEEDSDGGDSMDSDASSGPMEATSYLKLAQEIEEQNSIKKKKKKTNEEMVLVETTRVHNNINHDDDDDDDEDDGDNHDYDDGNDSYSVVHSYVGSVRQKGLV | Function: Involved in cytokinin-mediated development . Promotes the expression of cytokinin synthases (e.g. IPT3 and IPT7), thus triggering the accumulation of trans-zeatin riboside, trans-zeatin riboside monophosphate and isopentenyladenine 9-glucoside .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16200
Sequence Length: 144
Domain: Domains SOFL-A and SOFL-B are required for function in cytokinin-mediated development.
Subcellular Location: Cytoplasm
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Q95088 | INGDAKGTVFFEQETSEAPVKVTGEGLGLAKGLHGFHVHEFGDNTNGCMSSGPHFNPRNKEHGAPTDENRHLGDLGNIQAAGDSPTAVSITDSKITLFGADSIIGRTVVVHADA | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 11864
Sequence Length: 114
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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P0AGD2 | MKRFSLAILALVVATGAQAASEKVEMNLVTSQGVGQSIGSVTITETDKGLEFSPDLKALPPGEHGFHIHAKGSCQPATKDGKASAAESAGGHLDPQNTGKHEGPEGAGHLGDLPALVVNNDGKATDAVIAPRLKSLDEIKDKALMVHVGGDNMSDQPKPLGGGGERYACGVIK | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 17681
Sequence Length: 173
Subcellular Location: Periplasm
EC: 1.15.1.1
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Q59448 | MTAFYKLCGMSMLSLVLADCTFLSANKPYDRDHDGELIVHMKDVNTHKEVGTITISPYIHDGNQEGMLITPHLYNLPANTTHGMHIHINPSCEDNGIAAGGHWDPDNTQKHLGPYNDNGHKGDLPVLVVNADGTATEPVVAPKLNSLEELAGHSLMLHAGGDNYSDKPQPLGGGGARMWCGVIAD | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 19887
Sequence Length: 185
Subcellular Location: Periplasm
EC: 1.15.1.1
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P81926 | MSIKAVCVLVGSVKGTLNFKQDAIGSCTVTGEVSGLIPGKHGFHIHEYGDLTNGCTSSGGHFNPFKQIHGAPEDDIRHVGDLGNITADSSGVATVNITDRMISLTGEHSIIGRAVVVHAGEDDLGKGGHEDSKTTGHAGGRLSCGVIGINHL | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. The plasma superoxide dismutase has phagocytosis-stimulating activity and may play an important role in the biological defenses of the organism.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 15620
Sequence Length: 152
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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P34936 | MXKAVAVLTGSEGVXGTIFFTQ | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 2279
Sequence Length: 22
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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P28759 | MASLGGLQNVSGINFLIKEGPKVNAKFELKPPPYPLNGLEPVMSQQTLEFHWGKHHKTYVENLKKQVVGTELDGKSLEEIIVTSYNKGDILPAFNNAAQVWNHDFFWECMKPGGGGKPSGELLELIERDFGSFVKFLDEFKAAAATQFGSGWAWLAYRARKFDGENVANPPSPDEDNKLVVLKSPNAVNPLVWGGYYPLLTIDVWEHAYYLDFQNRRPDYISVFMDKLVSWDAVSSRLEQAKALITSA | Cofactor: Binds 1 Fe cation per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 27842
Sequence Length: 248
Subcellular Location: Plastid
EC: 1.15.1.1
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O51917 | MSVYTLPELPYDYSALAPVISPEIIELHHDKHHAAYVKGANDTLEQLAEARDKETWGSINGLEKNLAFHLSGHILHSIYWHNMTGDGGGEPLDKDGVGELADAIAESFGSFAGFRAQLTKAAATTQGSGWGVLAYEPLSGRLIVEQIYDHQGNVGQGSTPILVFDAWEHAFYLQYKNQKVDFIDAMWAVVNWQDVARRYEAAKSRTNTLLLAP | Cofactor: Binds 1 Fe(3+) or Zn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 23527
Sequence Length: 213
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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Q08713 | MTQVIQLKRYEFPQLPYKVDALEPYISKDIIDVHYNGHHKGYVNGANSLLDRLEKLIKGDLPQGQYDLQGILRGLTFNINGHKLHAIYWNNMAPAGKGGGKPGGALADLINKQYGSFDRFKQVFSESANSLPGSGWTVLYYDNESGNLQIMTVENHFMNHIAELPVILIVDEFEHAYYLQYKNKRGDYLNAWWNVVNWDDAEKRLQKYLNK | Cofactor: Binds 1 Fe cation per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 24266
Sequence Length: 211
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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P19666 | LNYEYSDLEPVLSAHLLSFHHGKHHQAYVNNLNATYEQIAAATKENDAHKIATLQSALRFNLGGHVNHWIYWDNLAPVKSGGGVLPDEHSPLTKAIKEKWGSYENFITLFNTRTAAIQGSGWGWLGYDTVSKSLRLFELGNQDMPEWSSIVPLLTIDVWEHAYYLDYQNLRPKYLTEVWKIVNWREVEKRYLQAIE | Cofactor: Binds 1 Fe cation per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 22657
Sequence Length: 196
EC: 1.15.1.1
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P53647 | MAEYTLPDLDWDYAALEPHISGQINEIHHTKHHATYVKGVNDALAKLEEARANEDHAAIFLNEKNLAFHLGGHVNHSIWWKNLSPDGGDKPTGELAAAIDDAFGSFDKFRAQFSAAANGLQGSGWAVLGYDTVGSRLLTFQLYDQQANVPLGIIPLLQVDMWEHAFYLQYKNVKADYVKAFWNVVNWADVQKRYAAATSKAQGLIFG | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 23030
Sequence Length: 207
Subcellular Location: Secreted
EC: 1.15.1.1
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P80582 | AEYTLPDLGWDYAASGPG | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 1883
Sequence Length: 18
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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Q9Y783 | MVNLGSIWQNLLASQAPLQSMTGNATTMAGLATYSLPQLPYAYNALEPYISAQIMELHHSKHHQTYVTNLNNALKVHVAAIASSDIPAQIAQQPAIKFNGGGHINHSLFWKNLAPAETPETNYSKAAPSLAAEIEKTWGSFDEFKKAFSAALLGIQGSGWGWLVKESTAEKGRLRIITTKDQDPVVGGEVPVFGVDMWEHAYYLQYLNGKAAYVENIWKVINWKTAEERFQGSREDAFADLKALL | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 27020
Sequence Length: 245
Subcellular Location: Mitochondrion matrix
EC: 1.15.1.1
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Q43008 | MALRTLASRKTLAAAALPLAAAAAARGVTTVALPDLPYDYGALEPAISGEIMRLHHQKHHATYVANYNKALEQLDAAVAKGDAPAIVHLQSAIKFNGGGHVNHSIFWNNLKPISEGGGDPPHAKLGWAIDEDFGSFEALVKKMSAEGAALQGSGWVWLALDKEAKKLSVETTANQDPLVTKGANLVPLLGIDVWEHAYYLQYKNVRPDYLSNIWKVMNWKYAGEVYENATA | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 24997
Sequence Length: 231
Subcellular Location: Mitochondrion matrix
EC: 1.15.1.1
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P28765 | HISEMIMQIHHTKHHQAYINNLKACTEKLKQAEQANDVAAMNALLPAIKFNGGGHINHTIFWTNMAPSAGGEPAGPVADAITKEFGSFQAFKDKFSTASVGVKGSGWGWLGYCPKNDKLAVATCQNQDPLQLTHGLIPLLGLDV | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 15505
Sequence Length: 144
Subcellular Location: Mitochondrion matrix
EC: 1.15.1.1
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Q9CPN6 | MAYTLPELGYAYDALEPHFDAMTMEIHHSKHHQAYVNNANAALENLPELAQGCPGQLLTKLAEVPADKLTAIRNNVGGHLNHSLFWKSLKKGTTLQGALKDAIVRDFGSVEAFQAEFEKAAATRFGSGWAWLVLQENGKLAVVSTANQDSPVMGKAIAGCEGYPLLGLDVWEHAYYLKFQNRRPDYIKEFWHVVNWDFVAERFEKKVEHCNCTK | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 24020
Sequence Length: 214
EC: 1.15.1.1
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O75007 | MTSQTHTLPPLPYAYDALEPVISKQIMELHHQKHHQTYINNLNAALSAQASATASNDVPTLISLQQKLRFNGGGHINHSLFWKNLTPPGTPANDIAGAPALREAIVSRWGSHEAFVKAFGAELLGLQGSGWGWLVSKGGAKGRLEIVTTKDQDPVNAPDVPVFGVDMWEHAYYLQYLNNKAGYVEGIWKIIHWAEAEKRYTAGVENPLKL | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
PTM: The N-terminus is blocked.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 23128
Sequence Length: 210
Subcellular Location: Mitochondrion matrix
EC: 1.15.1.1
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I3V6A7 | MATNGEIFNTYGHNRQTATVTKITASNESSNGVCYLSETANLGKLICIPMALRAAMELNVFQLISKFGTDAKVSASEIASKMPNAKNNPEAAMYLDRILRLLGASSILSVSTTKKSINRGGDDVVVHEKLYGLTNSSCCLVPRQEDGVSLVEELLFTSDKVVVDSFFKLKCVVEEKDSVPFEVAHGAKIFEYAATEPRMNQVFNDGMAVFSIVVFEAVFRFYDGFLDMKELLDVGGGIGTSVSKIVAKYPLIRGVNFDLPHVISVAPQYPGVEHVAGDMFEEVPKGQNMLLKWVLHDWGDERCVKLLKNCWNSLPVGGKVLIIEFVLPNELGNNAESFNALIPDLLLMALNPGGKERTISEYDDLGKAAGFIKTIPIPISNGLHVIEFHK | Function: Methyltransferase involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine . Catalyzes the conversion of (S)-scoulerine to (S)-tetrahydrocolumbamine . Can convert (S)-tetrahydrocolumbamine to tetrahydropalmatine . Can convert (S)-norreticuline to (S)-norcodamine . Can convert (S)-reticuline to (S)-codamine . Substrate preference is (S)-scoulerine > (S)-tetrahydrocolumbamine > (S)-norreticuline > (S)-reticuline .
Catalytic Activity: (S)-scoulerine + S-adenosyl-L-methionine = (S)-tetrahydrocolumbamine + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42699
Sequence Length: 390
Pathway: Alkaloid biosynthesis.
EC: 2.1.1.117
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I3PLQ6 | MEIHLESQEQEMKYQSQIWNQICGTVDTSVLRCAIQLGIFDAIHNSGKPMITLTELSSIVSSPSSSSIEPCNLYRLVRYLSQMDLISIGECLNEATVSLTGTSKLLLRNQEKSLIDWVLAISCEMMVVVWHELSSSVSTPADEPPIFQKVHGKNALELAGEFPEWNDLINNAMTSDTSVTKPALIQGCGKILNGVTSLIDVGGGHGATMAYIVEAFPHIKGAVIDLPHVVEAAPERPGVEFISGDIFKSISNADAVLLKYVLHNWEDTECVNLLKRCKEAVPADKGKVIIMDLVIDDDDNSILTQAKLSLDLTVMNHGGGRERTKEDWRNLIEMSGFSRHEIIPISAMPSIIVAYP | Function: Methyltransferase involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine . Catalyzes the conversion of (S)-scoulerine to (S)-tetrahydrocolumbamine . The heterodimers SOMT2-SOMT3 and SOMT2-6OMT convert 3-O-acetyl-4'-O-demethylpapaveroxine to 3-O-acetylpapaveroxine, where SOMT2 is the catalytic subunit .
Catalytic Activity: (S)-scoulerine + S-adenosyl-L-methionine = (S)-tetrahydrocolumbamine + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39087
Sequence Length: 356
Pathway: Alkaloid biosynthesis.
EC: 2.1.1.117
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C6TAY1 | MASPLNNGRKASEIFQGQALLYKHLLGFIDSKCLKWMVELDIPDIIHSHSHGQPITFSELVSILQVPPTKTRQVQSLMRYLAHNGFFEIVRIHDNIEAYALTAASELLVKSSELSLAPMVEYFLEPNCQGAWNQLKRWVHEEDLTVFGVSLGTPFWDFINKDPAYNKSFNEAMACDSQMLNLAFRDCNWVFEGLESIVDVGGGTGITAKIICEAFPKLKCMVLERPNVVENLSGSNNLTFVGGDMFKCIPKADAVLLKLVLHNWNDNDCMKILENCKEAISGESKTGKVVVIDTVINENKDERQVTELKLLMDVHMACIINGKERKEEDWKKLFMEAGFQSYKISPFTGYLSLIEIYP | Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the 4'-methylation of naringenin (4',5,7-trihydroxyflavanone) into ponciretin (4'-methoxy-5,7-dihydroxyflavanone). In vitro, also able to convert apigenin, daidzein, genistein and quercetin into the 4'-O-methylated compounds acacetin, formononetin, biochanine A and 4'-methylated quercetin, respectively.
Catalytic Activity: a 4'-hydroxyflavanone + S-adenosyl-L-methionine = a 4'-methoxyflavanone + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 40436
Sequence Length: 358
EC: 2.1.1.231
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P48434 | MNLLDPFMKMTEEQDKCISDAPSPTMSDDSAGSPCPSGSGSDTENTRPQENTFPKGDPDLKKESDEDKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKNKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQSEQEEGSEQTHISPNAIFKALQADSPQSSSSISEVHSPGEHSGQSQGPPTPPTTPKTDAQQPGKQDLKREGRPLAEGGRQPPHIDFRDVDIGELSSDVISNIETFDVNEFDQYLPPNGHPGVPATHGQVTTYSGTYGISSSASSPAGAGHAWMAKQQPQPPQPPAQPPAQHTLPALSGEQGPAQQRPHIKTEQLSPSHYSEQQQHSPQQQQQQQQQLGYGSFNLQHYGSSYPPITRSQYDYTEHQNSGSYYSHAAGQSGGLYSTFTYMNPTQRPMYTPIADTSGVPSIPQTHSPQHWEQPVYTQLTRP | Function: Transcription factor that plays a key role in chondrocytes differentiation and skeletal development . Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including COL2A1 . Plays a central role in successive steps of chondrocyte differentiation. Absolutely required for precartilaginous condensation, the first step in chondrogenesis during which skeletal progenitors differentiate into prechondrocytes (By similarity). Together with SOX5 and SOX6, required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes, the second step in chondrogenesis (By similarity). Later, required to direct hypertrophic maturation and block osteoblast differentiation of growth plate chondrocytes: maintains chondrocyte columnar proliferation, delays prehypertrophy and then prevents osteoblastic differentiation of chondrocytes (By similarity). Also required for chondrocyte hypertrophy, both indirectly, by keeping the lineage fate of chondrocytes, and directly, by remaining present in upper hypertrophic cells (By similarity). Low lipid levels are the main nutritional determinant for chondrogenic commitment of skeletal progenitor cells: when lipids levels are low, FOXO transcription factors promote expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). In addition to cartilage development, also acts as a regulator of proliferation and differentiation in epithelial stem/progenitor cells (By similarity). In response to bone morphogenetic protein stimulus, phosphorylation is induced and then sumoylation, allowing cooperation with SNAI2 to trigger neural crest delamination .
PTM: Phosphorylated at Ser-181 in the developing neural tube. Phosphorylation at either Ser-64 or Ser-181 is required for sumoylation, but phosphorylation is not dependent on sumoylation. Sumoylation is enhanced by PKA. Phosphorylation is required for interaction with SNAI2 to trigger neural crest delamination and for an efficient trunk neural crest delamination, whereas sumoylation plays a less significant role. Phosphorylation and sumoylation are induced by BMP signaling pathway.
Sequence Mass (Da): 54848
Sequence Length: 494
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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Q04887 | MNLLDPFMKMTDEQEKGLSGAPSPTMSEDSAGSPCPSGSGSDTENTRPQENTFPKGEPDLKKESEEDKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKNKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQAEAEEATEQTHISPNAIFKALQADSPHSSSGMSEVHSPGEHSGQSQGPPTPPTTPKTDVQAGKVDLKREGRPLAEGGRQPPIDFRDVDIGELSSDVISNIETFDVNEFDQYLPPNGHPGVPATHGQVTYTGSYGISSTAPTPATAGHVWMSKQQAPPPPPQQPPQAPQAPQAPPQQQAPPQQPQAPQQQQAHTLTTLSSEPGQSQRTHIKTEQLSPSHYSEQQQHSPQQISYSPFNLPHYSPSYPPITRSQYDYADHQNSGSYYSHAAGQGSGLYSTFTYMNPAQRPMYTPIADTSGVPSIPQTHSPQHWEQPVYTQLTRP | Function: Transcription factor that plays a key role in chondrocytes differentiation and skeletal development . Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including cartilage matrix protein-coding genes COL2A1, COL4A2, COL9A1, COL11A2 and ACAN, SOX5 and SOX6 . Also binds to some promoter regions . Plays a central role in successive steps of chondrocyte differentiation . Absolutely required for precartilaginous condensation, the first step in chondrogenesis during which skeletal progenitors differentiate into prechondrocytes . Together with SOX5 and SOX6, required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes, the second step in chondrogenesis . Later, required to direct hypertrophic maturation and block osteoblast differentiation of growth plate chondrocytes: maintains chondrocyte columnar proliferation, delays prehypertrophy and then prevents osteoblastic differentiation of chondrocytes by lowering beta-catenin (CTNNB1) signaling and RUNX2 expression . Also required for chondrocyte hypertrophy, both indirectly, by keeping the lineage fate of chondrocytes, and directly, by remaining present in upper hypertrophic cells and transactivating COL10A1 along with MEF2C . Low lipid levels are the main nutritional determinant for chondrogenic commitment of skeletal progenitor cells: when lipids levels are low, FOXO (FOXO1 and FOXO3) transcription factors promote expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation . Mechanistically, helps, but is not required, to remove epigenetic signatures of transcriptional repression and deposit active promoter and enhancer marks at chondrocyte-specific genes . Acts in cooperation with the Hedgehog pathway-dependent GLI (GLI1 and GLI3) transcription factors . In addition to cartilage development, also acts as a regulator of proliferation and differentiation in epithelial stem/progenitor cells: involved in the lung epithelium during branching morphogenesis, by balancing proliferation and differentiation and regulating the extracellular matrix . Controls epithelial branching during kidney development .
PTM: Acetylated; acetylation impairs nuclear localization and ability to transactivate expression of target genes . Deacetylated by SIRT1 .
Sequence Mass (Da): 56077
Sequence Length: 507
Domain: The transactivation domains TAM and TAC (for transactivation domain in the middle and at the C-terminus, respectively) are required to contact transcriptional coactivators and basal transcriptional machinery components and thereby induce gene transactivation.
Subcellular Location: Nucleus
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D3DJG4 | MGKWVTIIFVLFLYAIAQQENPAEEVKKQKELLLKEMGILPGDVYAEQGRDMFNKPMGNAGKSCSSCHGQDGRYLRGAYAHMPRYYKDMDAVADLDTRIKYCMEKYMGVGNVKHDLNFKSIATYVATLSNGMKMDVKLTHPKEREMYEKGRELWYARVGKMDFSCAICHDSEAGKRVFLQTVVAVKEDKVATHWPAYRFSNDQLWTMEDRIRGCFGDMRVAPPEHFHWAVVALNLYLSYKAKGGVVRVPGFIY | Cofactor: Binds 2 heme c groups covalently per subunit.
Function: C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.
PTM: Cysteine persulfide at Cys-214.
Catalytic Activity: 2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]
Sequence Mass (Da): 29025
Sequence Length: 253
Subcellular Location: Periplasm
EC: 2.8.5.2
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D3DJG5 | MRKLWFLPILLGAVGGVSLYAIAQQENPAEEVKKQKELLLKEMGILPGDVYAEQGRDMFNKPMGNAGKSCSSCHGQDGRYLRGAYAHMPRYYKDMDAVADLDTRIKYCMEKYMGVGNVKHDLNFKSIATYVATLSNGMKMDVKLTHPKEREMYEKGRELWYARVGKMDFSCAICHDTFGGQRIRLQTLAKVKEDKVATHWPAYRFSNDQLWTMEDRIRGCYNQIRVTPPPHFSWPQIALSLYMAYESKGGTIETPGFVR | Cofactor: Binds 2 heme c groups covalently per subunit.
Function: C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.
PTM: Cysteine persulfide at Cys-220.
Catalytic Activity: 2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]
Sequence Mass (Da): 29659
Sequence Length: 259
Subcellular Location: Periplasm
EC: 2.8.5.2
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Q1W3E4 | MTKHGFLLATLVLAGATLPIGPVTAATPEEEQAAFQAYFKQRFPNVPEDEFKNGTYAIDPVTRENWEAIEEFPPYENAISQGETLWNTPFADGQGYADCFPDGPAIMNHYPRWDRERGQVMTLPLALNACRTAHGETPLKYKKGPIADLLAYIAFESRGQITRVEIPQDDPRALAAYEQGKRFYFARRGQLNFACAHCHLATSGTKLRTETLSPAYGHTTHWPVYRSEWGEMGTLHRRFAGCNEQVRAKAFEPQGEEYRNLEYFLTYMNNGLELNGPGARK | Cofactor: Binds 1 heme group per subunit.
Function: C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the intermediary formation of conspicuous sulfur globules inside of the cells.
PTM: Cysteine persulfide at Cys-242.
Catalytic Activity: 2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]
Sequence Mass (Da): 31730
Sequence Length: 281
Subcellular Location: Periplasm
EC: 2.8.5.2
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Q8RLX0 | MKKTIQRGLFTGALVLLTAMTSKPAHAAVNYQALVDADVKKFQGYFLKEFPGVKLEDFGDGVYALDEDSRKQWKEMEEFPPYELDVEAGKALFNKPFANGKSLGSCFSNGGAVRGMYPYFDEKRKEVITLEMAINECRVANGEKPYAPKKGDIARVSAYIASISRGQKIDVKVKSKAAYDAYMKGKEMFYAKRGQLNMSCSGCHMEYSGRHLRAEIISPALGHTTHFPVFRSKWGEIGTLHRRYAGCNENIGAKPFPAQSKEYRDLEFFQTVMSNGLKFNGPASRK | Cofactor: Binds 1 heme group per subunit.
Function: C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c and which then may be used for reductive CO(2) fixation.
PTM: Cysteine persulfide at Cys-247.
Catalytic Activity: 2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]
Sequence Mass (Da): 32026
Sequence Length: 286
Subcellular Location: Periplasm
EC: 2.8.5.2
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Q46337 | MSQNTSYRLPAEQSPAARIDRGEALVLTVDGKQLEAFRGDTVASAMLANGQRACGNSMYLDRPRGIFSAGVEEPNALVTVEARHEQDINESMLAATTVPVTANLSATLLRGLGVLDPSTDPAYYDHVHVHTDVLVVGAGPAGLAAAREASRSGARVLLLDERAEAGGSLRDAAGEQIDGQDAAAWIDATVAELAAAEETTHLQRTTVLGSYDANYVVAVQRRTVHLDGPSGAGVSRERIWHIRANQVVLATGAHERPIVFENNDRPGIMLAGAVRSYLNCYGVRAGSQIVVATTNDSAYPLVADLAASGGVVAVIDARTTVSAAAAEAVGAGVRVITGSVVVDTEANESGELSAVIVAELGEDRELGEPQRFEADVLAVAGGFNPVVHLHSQRQGKLVWDTSIHAFVPDAAVANQHLAGALTGLFDTASALSTGAAVGAAAATAAGFERIAQVPQALPVPAGETRPVWLVPSLNGDQATNYTTHFVDLQRDQTVSDVLRATGAGLESVEHIKRYTSISTANDQGKTSGVAAIGVIAAVLGIENPAEIGTTTFRAPYTPVAFAALAGRTRGELLDPARITPMHSWHLAQGAKFEDVGQWKRAWYFPQDGEDMDAAVYRECAAVRESVGMLDATTLGKIEIRGADAAEFLNRIYTNGYTKLKVGMARYGVMCKADGMVFDDGVTLRLAEDRFLMHTTTGGAAGVLDWLEEWLQTEWPELDVTCTSVTEQLATVAVVGPRSRDVVAKLVTGLDVSNDAFKFMSFQDVTLDSGIEARISRISFSGELAYEIAIPSWHGLRVWEDVYAAGQEFNITPYGTETMHVLRAEKGFIIVGQDTDGTVTPQDAGMEWVVSKLKDFVGKRSFSREDNLREDRKHLVSVLPVDTALRLAEGAALVADGAVETEGCTPMEGWVTSSYNSPALGRTFGLALIKNGRSRIGEVLKTPVNGQLVDVLVSDLVLFDPEGSRRDG | Function: Catalyzes the oxidative demethylation of sarcosine to yield glycine, hydrogen peroxide and 5,10-methylenetetrahydrofolate.
Catalytic Activity: H2O + O2 + sarcosine = formaldehyde + glycine + H2O2
Sequence Mass (Da): 102767
Sequence Length: 967
Subcellular Location: Cytoplasm
EC: 1.5.3.1
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Q08IS0 | MKKTVTAVALLCALSSTAIAPTFAADDDEAARLKAIEEYRKQIADGNPSDLLAMEGEELWRTPYGPKNQSLEQCDLGLGPGVVKGAAAKLPRYFPDTGKVEDLESRLMTCMERLQGVERQKVIDSPWRKGEKLRMDKIVAYIVTESNGEKIDVDMSHPKMKEMYELGKRMFFYRTGPFDFSCATCHGKDGQRIRLQELPNLTKHEGAAAGWGSWPAYRVSNSQFWTMQMRLNDCFRQQRTAEPIYGSDATIALSVYMAANGNGGVMLTPGIKR | Cofactor: Binds 1 heme group per subunit.
Function: C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.
PTM: Cysteine persulfide at Cys-234.
Catalytic Activity: 2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]
Sequence Mass (Da): 30473
Sequence Length: 273
Subcellular Location: Periplasm
EC: 2.8.5.2
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O33434 | MPRFTKTKGTLAATALGLALAGAAFADPVEDGLVIETDSGPVEIVTKTAPPAFLADTFDTIYSGWHFRDDSTRDLERDDFDNPAMVFVDRGLDKWNAAMGVNGESCASCHQGPESMAGLRAVMPRVDEHTGKLMIMEDYVNACVTERMGLEKWGVTSDNMKDMLSLISLQSRGMAVNVKIDGPAAPYWEHGKEIYYTRYGQLEMSCANCHEDNAGNMIRADHLSQGQINGFPTYRLKDSGMVTAQHRFVGCVRDTRAETFKAGSDDFKALELYVASRGNGLSVEGVSVRH | Cofactor: Binds 2 heme c groups covalently per subunit.
Function: C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.
PTM: Cysteine persulfide at Cys-251.
Catalytic Activity: 2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]
Sequence Mass (Da): 31748
Sequence Length: 290
Subcellular Location: Periplasm
EC: 2.8.5.2
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Q94BM7 | MKGSSESSSRGLNNTSGVSEFCTDGSKSLSHIDYVRSLLGSHKEANLGGLDDDSIVRALECEDVSLRQWLDNPDRSVDAFECFHVFRQIVEIVNAAHSQGIVVHNVRPSCFVMSSFNNVSFIESASCSDSGSDEDATTKSREIGSSRQEEILSERRSKQQEEVKKQPFPMKQILAMEMSWYTSHEEDNGSLCNCASDIYRLGVLLFELFCPVSSREEKSRTMSSLRHRVLPPQILLNWPKEASFCLWLLHPEPSCRPSMSELLQSEFINEPRENLEEREAAMELRDRIEEQELLLEFLFLIQQRKQEAADKLQDTISLLSSDIDQVVKRQLVLQQKGRDVRSFLASRKRIRQGAETTAAEEENDDNSIDEESKLDDTLESTLLESSRLMRNLKKLESVYFATRYRQIKAATAAEKPLARYYSALSCNGRSSEKSSMSQPSKDPINDSRQGGWIDPFLEGLCKYLSFSKLRVKADLKQGDLLNSSNLVCAIGFDRDGEFFATAGVNKKIKIFECESIIKDGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNFEGVVQVWDVARNQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICCVQFPSETGRSLAFGSADHKVYYYDLRNPKLPLCTMIGHHKTVSYVRFVDSSTLVSSSTDNTLKLWDLSMSISGINETPLHSFMGHTNVKNFVGLSVSDGYIATGSETNEVFVYHKAFPMPVLSYKFKTIDPVSELEVDDASQFISSVCWRGQSSTLVAANSTGNIKILEMV | Function: Repressor of photomorphogenesis in the light. Probably part of the COP1/SPA E3 ubiquitin-protein ligase complex.
Sequence Mass (Da): 89071
Sequence Length: 794
Domain: The protein kinase domain is predicted to be catalytically inactive. The DWD box is required for interaction with DDB1A (By similarity).
Subcellular Location: Nucleus
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Q86WD7 | MASYLYGVLFAVGLCAPIYCVSPANAPSAYPRPSSTKSTPASQVYSLNTDFAFRLYRRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNLTHTPESAIHQGFQHLVHSLTVPSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIAQARINSHVKKKTQGKVVDIIQGLDLLTAMVLVNHIFFKAKWEKPFHPEYTRKNFPFLVGEQVTVHVPMMHQKEQFAFGVDTELNCFVLQMDYKGDAVAFFVLPSKGKMRQLEQALSARTLRKWSHSLQKRWIEVFIPRFSISASYNLETILPKMGIQNVFDKNADFSGIAKRDSLQVSKATHKAVLDVSEEGTEATAATTTKFIVRSKDGPSYFTVSFNRTFLMMITNKATDGILFLGKVENPTKS | Function: Protease inhibitor that inhibits trypsin and trypsin-like serine proteases (in vitro). Inhibits plasmin and thrombin with lower efficiency (in vitro).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 46557
Sequence Length: 417
Subcellular Location: Secreted
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Q96EA4 | MEADIITNLRCRLKEAEEERLKAAQYGLQLVESQNELQNQLDKCRNEMMTMTESYEQEKYTLQREVELKSRMLESLSCECEAIKQQQKMHLEKLEEQLSRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATLLQMKGSQTEFEQQERLLAMLEQKNGEIKHLLGEIRNLEKFKNLYDSMESKPSVDSGTLEDNTYYTDLLQMKLDNLNKEIESTKGELSIQRMKALFESQRALDIERKLFANERCLQLSESENMKLRAKLDELKLKYEPEETVEVPVLKKRREVLPVDITTAKDACVNNSALGGEVYRLPPQKEETQSCPNSLEDNNLQLEKSVSIYTPVVSLSPHKNLPVDMQLKKEKKCVKLIGVPADAEALSERSGNTPNSPRLAAESKLQTEVKEGKETSSKLEKETCKKLHPILYVSSKSTPETQCPQQ | Function: Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. Also required for correct spindle orientation. Does not appear to be required for the removal of spindle assembly checkpoint (SAC) proteins from the kinetochore upon bipolar spindle attachment . Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track) . Plays a role in cell migration .
PTM: Monoubiquitinated with'Lys-48' linkage . Deubiquitinated by USP45 .
Sequence Mass (Da): 70172
Sequence Length: 605
Subcellular Location: Cytoplasm
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O48661 | MSSTQEASVTDLPVKRPREAEEDNNGGAMETENGGGEIKEPSCMSSIIPGWFSEISPMWPGEAHSLKVEKILFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSISNPKKVLVIGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQYFPNVAVGYEDPRVNLIIGDGVAFLKNAAEGTYDAVIVDSSDPIGPAKELFEKPFFESVNRALRPGGVVCTQAESLWLHMDIIEDIVSNCRDIFKGSVNYAWTSVPTYPSGVIGFMLCSSEGPQVDFKKPVSLIDTDESSIKSHCPLKYYNAEIHSAAFCLPSFAKKVIDSKAN | Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence Mass (Da): 37140
Sequence Length: 340
Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
EC: 2.5.1.16
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O48659 | MEEQGNNESAYISSILPGWFSEISPLWPGEAHSLKVEKILFQGKSDYQNVVVFQSSTYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLVIGGGDGGVLREVSRHSSVEQIDICEIDKMVIDVSKQFFPNVAIGYEDPRVKLHVGDGVAFLKNVPEGTYDAVIVDSSDPIGPAQELFEKPFFESVARALCPGGVVCTQAESIWLHMHIIEDIVSNCRQIFKGSVNYAWTTVPTYPSGVIGFMLCSTEGPAVDFKNPINPIDADDSHTKTRGPLKFYNSEIHSASFCLPSFAKRVIESNAK | Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence Mass (Da): 33917
Sequence Length: 308
Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
EC: 2.5.1.16
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Q9ZTR0 | MAAESTVELESSMKEHRDDDEKSNGFSVSAVSMDVEGGDKDPSGNGVSSVIPGWFSEISPMWPGEAHSLKIEKILFQGKSEYQKVMVFQSSTYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLVIGGGDGGVLREVARHSSIEKIDICEIDNMVVEVSKQFFPEVAVGFNDPRVTLRIGDGVAFLKAAPEGTYDAVIVDSSDPIGPAQELFEKPFFQSVARALRPGGVMCTQAESIWLHMDIIEDIVSNCRHIFKGSVNYAWTTVPTYPSGMIGFMLCSTEGPLVDFKHPVNPIDQKDCQKSVRPLKFYNSEIHTAAFCLPSFAKRKIGSKET | Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence Mass (Da): 37590
Sequence Length: 342
Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
EC: 2.5.1.16
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Q5MJ70 | MRHNQMCCETPPTVTVYVKSGSNRSHQPKKPITLKRPICKDNWQAFEKNTHNNNKSKRPKGPCLVIQRQDMTAFFKLFDDDLIQDFLWMDCCCKIADKYLLAMTFVYFKRAKFTISEHTRINFFIALYLANTVEEDEEETKYEIFPWALGKNWRKLFPNFLKLRDQLWDRIDYRAIVSRRCCEEVMAIAPTHYIWQRERSVHHSGAVRNYNRDEVQLPRGPSATPVDCSLCGKKRRYVRLGLSSSSSLSSHTAGVTEKHSQDSYNSLSMDIIGDPSQAYTGSEVVNDHQSNKGKKTNFLKKDKSMEWFTGSEE | Function: Regulates the G1/S phase transition of the cell cycle by binding and activating CDK1 and CDK2 . Contributes to CDK2 activation without promoting CDK2 phosphorylation, by inducing a conformation change of the CDK2 T-loop that obstructs the substrate-binding cleft prior to kinase activation . Mediates cell survival during the DNA damage process through activation of CDK2 .
Sequence Mass (Da): 36463
Sequence Length: 313
Domain: The C-terminus is required for CDK2-activation, but not CDK2-binding.
Subcellular Location: Nucleus
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Q5IBH7 | MRHNQMYCETPPTVTIHVKSGSNRSHQTRKPISLKRPILKDSWEASENNAQNNKSKRPRGPCLIIQRQEMTAFFKLFDDDLIQDFLWMDCCCKIADKYLLAMTFVYFKRAKFTINEHTRINFFIALYLANTVEEDEEEAKYEIFPWALGKNWRKLFPNFLKLRDQLWDRIDYRAIVSRRCCEEVMAIAPTHYIWQRERSVHHSGAVRNYNRDEVHLPRGPSATPVDCSLCGKKGRYVRLGLSSSSSSSSDTGELMEKDSQELHSAFSVDTAGDPPHTYSQVANDHQSNKENETNFVKKNKSVEWFAESEE | Function: Regulates the G1/S phase transition of the cell cycle by binding and activating CDK1 and CDK2 . Contributes to CDK2 activation without promoting CDK2 phosphorylation, by inducing a conformation change of the CDK2 T-loop that obstructs the substrate-binding cleft prior to kinase activation. Interferes with CDKN1B-mediated inhibition of CDK2. Mediates cell survival during the DNA damage process through activation of CDK2 (By similarity).
Sequence Mass (Da): 36115
Sequence Length: 310
Domain: The C-terminus is required for CDK2-activation, but not CDK2-binding.
Subcellular Location: Nucleus
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P0C0J1 | MNKKKLGVRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRGDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP | Function: Cysteine protease that acts as a key streptococcal virulence factor by cleaving host proteins involved in immune response . Triggers inflammation by mediating cleavage of host proteins, which can both promote host pathogenesis by triggering sterile inflammation and/or restrict streptococcal infection, depending on host immune statue and infection site . Cleaves host gasdermin-A (GSDMA) in epithelial cells, promoting GSDMA activation and formation of gasdermin pores, triggering pyroptosis . Pyroptosis triggers the elimination of the infected skin cell, depriving the pathogen of its protective niche, while inducing an inflammatory response . This ultimately prevents bacterial penetration of the epithelial barrier and a subsequent systemic dissemination of the pathogen . Also mediates cleavage of the cytokine precursor interleukin-1 beta (IL1B) to its mature form, resulting in inflammation and septic shock . SpeB-mediated maturation of IL1B plays a dual role depending on infection site: while IL1B inflammatory response prevents bacterial growth during invasive skin infections, it promotes streptococcal infection of the nasopharynx by disrupting colonization resistance mediated by the microbiota . Inhibits host autophagy be catalyzing cleavage and inactivation of key autophagy factors, such as CALCOCO2, NBR1 and SQSTM1 . Cleaves and inhibits a number of complement factors, such as C2, C3-beta chain of C3, C4, C5 or SERPING1, thereby promoting evasion of host immunity . May also impair adaptive immunity by catalyzing cleavage and degradation of host immunoglobulins to promote immune system evasion; the relevance of this activity is however unsure in vivo . Catalyzes maturation and release of the peptide hormone bradykinin from the precursor Kininogen-1 (KNG1) to produce hypotension during septic shock . Also involved in bacterial translocation across the host epithelial barrier by mediating cleavage and degradation of host epithelial junction proteins, such as CDH1 and OCLN . Additionally, has been involved in degradation of fibronectin and vitronectin, two host extracellular matrix proteins involved in tissue integrity . Also able to catalyze cleavage and degradation of streptococcal proteins, such as C5a peptidase, EndoS or SmeZ . Degradation of streptococcal proteins is however strictly regulated to preserve integrity of other virulence factors .
PTM: The mature protease is derived from the precursor sequence by cleavage, either in cis via an autocatalytic mechanism, or in trans by mature SpeB or host proteases (trypsin, plasmin or subtilisin) . Maturation can involve a number of protein cleavage intermediates . Mature SpeB probably plays the most important role in protein maturation in physiological conditions .
Catalytic Activity: Preferential cleavage with hydrophobic residues at P2, P1 and P1'.
Sequence Mass (Da): 43130
Sequence Length: 398
Domain: The C-terminal active site loop is required for the recognition and recruitment of substrates and release of hydrolyzed products.
Subcellular Location: Secreted
EC: 3.4.22.10
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A6TS03 | MDIKSFEKIQLYGFNNLTKTLSFNIYDICYAKAPEQSKAYIAYIDEQYNAERLTKILSNVADITGANILSISKQDYDPQGASVTMLVAEEMTVPTLTPESLTGESPGPLPGNKPSPGSIVTHLDKSHVTVHTYPETHPLDGISTFRADIDVSTCGHISPIKALNYLIHSFESDIVTIDYRVRGFTRDINGQKYFIDHDINSIQNYIAKDILNLYHAIDVNVYQENIFHTKMTLKDFKLNNYLFGVSEEELSDHESASIKDQLRDEMQEIFYGRNVTKV | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 31458
Sequence Length: 278
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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A3PFH4 | MTNIQTWIDEYHKGSRFGLNGDVLIKQKSQYQEIIVIENEYYGRALMLDGCWMTSLKDEKYYHECLVHPALSSIDEKSNVLIIGGGDGGTVRECVKYAQISKIDLVEIDEEVIKISKKFLKEIGGEAWHDKRLEIHVDDGVKWVKKTRDNYYDVIFIDCSDPSEFSNLLFSDSFYKECKRILTPKGILATQSESPESFKNIHINILKTLKNIFKVSETMYSFVPIYPSGIWSWTFASSEDLNLSKQNYDEILKIEKGCEIWNLNFQNAAFKMMPNKIIKELDS | Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence Mass (Da): 32761
Sequence Length: 283
Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
Subcellular Location: Cytoplasm
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Q8ZXM4 | MSKVPGPIVLMEPLSGKTSLIIKINAIHVSKRSKYQGILIVDTDDYGRTLVLDDYIQSSYYDEIYYHESLVHPAVTTHPRPSDVLILGGGEGATLREVLKHNTVKRAVMVDIDGDVVELSKKYLPQMHQGAFDDPRSEVRIEDGFVYVENALKRGEKFDVVIMDLTDPYSSDIAKQLYTPEFFGKVKRLLREDGIVVTQAGNSFYFPEAYDYVLQGVKGNFPIIAEYSVWIPSFGYAVNFVLGSLKHDPHSLSAEEVDKRLSERGVRAEFYSGKTHIALMNMPVIKKILRV | Function: Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to norspermidine and 1,3-diaminopropane to yield norspermine, and to spermidine to yield thermospermine. It can also synthesize thermospermine from putrescine (1,4-diaminobutane) and caldopentamine from norspermine with a very low activity. The biosynthesis of caldohexamine and caldoheptamine from caldopentamine has been also observed.
Catalytic Activity: norspermidine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + norspermine + S-methyl-5'-thioadenosine
Sequence Mass (Da): 32806
Sequence Length: 291
Subcellular Location: Cytoplasm
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O66615 | MAKTLGLHILADLYGVDADKIDRVEDIRELLEGAVKYANLTKISSHYYQFQPHGATGVVLLAESHISIHTWPEHGLATVDVYTCGDPSKAYRAMDYIITQLNPKRIDKQVHERGIVEEESNQSEAEKLRSILLQV | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 15200
Sequence Length: 135
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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O28663 | MIVGRHIIAELYGVKEELIAKEEVVRSIVEEVVDKAELTKVGSVYKQFNPHGVTGIVLIAESHVSIHTWPEYGLVNLDIFTCGDTSKVEKAFKLFLEKFKPESYRHYVLDRG | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 12733
Sequence Length: 112
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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O34426 | METMGRHVISELWGCDFDKLNDMDFIEKTFVNAALKSGAEVREVAFHKFAPQGVSGVVIISESHLTIHSFPEHGYASIDVYTCGDLDPNVAADYIAEALHADTRENIEIPRGMGPVQIKQAQAKVL | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 13873
Sequence Length: 126
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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C0ZGF5 | MEYSTFGRHVAVDTWGVQFDLLNDAEFLKKEMIEAAEACGATVLSVQAKQFSPQGATVLVLLSESHLSIHTYPERGFAALDCYTCGETVDPQIAIDYLVSVLKPEKTYAKKLVRGLGELQVVEPEMKLVEAAK | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 14638
Sequence Length: 133
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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Q8RA74 | MNALGRHILAEVYGCDSRILDDVEMIEDIMVQAAIATGAEVREVAFHKFNPQGVSGVVVISESHLTIHTWPELGYAAVDVFTCGDHVNPWDGVNYIARMLKAENMTATEVKRGVFEKPVKVANF | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 13674
Sequence Length: 124
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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Q3AB53 | MNALGRHVIAELYGCGFDVLNDVKRVEEIMVRSALEAGAEIREVAFHKFSPQGVSGVVVISESHLAIHTWPELGYAAVDVFTCGDTVDPWDATNYLAKEFGAKYMTAKETKRGVMVEEFAESQAVNL | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 13952
Sequence Length: 127
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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Q8L7L1 | MDRQPERENDELPSPAIISDRVLVNGVVTPLTLTAEGELRSTESGRRKSTLAKEILSFVVEGNKVRVKTLVEKGGGICCRGSAGDYARNDFVFEPLSDESRKLWSDKFHQHLVSLGRPKKLLVFVNPFGGKKTARKIFQEEVKPLFEDANIQLEIQETKYQLHAKEIVRSMDVSKYDGIVCVSGDGILVEVVNGLLEREDWKTAIKLPIGMVPAGSGNGMIKSLLEPVGLPCSATSATISIIRGRTRSLDVATISQGTTKFFSVLMLAWGLVADIDIESEKFRWMGSARFDIYGLQRIICLRQYHGRILFVPAPGFESYGQRASCSIDKEPSGSDKTLVYQGPDSKLENLDWREMKGPFVSVWLHNVPWGAENTLAAPDAKFSDGFLDLIVMKDCPKLALLSLMTKLSDGTHVQSPYASYLKVKAFVLEPGARIDEPDKEGIIDSDGEVLARGRKSYKCDQKALMSYDKLQISVDQGLATLFSPE | Function: Involved in the production of sphingolipid metabolites. Phosphorylates sphingosine and various sphingoid long-chain base (LCB) products, such as phytosphingosine (PHS, 4-hydroxysphinganine), 4-hydroxy-8-sphingenine, 4,8-sphingadienine, D-erythro-dihydrosphingosine and D,L-threo-dihydrosphingosine. Is required for abscisic acid (ABA) signaling that mediates stomatal closure, inhibition of seed germination and root elongation. May function upstream of PLDALPHA1 and phosphatidic acid (PA) in an amplification response to ABA that mediates stomatal closure.
Catalytic Activity: a sphingoid base + ATP = a sphingoid 1-phosphate + ADP + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53699
Sequence Length: 485
Subcellular Location: Vacuole membrane
EC: 2.7.1.91
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Q9Y657 | MKTPFGKTPGQRSRADAGHAGVSANMMKKRTSHKKHRSSVGPSKPVSQPRRNIVGCRIQHGWKEGNGPVTQWKGTVLDQVPVNPSLYLIKYDGFDCVYGLELNKDERVSALEVLPDRVATSRISDAHLADTMIGKAVEHMFETEDGSKDEWRGMVLARAPVMNTWFYITYEKDPVLYMYQLLDDYKEGDLRIMPDSNDSPPAEREPGEVVDSLVGKQVEYAKEDGSKRTGMVIHQVEAKPSVYFIKFDDDFHIYVYDLVKTS | Function: Chromatin reader that specifically recognizes and binds histone H3 both trimethylated at 'Lys-4' and asymmetrically dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator of Wnt signaling pathway downstream of PRMT2. In case of cancer, promotes cell cancer proliferation via activation of the Wnt signaling pathway . Overexpression induces metaphase arrest and chromosomal instability. Localizes to active rDNA loci and promotes the expression of rRNA genes . May play a role in cell-cycle regulation during the transition from gamete to embryo. Involved in oocyte meiotic resumption, a process that takes place before ovulation to resume meiosis of oocytes blocked in prophase I: may act by regulating maternal transcripts to control meiotic resumption.
PTM: Phosphorylated during oocyte meiotic maturation.
Sequence Mass (Da): 29601
Sequence Length: 262
Domain: The 3 tudor-like domains (also named Spin/Ssty repeats) specifically recognize and bind methylated histones . H3K4me3 and H3R8me2a are recognized by tudor-like domains 2 and 1, respectively .
Subcellular Location: Nucleus
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Q75GR5 | MSGLYSPGFSPARNLSPQIRSNPTDVDSQYLAELLAEHQKLGPFMQVLPICSKLLSQEIMRVSSIVHNHGFGDFDRHRFRSPSPMSSPNPRSNRSGNGFSPWNGLHQERLGFPQGTSMDWQGAPPSPSSHVVKKILRLDVPVDSYPNFNFVGRILGPRGNSLKRVEASTGCRVFIRGKGSIKDPGKEDKLRGKPGYEHLSDPLHILIEAEFPASIIDARLRHAQEVIEELLKPVDESQDFYKRQQLRELAMLNSTLREDSPHPGSVSPFSNGGMKRAKTGQ | Function: Involved in flowering time control. Binds DNA and RNA in vitro.
PTM: Ubiquitinated by SPL11. Ubiquitination probably leads to its subsequent degradation, thus negatively regulating flowering time control.
Sequence Mass (Da): 31285
Sequence Length: 281
Subcellular Location: Nucleus
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F6UH96 | MQLSVVDPTWELLDPNPDIRALFLEFNDTFFWGQLSGIEVKWSARMTLCAGVCSYEGRGGLCSIRLSEPLLKLRPRKDLVQTLLHEMIHALLFVTHNNKDHDSHGPEFCKHMERINKRTGANISVYHNFHDEVDEYRKHWWLCNGPCQKRKPYFGYVKRAMNRAPSSLDPWWADHQRTCGGEFVKIKEPENYSQKRKRNNDPTKSELGNSSHVKINKGKSNGVDIRTVIPFSGTGYKLFEPSKSDAQLKIQNDNPTKDKAVMHHTPPSTNQTDSTFLSRKIVSAKKISVANTKVFINLNGSPIKLPSSSNNKSHQDSSKQKSVLHFFKTQKDNSIDLTSSSQSFPSTSQGPNREETEHFYKKLQMDDKESKDTFIIHSLNKTNVSDSLNNKSCAGPAATINSGLNHTKVCCPVCGTEIFESKINDHLDTCLQNYNT | Function: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity (By similarity). DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde. Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis. Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as top1, top2a, histones H3 and H4 (By similarity). Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs. SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs (By similarity). May also act as a 'reader' of ubiquitinated pcna: facilitates chromatin association of rad18 and is required for efficient pcna monoubiquitination, promoting a feed-forward loop to enhance pcna ubiquitination and translesion DNA synthesis. Acts as a regulator of translesion DNA synthesis by recruiting vcp/p97 to sites of DNA damage (By similarity).
PTM: Autocatalytically cleaved in response to double-stranded DNA-binding: autocatalytic cleavage takes place in trans and leads to inactivation.
Sequence Mass (Da): 49444
Sequence Length: 436
Domain: The UBZ4-type zinc fingers mediate binding to 'Lys-48'- and 'Lys-63'-linked polyubiquitin.
Subcellular Location: Nucleus
EC: 3.4.24.-
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Q59072 | MDKYKNLTRSLTREFINLNPIQRGGILPKEAKKAVYEYWDGYSVCDYCHGRLDEVTCPPIKDFLEDIAKFLNMDCARPTHGAREGKFIVMHAICKEGDYVVLDKNAHYTSYVAAERAKLNVAEVGYEEEYPTYKINLEGYKEVIDNLEDKGKNVGLILLTHVDGEYGNLNDAKKVGKIAKEKGIPFLLNCAYTVGRMPVNGKEVKADFIVASGHKSMAASAPCGILAFSEEFSDKITKTSEKFPVKEIEMLGCTSRGLPIVTLMASFPHVVERVKKWDEELKKTRYVVDELEKIGFKQLGIKPKEHDLIKFETPVLDEIAKKDKRRGFFFYDELKKRGIGGIRAGVTKEIKMSVYGLEWEQVEYVVNAIKEIVESCK | Function: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)).
Catalytic Activity: H(+) + hydrogen sulfide + O-phospho-L-seryl-tRNA(Cys) = L-cysteinyl-tRNA(Cys) + phosphate
Sequence Mass (Da): 42764
Sequence Length: 377
EC: 2.5.1.73
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Q8TYR3 | MNLDRYRNIVRETERKYINVNPIQRGGVLTPEARKALLEFGDGYSVCDFCEGLLHEIEKPPIRQFHEDLAEFLGMDVVRITAGARYAKEAVMSALCEEGDVVVADSLAHYTTFVAAEKAGATVREVPNTGHPEYKVKVDEYARVIDEVEDERGDPPALALLTHVDSEYGNLADAEKFVKICRKKGVPALLNCAYTMGRMDLSNLSPKPDFMVGSGHKGMAACAPCGVLAMREEWEEEVLRGSSLRGDVSGREWPHKEVEMLGCTVMGAPIVTMMASFPHVVERVKRWKEEVRKTRWFVKEMERIEGVRQLGERPKRHDLVKFETPGFHEVAEDHPRRGYFLYEELKKRGVIGIQPGQTETIKASVYGLTDEQVEHVVRAFHEIAEEYGLEVS | Function: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)).
Catalytic Activity: H(+) + hydrogen sulfide + O-phospho-L-seryl-tRNA(Cys) = L-cysteinyl-tRNA(Cys) + phosphate
Sequence Mass (Da): 44252
Sequence Length: 392
EC: 2.5.1.73
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Q94BN2 | MEGDVGIGLVCQNTMDGKASNGNGLEKTVPSCCLKAMACVPEDDAKCHSTVVSGWFSEPHPRSGKKGGKAVYFNNPMWPGEAHSLKVEKVLFKDKSDFQEVLVFESATYGKVLVLDGIVQLTEKDECAYQEMIAHLPLCSISSPKNVLVVGGGDGGVLREISRHSSVEVIDICEIDKMVIDVSKKFFPELAVGFDDPRVQLHIGDAAEFLRKSPEGKYDAIIVDSSDPVGPALALVEKPFFETLARALKPGGVLCNMAESMWLHTHLIEDMISICRQTFKSVHYAWSSVPTYPSGVIGFVLCSTEGPAVDFKNPINPIEKLDGAMTHKRELKFYNSDMHRAAFALPTFLRREVASLLAS | Catalytic Activity: S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) + S-methyl-5'-thioadenosine + spermine
Sequence Mass (Da): 39239
Sequence Length: 359
Pathway: Amine and polyamine biosynthesis; spermine biosynthesis; spermine from spermidine: step 1/1.
EC: 2.5.1.22
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Q3SZA5 | MAAARHSTLDFMLGAKADGETILKGLQSIFQEQGMTESVHTWQDHGYLATYINKNGSFANLRIYPHGLVLLDLQSYDGDAQGKEVDSLLNKVEERMKELSQDSTERVKRLPPIVRGGAIDRYWPTADGRLVEYDIDKVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRAIMGSGKEDYSGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRKTCGDVLDNLKGDCYQVLIEDCIPVLKRYAKEGREFDYVINDLTAVPISTSPEEDSTWEFLRLILDLSMKVLKQDGKYFTQGNCVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTVWKKAKP | Function: Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM).
Catalytic Activity: S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) + S-methyl-5'-thioadenosine + spermine
Sequence Mass (Da): 41224
Sequence Length: 365
Domain: Composed of 3 domains: the N-terminal domain has structural similarity to S-adenosylmethionine decarboxylase, the central domain is made up of four beta strands and the C-terminal domain is similar in structure to spermidine synthase. The N- and C-terminal domains are both required for activity.
Pathway: Amine and polyamine biosynthesis; spermine biosynthesis; spermine from spermidine: step 1/1.
EC: 2.5.1.22
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P52788 | MAAARHSTLDFMLGAKADGETILKGLQSIFQEQGMAESVHTWQDHGYLATYTNKNGSFANLRIYPHGLVLLDLQSYDGDAQGKEEIDSILNKVEERMKELSQDSTGRVKRLPPIVRGGAIDRYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRAIMGSGKEDYTGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRKTCGDVLDNLKGDCYQVLIEDCIPVLKRYAKEGREFDYVINDLTAVPISTSPEEDSTWEFLRLILDLSMKVLKQDGKYFTQGNCVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTVWKKAKP | Function: Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM).
Catalytic Activity: S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) + S-methyl-5'-thioadenosine + spermine
Sequence Mass (Da): 41268
Sequence Length: 366
Domain: Composed of 3 domains: the N-terminal domain has structural similarity to S-adenosylmethionine decarboxylase, the central domain is made up of four beta strands and the C-terminal domain is similar in structure to spermidine synthase. The N- and C-terminal domains are both required for activity.
Pathway: Amine and polyamine biosynthesis; spermine biosynthesis; spermine from spermidine: step 1/1.
EC: 2.5.1.22
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P97355 | MAAARHSTLDFKLGAKADGEAILKGLQSIFQEQGMTESVHTWQDHGYLATYTNKNGSFANLRIYPHGLVLLDLQSYDSDVQGKQETDSLLNKIEEKMKELSQDSTGRVKRLPPIVRGGAIDRYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRAIMGSGKEDYTGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRRTCGDVLDNLRGDCYQVLIEDCIPVLKMYAKEGREFDYVINDLTAVPISTSPEEDSTWDFLRLILDLSMKVLKQDGKYFTQGNCVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTVWKKAKP | Function: Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM) . Required for normal viability, growth and fertility .
Catalytic Activity: S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) + S-methyl-5'-thioadenosine + spermine
Sequence Mass (Da): 41313
Sequence Length: 366
Domain: Composed of 3 domains: the N-terminal domain has structural similarity to S-adenosylmethionine decarboxylase, the central domain is made up of four beta strands and the C-terminal domain is similar in structure to spermidine synthase. The N- and C-terminal domains are both required for activity.
Pathway: Amine and polyamine biosynthesis; spermine biosynthesis; spermine from spermidine: step 1/1.
EC: 2.5.1.22
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Q12455 | MVNNSQHPYIKDGWFREINDKSFPGQAFTMTVDSILYEARSEFQDILIFRNKVYGTVLVLDGIVQCTEFDEFAYQEMITHIAMFAHSNPKRVLIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKFLPTLSNGAFDDERLDLKLCDGFKFLQDIGASDVHKKFDVIITDSSDPEGPAEAFFQERYFELLKDALNPNGVVIMQSSENFWLNLKYLHDLKNTAKKVFPNTEYCYTMVPTYTSGQLGLIVCSNNANIPLNIPQRKISEQEQGKLKYYNPQIHSSAFVLPTWADKVINE | Catalytic Activity: S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) + S-methyl-5'-thioadenosine + spermine
Sequence Mass (Da): 34091
Sequence Length: 300
Pathway: Amine and polyamine biosynthesis; spermine biosynthesis; spermine from spermidine: step 1/1.
EC: 2.5.1.22
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Q9PTL1 | NPCSCSQSHCCSRYLCMGAMSLFLPCLLCYPPAKGCLKLCRGCYDRVNRPGCRCKNSNTVYCKLESCPSRGQGKPS | Function: Inhibits fibroblast growth factor (FGF)-induced retinal lens fiber differentiation (By similarity). Inhibits TGFB-induced epithelial-to-mesenchymal transition in lens epithelial cells (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 8349
Sequence Length: 76
Domain: The Cys-rich domain is responsible for the localization of the protein to the membrane ruffles.
Subcellular Location: Cytoplasm
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Q9Y6N5 | MVPLVAVVSGPRAQLFACLLRLGTQQVGPLQLHTGASHAARNHYEVLVLGGGSGGITMAARMKRKVGAENVAIVEPSERHFYQPIWTLVGAGAKQLSSSGRPTASVIPSGVEWIKARVTELNPDKNCIHTDDDEKISYRYLIIALGIQLDYEKIKGLPEGFAHPKIGSNYSVKTVEKTWKALQDFKEGNAIFTFPNTPVKCAGAPQKIMYLSEAYFRKTGKRSKANIIFNTSLGAIFGVKKYADALQEIIQERNLTVNYKKNLIEVRADKQEAVFENLDKPGETQVISYEMLHVTPPMSPPDVLKTSPVADAAGWVDVDKETLQHRRYPNVFGIGDCTNLPTSKTAAAVAAQSGILDRTISVIMKNQTPTKKYDGYTSCPLVTGYNRVILAEFDYKAEPLETFPFDQSKERLSMYLMKADLMPFLYWNMMLRGYWGGPAFLRKLFHLGMS | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the oxidation of hydrogen sulfide with the help of a quinone, such as ubiquinone-10, giving rise to thiosulfate and ultimately to sulfane (molecular sulfur) atoms. Requires an additional electron acceptor; can use sulfite, sulfide or cyanide (in vitro) . It is believed the in vivo electron acceptor is glutathione .
Catalytic Activity: 2 H(+) + hydrogen sulfide + sulfite + ubiquinone-10 = thiosulfate + ubiquinol-10
Sequence Mass (Da): 49961
Sequence Length: 450
Subcellular Location: Mitochondrion
EC: 1.8.5.8
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Q9R112 | MAPLVTVVSSPRARLFACFLRLGTQQAGPLQLHTGACCTAKNHYEVLVLGGGAGGITMATRMKRRVGAENVAIVEPSERHFYQPIWTLVGAGAKELSLSVRSTLSVIPSGVQWIQDRVAELNPDENCIRTDSGKEISYRYLIIALGIQLDYEKIKGLPEGFAYPKIGSNYSVKTVEKTWKALQGFKEGNALFTFPNTPVKCAGAPQKIMYLSEAYFRKTGKRPKANIIFNTALGTIFGVKKYADALQEIIRERDVSVNYKHNLIEVRPDKQEAVFEILDKPGETHVIPYEMLHVTPPMSAPDVLKRSPVADSAGWVDVDKETLQHKKYPNVFGIGDCTNLPTSKTAAAVAAQSGILDRTMCLIMKNQRPIKKYDGYTSCPLVTGYNRVILAEFDYTAQPLETFPFDQSKERITMYLMKADMMPFLYWNMMLRGYWGGPAFLRKLFHLGMN | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the oxidation of hydrogen sulfide with the help of a quinone, such as ubiquinone-10, giving rise to thiosulfate and ultimately to sulfane (molecular sulfur) atoms. Requires an additional electron acceptor; can use sulfite, sulfide or cyanide (in vitro). It is believed the in vivo electron acceptor is glutathione.
Catalytic Activity: 2 H(+) + hydrogen sulfide + sulfite + ubiquinone-10 = thiosulfate + ubiquinol-10
Sequence Mass (Da): 50282
Sequence Length: 450
Subcellular Location: Mitochondrion
EC: 1.8.5.8
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Q7ZAG8 | MTKVLVLGGRFGALTAAYTLKRLVGSKADVKVINKSRFSYFRPALPHVAIGVRDVDELKVDLSEALPEKGIQFQEGTVEKIDAKSSMVYYTKPDGSMAEEEYDYVIVGIGAHLATELVKGWDKYGYSVCEPEFATKLREKLESFQGGNIAIGSGPFYQGHNPKPKVPENFVPNADSACEGPVFEMSLMLHGYFKKKGMLDKVHVTVFSPGEYLSDLSPNSRKAVASIYNQLGIKLVHNFKIKEIREHEIVDEKGNTIPADITILLPPYTGNPALKNSTPDLVDDGGFIPTDLNMVSIKYDNVYAVGDANSMTVPKLGYLAVMTGRIAAQHLANRLGVPTKVDKYYPTIMCVADNPYEGYAVSVKDDTWYGGTVSIADPAAVNHLKKELFTKYYMWTKGDMALEKFLASW | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the oxidation of sulfides, such as hydrogen sulfide, with the help of a quinone. Has the highest activity with caldariella quinone and decylubiquinone, and lower activity with naphtoquinones. Consecutive reaction cycles lead to the accumulation of a polysulfide product on the active site Cys residues; these products are released when they exceed a critical length, typically as cyclooctasulfur.
Catalytic Activity: n a quinone + n H(+) + n hydrogen sulfide = n a quinol + n sulfur
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 45152
Sequence Length: 409
Subcellular Location: Membrane
EC: 1.8.5.4
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B7JBP8 | MAHVVILGAGTGGMPAAYEMKEALGSGHEVTLISANDYFQFVPSNPWVGVGWKERDDIAFPIRHYVERKGIHFIAQSAEQIDAEAQNITLADGNTVHYDYLMIATGPKLAFENVPGSDPHEGPVQSICTVDHAERAFAEYQALLREPGPIVIGAMAGASCFGPAYEYAMIVASDLKKRGMRDKIPSFTFITSEPYIGHLGIQGVGDSKGILTKGLKEEGIEAYTNCKVTKVEDNKMYVTQVDEKGETIKEMVLPVKFGMMIPAFKGVPAVAGVEGLCNPGGFVLVDEHQRSKKYANIFAAGIAIAIPPVETTPVPTGAPKTGYMIESMVSAAVHNIKADLEGRKGEQTMGTWNAVCFADMGDRGAAFIALPQLKPRKVDVFAYGRWVHLAKVAFEKYFIRKMKMGVSEPFYEKVLFKMMGITRLKEEDTHRKAS | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone. Consecutive reaction cycles lead to the accumulation of a polysulfide product on the active site Cys residues; these products are released when they exceed a critical length, typically as cyclooctasulfur.
Catalytic Activity: n a quinone + n H(+) + n hydrogen sulfide = n a quinol + n sulfur
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 47406
Sequence Length: 434
Subcellular Location: Membrane
EC: 1.8.5.4
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O67931 | MAKHVVVIGGGVGGIATAYNLRNLMPDLKITLISDRPYFGFTPAFPHLAMGWRKFEDISVPLAPLLPKFNIEFINEKAESIDPDANTVTTQSGKKIEYDYLVIATGPKLVFGAEGQEENSTSICTAEHALETQKKLQELYANPGPVVIGAIPGVSCFGPAYEFALMLHYELKKRGIRYKVPMTFITSEPYLGHFGVGGIGASKRLVEDLFAERNIDWIANVAVKAIEPDKVIYEDLNGNTHEVPAKFTMFMPSFQGPEVVASAGDKVANPANKMVIVNRCFQNPTYKNIFGVGVVTAIPPIEKTPIPTGVPKTGMMIEQMAMAVAHNIVNDIRNNPDKYAPRLSAICIADFGEDAGFFFADPVIPPRERVITKMGKWAHYFKTAFEKYFLWKVRNGNIAPSFEEKVLEIFLKVHPIELCKDCEGAPGSRC | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone. Consecutive reaction cycles lead to the accumulation of a polysulfide product on the active site Cys residues; these products are released when they exceed a critical length, typically as cyclooctasulfur.
Catalytic Activity: n a quinone + n H(+) + n hydrogen sulfide = n a quinol + n sulfur
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 47449
Sequence Length: 430
Subcellular Location: Membrane
EC: 1.8.5.4
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O48666 | MGSLGAILKHPEDFYPLLKLKFAARHAEKQIPPEPHWAFCYSMLHKVSRSFGLVIQQLGPQLRDAVCIFYLVLRALDTVEDDTSIPTEVKVPILMAFHRHIYDKDWHFSCGTKEYKVLMDEFHHVSNAFLELGSGYQEAIEDITMRMGAGMAKFICKEVETINDYDEYCHYVAGLVGLGLSKLFHASGAEDLATDSLSNSMGLFLQKTNIIRDYLEDINEIPKSRMFWPRQIWSKYVDKLEDLKYEENSAKAVQCLNDMVTDALVHAEDCLKYMSDLRGPAIFRFCAIPQIMAIGTLALCFNNTQVFRGVVKMRRGLTAKVIDQTKTMSDVYGAFFDFSCLLKSKVDNNDPNATKTLSRLEAIQKTCKESGTLSKRKSYIIESESGHNSALIAIIFIILAILYAYLSSNLLLNKQ | Function: Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways . Catalyzes the biosynthesis of squalene .
Catalytic Activity: 2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47056
Sequence Length: 415
Pathway: Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.5.1.21
|
P84109 | LNRDDDSDLHSPRYSFSEDTKCDDGWFVGTSRRTK | Function: Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin-stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions (By similarity).
PTM: O-glycosylated.
Sequence Mass (Da): 4107
Sequence Length: 35
Subcellular Location: Cell junction
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G5EE56 | MGCLFSKERRSGGSDMGVSERIDVSRFQTPQQQTVFHVNNGGNEGTISQLNGTSDGMMGNGRGGGGGGGAQERETLVALYPYDSRADGDLSFQKGDAMYLLDHSNCDWWYVRHQRTGQTGYVPRNFVAKQQTIESEEWYAGKIPRNRAERLVLSSHLPKGTFLIREREADTREFALTIRDTDDQRNGGTVKHYKIKRLDHDQGYFITTRRTFRSLQELVRYYSDVPDGLCCQLTFPAPRLAPTRPDLSHDTQQNWEIPRNQLHLKRKLGDGNFGEVWYGKWRGIVEVAIKTMKPGTMSPEAFLQEAQIMKQCDHPNLVKLYAVCTREEPFYIITEYMINGSLLQYLRTDGSTLGIQALVDMAAQIANGMMYLEERKLVHRDLAARNVLVGDKISGVPVVKVADFGLARKLMEEDIYEARTGAKFPIKWTAPEAATCGNFTVKSDVWSYGILLYEIMTKGQVPYPGMHNREVVEQVELGYRMPMPRGCPEQIYEEVLLKCWDKTPDRRPTFDTLYHFFDDYFVSTQPNYAPPSA | Function: Non-receptor tyrosine-protein kinase which plays a role in endoderm development by controlling spindle orientation in EMS blastomere, probably downstream of receptor mes-1. Also involved in embryonic body morphogenesis, especially in the formation of the pharynx and the intestine . May be dispensable for pharyngeal muscle organization in the adult . Probably phosphorylates netrin receptor unc-5, to regulate distal tip cell (DTC) migration during gonad development and in axon repulsion . Plays a role in the migration of the QR neuroblast, a precursor of the AVM neuron, and in the migration of the axon cone of AVM, ALM, CAN and PVM neurons . May act downstream of migratory protein mig-13 to control AVM neuron migration . Probably downstream of integrin ina-1/pat-3, plays a role in the clearance of apoptotic cells during mid-embryogenesis . Phosphorylates ced-1 at 'Tyr-1019' which promotes ced-1 proteasomal degradation, maintaining appropriate ced-1 levels for apoptotic cell clearance .
PTM: May be phosphorylated on Tyr-528 by csk-1.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 60661
Sequence Length: 533
Subcellular Location: Cell membrane
EC: 2.7.10.2
|
Q03707 | MNSDLEYLEDGFDPNSMKVATLRRILVENNVDFPSNARKNALVGLFDEKVKPQIPQLRKMYLNVRPSDEGIVKMDRPSSSPSIASPRRSRRARREKSASPMAKQFKKNRILDDVSNDDDDDDDDDDDNDKKDDPLIVPSGTDTDEVDDEEDDVITSSSNKSDTNDFQQNSDTRKKRKDPDSDDWSESNSKENKIDNKHLNLLSSDSEIEQDYQKAKKRKTSDLNQEHGNGSAILGKLSVKTPIKNTNRKPVSMDNFNDSLTSSGTENDPFVPNIRHNPKELGTANGTGHSTPLSKLKVSASFADKLPQKEVPSTILVPEVEQQEPSQSERTPSLFSSEGSGSESEAPLLPEITTPGPHQPMGNTSNNVVEMIDTDSSNLVSDEDEVLVPTRIETPQLPTEKDVEKCEARVQELQEEVNEQLEHENGSEFDVKQGSGKVGNRHKFKRALKFLSKSLLALFLFCIFIVIPLLFGLWYREQRLLIGYCGHEVPSHRVSGNSFEFIQKLDNLLQDYRPKCIPCPPNGICYPYLKLKCKPDYKLAPSRLDFLEIIPAQGKCVKDDKKQQLVSEVVEKSLEFLRAKNAQISCGDGKDDIESGMTEDALYQIFNEARAPWIRDDEFEDLWIQVIKDLTEEPEILWRQLSPTDNNIGGNSNNIIKTNDVPRQKRHLPEKFISKTRNFRSTSKKYIGMKCRFEREIYQTYKKFQRPIWLMFLLIVISKVIEIKLKNYYRKKARIEELVTQTMEKLKFQKIKSMSDPKENAYLSIVQLRDIFLSDIVDLKYKNQLWSEVVKYLEHNNSNIKSNLTEIRGEIMKCWEWIGPMELNEPKDSAENKI | Function: Plays a role in sister chromatid separation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 95498
Sequence Length: 834
Subcellular Location: Nucleus inner membrane
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O04023 | MECRSLDLTIISAEDLKDVQLIGKQDLYAVVSINGDARTKQKTKVDKDCGTKPKWKHQMKLTVDDAAARDNRLTLVFEIVADRPIAGDKPVGEVSVPVKELLDQNKGDEEKTVTYAVRLPNGKAKGSLKFSFKFGEKYTYGSSSGPHAPVPSAMDHKTMDQPVTAYPPGHGAPSAYPAPPAGPSSGYPPQGHDDKHDGVYGYPQQAGYPAGTGGYPPPGAYPQQGGYPGYPPQQQGGYPGYPPQGPYGYPQQGYPPQGPYGYPQQQAHGKPQKPKKHGKAGAGMGLGLGLGAGLLGGLLVGEAVSDIADMGDMGDMGDMGGFDF | Function: May act as an activator of the calcium-dependent activation of RBOHF that mediates reactive oxygen species (ROS) production and may play a role in cold responses.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 34189
Sequence Length: 324
Subcellular Location: Endoplasmic reticulum membrane
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O04133 | MTMEYRTLELNIISAKDIKNVNLFSKMDVYAAVSLSGDPLHPQGATTHVHKDAGSNPTWNYPVKFSVNESLAKENRLSLEIKLISDRTLGDTVIGTVHVPLRELLDNPGDDSSFRQVSYQVMKQSRKSKGSLNFSYKFGEHVPAPAAKTPKAAKAGQEPVMAYPPAGAGSSSMPYGTPHPPPPQQYAATGYGYPPQQVHGGYPPQAAYGYPPQTGYGYPQQSGYGYPQQSGYGYPPQAQKPKKNKFGMGLGAGLLGGALGGMLIGDMVSDAAEYDAGYDAGFDDAGGFDF | Function: May play a role in cold responses.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31011
Sequence Length: 290
Subcellular Location: Endoplasmic reticulum membrane
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Q8L3X8 | MRRYSPPYYSPPRRGYGGRGRSPPPPPPRRGYGGGGGGGGRRGSSHGSLLVRNIPLDCRPEELREPFERFGPVRDVYIPRDYYSGQPRGFAFVEFVDAYDAGEAQRSMNRRSFAGREITVVVASESRKRPEEMRVKTRTRSREPSGSRDRSHGRSRSRSISRSRSPRRPSDSRSRYRSRSYSPAPRRRGGPPRGEEDENYSRRSYSPGYEGAAAAAPDRDRNGDNEIREKPGYEAEDRRRGGRAVSRSPSGSRSRSVEVSPR | Function: Involved in intron recognition and spliceosome assembly (Probable). Probably active at the 5' splice sites.
PTM: Phosphorylated.
Sequence Mass (Da): 29567
Sequence Length: 262
Subcellular Location: Nucleus speckle
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Q9SEU4 | MRGRSYTPSPPRGYGRRGRSPSPRGRYGGRSRDLPTSLLVRNLRHDCRQEDLRKSFEQFGPVKDIYLPRDYYTGDPRGFGFVQFMDPADAADAKHHMDGYLLLGRELTVVFAEENRKKPTEMRARERGGGRFRDRRRTPPRYYSRSRSPPPRRGRSRSRSGDYYSPPPRRHHPRSISPREERYDGRRSYSRSPASDGSRGRSLTPVRGKSRSLSPSPRRSISRSPRRSRSPSPKRNRSVSPRRSISRSPRRSRSPRRSRRSYTPEPARSRSQSPHGGQYDEDRSPSQ | Function: Involved in intron recognition and spliceosome assembly. Binds to multiple 5'-GAAG-3' repeats found in its third intron, suggesting autoregulation of alternative splicing . May be necessary for accurate splicing of the 3' region of introns.
PTM: Phosphorylated by AFC2.
Sequence Mass (Da): 33337
Sequence Length: 287
Subcellular Location: Nucleus speckle
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Q9V9J3 | MGNCLTTQKGEPDKPADRIKLDDPPTIGVGVGVPQIPMPSHAGQPPEQIRPVPQIPESETAGANAKIFVALYDYDARTDEDLSFRKGEHLEILNDTQGDWWLARSKKTRSEGYIPSNYVAKLKSIEAEPWYFRKIKRIEAEKKLLLPENEHGAFLIRDSESRHNDYSLSVRDGDTVKHYRIRQLDEGGFFIARRTTFRTLQELVEHYSKDSDGLCVNLCKPCVQIEKPVTEGLSHRTRDQWEIDRTSLKFVRKLGSGQFGDVWEGLWNNTTPVAIKTLKSGTMDPKDFLAEAQIMKKLRHTKLIQLYAVCTVEEPIYIITELMKHGSLLEYLQAIAGKGRSLKMQTLIDMAAQIAAGMAYLESQNYIHRDLAARNVLVGDGNIVKIADFGLARLIKEDEYEARVGARFPIKWTAPEAANYSKFSIKSDVWSFGILLTELVTYGRIPYPGMTNAEVLTQVEHGYRMPQPPNCEPRLYEIMLECWHKDPMRRPTFETLQWKLEDFYTSDQSDYKEAQAY | Function: Required directly or indirectly for the phosphorylation of drpr which is necessary for the interaction of drpr with shark and subsequent glial phagocytic activity . Together with drpr and shark, promotes the migration of macrophages to sites of wounding as part of a signaling cascade where Scr42a detects production of hydrogen peroxide at wound sites which triggers phosphorylation of drpr and subsequent recruitment and activation of shark . Essential for correct eye morphogenesis (ommatidial R7 neuron formation) which requires the Ras1/MAPK signal transduction pathway . May be involved in the regulation of cytoskeleton organization and cell-cell contacts in developing ommatidia . During embryogenesis, involved in regulation of dorsal closure where it may have a role in activating the JNK pathway in leading edge cells during this process .
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 59069
Sequence Length: 517
EC: 2.7.10.2
|
P00528 | MGNKCCSKRQDQELALAYPTGGYKKSDYTFGQTHINSSGGGNMGGVLGQKHNNGGSLDSRYTPDPNHRGPLKIGGKGGVDIIRPRTTPTGVPGVVLKRVVVALYDYKSRDESDLSFMKGDRMEVIDDTESDWWRVVNLTTRQEGLIPLNFVAEERSVNSEDWFFENVLRKEADKLLLAEENPRGTFLVRPSEHNPNGYSLSVKDWEDGRGYHVKHYRIKPLDNGGYYIATNQTFPSLQALVMAYSKNALGLCHILSRPCPKPQPQMWDLGPELRDKYEIPRSEIQLLRKLGRGNFGEVFYGKWRNSIDVAVKTLREGTMSTAAFLQEAAIMKKFRHNRLVALYAVCSQEEPIYIVQEYMSKGSLLDFLREGDGRYLHFEDLIYIATQVASGMEYLESKQLIHRDLAARNVLIGENNVAKICDFGLARVIADDEYCPKQGSRFPVKWTAPEAIIYGKFSIKSDVWSYGILLMELFTYGQVPYPGMHSREVIENIERGFRMPKPTNHYFPDNIYQLLLQCWDAVPEKRPTFEFLNHYFESFSVTSEVPYREVQD | Function: May play a role in the development of neural tissue and smooth muscle.
PTM: Phosphorylated.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 63003
Sequence Length: 552
EC: 2.7.10.2
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Q01406 | MTVLLLVVLQMWKATAGHSIAVSQDDGADDWETDPDFVNDVSEKEQRWGAKTVKGSGHQEHINIHQLRENVFQEHQTIKEKELETGPKASHGYGGKFGVEQDRMDKSAVGHEYQSKLSKHCSQVDSVKGFGGKFGVQTDRVDQSAVGFEYQGKTEKHASQKDYSSGFGGKYGVQADRVDKSAVGFDYQGKTEKHESQKDYSKGFGGKYGVDKDKVDKSAVGFEYQGKTEKHESQKDYVKGFGGKFGVQTDRQDKCALGWDHQEKVQLHESQKDYKSGFGGKFGVQTERQDPSAVGFDYKEKLAKHESQQDYSKGFGGKYGVQKDRMDKNAATFEDIEKPTSTYQKTKPVERVANKTSSIRANLENLAKEKEQEDRRKAEAERAQRMAREKQEQEEARRKLEEQAKAKKQTPPPSPTTQPAEPKTPSSPVYQDAVSYDAESAYKNSSTTYSAEHEPESGYKTTGSDYQEAVSQREAEYEPETVYEVAGAGDHYQAEENTYDEYENELGITAIALYDYQAAGDDEISFDPDDIITNIEMIDDGWWRGVCKGRYGLFPANYVELRQ | Function: Contributes to the organization of the actin cytoskeleton and cell shape (By similarity). Plays a role in the formation of lamellipodia and in cell migration (By similarity). Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones, and may play a role in the regulation of neuronal spine density (By similarity). Plays a role in focal adhesion assembly and turnover (By similarity). Plays a role in intracellular protein transport and endocytosis, and in modulating the levels of potassium channels present at the cell membrane (By similarity). Plays a role in endocytosis via clathrin-coated pits (By similarity).
PTM: Acetylated.
Sequence Mass (Da): 63329
Sequence Length: 563
Domain: The SH3 motif may mediate binding to the cytoskeleton.
Subcellular Location: Cytoplasm
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Q75K18 | MVLADLGNQLSSALRSLNETTIVNEDTINQLLKEVGNALSKSDVSMSLIIQMRKNIKDKIKLDQMAAGLNKRKIIKQVVFDELIRLLDPGVPLWKPTKGKSNIVMFVGLQGAGKTTSVTKLAYFYKKKGFSTAIVCADTFRAGAFDQVRHNAAKAKIHYYGSETEKDPVVVARTGVDIFKKDGTEIIIVDTSGRHKQDSELFEEMKQIETAVKPDNCIFVMDSSIGQAAYEQATAFRSSVKVGSIIITKMDGNSMGGGAISAVAATNTPIIFIGTGEHLTDLELFDPSTFVSKLLGYGDMKGMLEKIKEVIPEDSTSLKEIAQGKFTLRSMQQQFQQIMQLGPIDKLVQMIPGMNQLPQLQGNEGGLKLKAYINILDSLSEKELDGKKPITQKRIITIAQGSGRHPNEVVELLEQHKTFEKLIGKGGPGGGLGSLMAGKGGPKNMEQAMKQMNANGGMQGLMNSLKGMGGMGDLAKMFGGGGGGGGGMPSMGDLAKMMGGMGGGGRGGGGMPNMGDLAKMMGGMGGGAGKGGQNGFPNLDLD | Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). As part of the SRP complex, associates with the SRP receptor (SR) component srpra to target secretory proteins to the endoplasmic reticulum membrane. Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes. Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA. Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit srpra. SR compaction and GTPase mediated rearrangement of SR drive SRP-mediated cotranslational protein translocation into the ER (By similarity). Requires the presence of srp9/srp14 and/or srp19 to stably interact with RNA (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 57610
Sequence Length: 542
Domain: The NG domain, also named G domain, is a special guanosine triphosphatase (GTPase) domain, which binds GTP and forms a guanosine 5'-triphosphate (GTP)-dependent complex with a homologous NG domain in the SRP receptor subunit srpra. The two NG domains undergo cooperative rearrangements upon their assembly, which culminate in the reciprocal activation of the GTPase activity of one another. SRP receptor compaction upon binding with cargo-loaded SRP and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER.
Subcellular Location: Cytoplasm
EC: 3.6.5.4
|
O15821 | MVLSQLGSSLVTALRKMTSSTVVDEEVINTLLKEIETSLLGEDVNPIFIRQMVNNIKKKINSEDIPDGIDKRKLIKDSVFEELINLVDPKTEAFKPKKGKTCVLMMVGLQGAGKTTTITKLALYYKNRGYKPAVVGADTFRAGAYEQLQMNAKRAGVPFFGIKEESDPVKVASEGVRTFRKEKNDIILVDTSGRHKQDKELFKEMQSVRDAIKPDSIIFVMDGAIGQAAFGQAKAFKDAVEVGSVIITKLDGHSNGGGALSAVAATKSPIIFIGTGEKVNEIEEFDAESFVRKLLGMGDLKGIAKLAKDFAENAEYKTMVKHLQEGTLTVRDWKEQLSNLQKMGQLGNIMQMIGLNHPMFQGGNIEKKFKVFMVILDSMTDRELDGSAKTMLNDESRIRRLARGSGRDIREVNELFEQIKLFQQCIDRLPKAMRAQLGNCNAQPNEAAMMQQMQRMLPKGVNQAQLQQLMKQMNAAGLGGTGKKGKK | Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory proteins to the endoplasmic reticulum membrane. Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes. Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA. Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit SRPRA. SR compaction and GTPase mediated rearrangement of SR drive SRP-mediated cotranslational protein translocation into the ER. Requires the presence of SRP9/SRP14 and/or SRP19 to stably interact with RNA.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 53857
Sequence Length: 487
Domain: The NG domain, also named G domain, is a special guanosine triphosphatase (GTPase) domain, which binds GTP and forms a guanosine 5'-triphosphate (GTP)-dependent complex with a homologous NG domain in the SRP receptor subunit SRPRA. The two NG domains undergo cooperative rearrangements upon their assembly, which culminate in the reciprocal activation of the GTPase activity of one another. SRP receptor compaction upon binding with cargo-loaded SRP and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER.
Subcellular Location: Cytoplasm
EC: 3.6.5.4
|
Q8MZJ6 | MVLADLGRKITTALLPRQRTVINEEVLQAMLKEICTALLEADVNVKLVGKLRQNVRAAIDFEDMGAGLSKRRIIQTSVFNELCKLLDPGVPVWHPTKGHSNVIMFVGLQGSGKTTTCTKLAYHYQKKGWKTCLVCADTFRAGAFDQLKQNATKARVPFYGSYTEMDPVVIAQEGVEKFKEDSFEVIIVDTSGRHKQEESLFEEMLQVSQAIDPDNIIFVMDGTIGQACESQARAFKEKVDVASVIVTKLDGHAKGGGALSAVAATRSPIIFIGTGEHIDEMEPFKTKPFVSKLLGMGDLEGLMEKVSDLKLDENEELMDKLKHGQFTLRDMYEQFQNIMKMGPFNQIIGMIPGFSPDFMSKGNERESMAKLKRLMTMMDSMNDGELDHPNGAKLFSKQPGRAARVARGSGTSVREVNELLKQYSNFSATVKKMGGIKGLFKGGDLGKNVNPSQMAKLNQQMAKMMDPRVLQQMGGMSGLQNMMRQFQQGASNMPGFKGK | Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (By similarity). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory proteins to the endoplasmic reticulum membrane (By similarity). Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes (By similarity). Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA (By similarity). Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit SRPRA (By similarity). SR compaction and GTPase mediated rearrangement of SR drive SRP-mediated cotranslational protein translocation into the ER (By similarity). Requires the presence of SRP9/SRP14 and/or SRP19 to stably interact with RNA (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 55175
Sequence Length: 499
Domain: The NG domain, also named G domain, is a special guanosine triphosphatase (GTPase) domain, which binds GTP and forms a guanosine 5'-triphosphate (GTP)-dependent complex with a homologous NG domain in the SRP receptor subunit SRPRA (By similarity). The two NG domains undergo cooperative rearrangements upon their assembly, which culminate in the reciprocal activation of the GTPase activity of one another (By similarity). SRP receptor compaction upon binding with cargo-loaded SRP and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER (By similarity).
Subcellular Location: Nucleus speckle
EC: 3.6.5.4
|
P44518 | MFENLSDRLSKTLRNITGKGRLTEDNIKETLREVRMALLEADVALPVVREFIAKVKESALGEEVNKSLTPGQEFLKIVQRELEKAMGEANESLNLATQPPAVILMAGLQGAGKTTSVGKLAKFLRERHKKKVLVVSADVYRPAAIKQLETLAQSVGVDFFPSDVKQNPVDIAKSALADAKLKFYDVLIVDTAGRLHVDTEMMDEIKQVHAALNPIETLFTVDAMTGQDAANTAKAFNEALPLTGVILTKVDGDARGGAALSIRQITGKPIKFLGVGEKTEALEPFHPDRVASRILGMGDVLSLIEDLERSVDREKAEKMAQKFKKGDDFTLDDFREQLIEMKKMGGMMSMLEKLPGAKNLSEHVKNQVDDKMFVKMEAIINSMTLKERANPDIIKGSRRRRIALGSGTQVQDVNKLLKQFDEMQRMMKKMRKGGMAKMMRGMQGLMGGGLGGLGGLGGMFKR | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 50843
Sequence Length: 462
Domain: Composed of three domains: the N-terminal N domain, which is responsible for interactions with the ribosome, the central G domain, which binds GTP, and the C-terminal M domain, which binds the RNA and the signal sequence of the RNC.
Subcellular Location: Cytoplasm
EC: 3.6.5.4
|
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