ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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P06015 | MVTKERNAALKIVMLVASALTLHPQQALAQTAGRPLADVVGKTLCTYSKTAKRQAANLAQTLQRASSAAKQSRQAQQLAALALAKLPDYKEAAATLLIYATHKIQDAQASIENWTGENTKLVGQAMYSSGRIDELMLLLEGHREDGANGQDKTCLGAAAGGNTVNEFVKTECDTESGHNIEADNSNIGQAATTLSQESTDPEASGGASCKITANLATDYDSHANELPLLGGLLTIHNAGGFKTGQSLQTAAPTNKLISALKNKGAGVAAKLATVTSAAPTSKQELKTLLASKGERAKLQAANDEYNNWKPGAKPEDFDAHIKKVFGAEDGKDSAYAIALEGISIEAPLGGGQTQNKQLYSMQPKDLMAALIGTIAELQTAAATKPACPGHKQTTTESDALCSKIKDANECNSKHFCSYNGTETDSAKKCKYNATKASASDAPVTQAQTTSRSETPAEKCTGKKKDDCKDGCKWEAETCKDSSILLTKNFALSVVSAALVALLF | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 52814
Sequence Length: 503
Subcellular Location: Cell membrane
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P06017 | DQKGKSPESECNKISEEPKCNEDKICSWHKEVKAGEKHCKFNSTKAKEKGVAVTQTQTAGGTEATTDKCKGKLEDTCKKESNCKWEGETCKDSSILVNKQLALSVVSAAFAALLF | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 12530
Sequence Length: 115
Subcellular Location: Cell membrane
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P26335 | KNTGRRPNYRECEMRDGECNAKVAKTAEPDSKTNTTGNNSFAIKTSTLLLAVLLF | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 6077
Sequence Length: 55
Subcellular Location: Cell membrane
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P20950 | MFTQAVIALIGLVSIRTGKTEDVTPCTTNCGCWARLEKQITVYRGDYSAAEENLKENKKNFGKIIAATVLGSEKLKATVAPVLLSAAQIIHECEEALTTARPAILDAEKKVAELRALYDVQQKLKEGNGELQLHIQDDTNINTAKEVPKANLGNINKKGCADDLNTPDAATIDKTNIETEGPTPKVITHVHVEARCQRDGTPTNGCHDGQLGQNGKLEFSLTYDSKDTNDLATWLADTATKKQISATEVDFIGNLNTEANTAIKGLKSSNPAPACSKKIRDYKTIADNSKFNLMVTKALIGKTDAEAGQESKEPELAAAITKYYGTEGTKFEDQLWKAIERTPAYLGDQKKEQTTKIEKLETLTEVGEATARGLVKQLAAGAQARQTASGDDQSAENQCGGKKEDECKDGCELVEGVCKPVKQGEGENKEKTGTTNTTGSNSFVIKKAPLWLAFLLF | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 49416
Sequence Length: 457
Subcellular Location: Cell membrane
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P02897 | MPTAGAVLLLATAAVLSRPAAAANEKKPLTISAAGAVCGFSNELKEVASFAATKVNAYLTETEQLGTLAVDFCAAIFNGNGKPTAGEVYAALLAAKTQTDRQAQQQKLVTGALLASSLCSQQAGHIESFIHVFYQAHRDATTTCIYKSDEHQRKAADVPCVNNGGGLNKITITTRATKPQLNSKYKAIVAGTTPNGAAAEKNCKLVNGEQSQNVFLASQTTNIALKWGDGLLTVPIGDTAISASNWEPNNKDSIASGNYKECAAALEQVPPRQSTATAAASKLLKLEAEDDPKLEEELISKNSFYGDFPISNVKITATDFSSLHSKLKSYRKKHTADGHQLLKAKLQHLEKQMQMNATACKLGAEISSGEPSTAKTTTSGRCEGKAKTACPKSDYRQREEKDGKEECKPKSGEEQKTQTTGAGEGAADKKEEKCKGKLEPECTKAPECKWEGETCKDSSILVNKQFTLSMISAAFM | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 50723
Sequence Length: 476
Subcellular Location: Cell membrane
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P02898 | SEPTMSTRVQQATSCVLLIIGCTNYAASKQQTENNAVCDTPCKCLGRLAVQKAYLEGALEHARQSIKAFASSSRQHTIAAGATNTKLSGHHPNQGRRGRRRSSSARPNNSKGNSPSKRAGGAVRGETPASGRLKAAKLLKSSNYETATFTPTEMTIQNRRACEQVDESKEYRFDELNFDKEQGIPTPALTLEISMGCQKNPGDTGGACDGTNADDGVVTKLTFTTAAPVAETSPLVAGAYKKTSKASLSISNRTEEGRVANSKAAHEAAKRLMAIKQPSDLSTYTDDSSFALLVGQLAMKPPLGAELTPALRDQVNKFITDNYGANEGDFRSKFLAKTEQAAVFYLDGKSKKTKKISELESKSELVTASGYAFFKGIHTEQAEKVENPRSQGNPETAENKKEGGNTAKPFCSTIQNQTECEGVKGTPPTGKAKVCGWIEGKCQDSSFLLSKQFALSVVSAAFAALLF | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 49963
Sequence Length: 467
Subcellular Location: Cell membrane
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P0DJF0 | VVGGDCIPQVPFLAFLYSEYFC | Function: Thrombin-like serine protease which cleaves specifically the Aalpha chain of human fibrinogen (FGA) to release fibrinopeptide A. Also cleaves rapidly the Bbeta chain of human fibrinogen (FGB). Is selective for Arg over Lys at position 1 of the tripeptide substrates.
PTM: Glycosylated; required for activity. Highly glycosylated with 42% of N-linked carbohydrates composed of Fuc(1):GalN(4):GlcN(5):Gal(1):Man(2) and a high content of sialic acid residues (8-12%).
Sequence Mass (Da): 2468
Sequence Length: 22
Subcellular Location: Secreted
EC: 3.4.21.-
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Q7LZF4 | VIGGAEENINEHRSL | Function: Snake venom serine protease that potently induces platelet aggregation. Its aggregatory activity is partially inhibited by monoclonal antibodies against GPIb and the thrombin receptor. Its ability to induce intracellular Ca(2+) release is blocked by pretreating platelets with thrombin. Hydrolyzes thrombin chromogenic substrate CBS 34.47, but shows very weak coagulant activity. Can hydrolyze fibrinogen alpha-chains.
Sequence Mass (Da): 1638
Sequence Length: 15
Subcellular Location: Secreted
EC: 3.4.21.-
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C0HK18 | GGDECNINEHRSPQETLPDVPHCANINLLDYEVCRTAHPQFRLPATSRTLCAGILEGGKDTCHR | Function: Thrombin-like snake venom serine protease.
Sequence Mass (Da): 7072
Sequence Length: 64
Subcellular Location: Secreted
EC: 3.4.21.-
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C0HLA3 | VFGGDECNINEHRSLVVLFDSDGFLCAGTLINKEWVLTAAHCDSENFQMQLGV | Function: Snake venom serine protease that has fibrinogenolytic activity. Hydrolyzes the alpha-chain of fibrinogen (FGA), without affecting the beta- and the gamma-chains. Also displays hydrolytic activity towards S-2302 (plasma kallikrein substrate) and S-2251 (substrate for plasmin), but has no hydrolytic activity with S-2238 (thrombin substrate) or S-2222 (factor Xa).
PTM: N-glycosylated.
Sequence Mass (Da): 5845
Sequence Length: 53
Subcellular Location: Secreted
EC: 3.4.21.-
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Q9AST6 | MADVPGYLRTCLDMGKIAFLAILVSTGIVLQILACALFNNWWPMLSVIMYVLLPMPLLFFGGSDSTSLFNESDNSWINAAKFLTGASAVGSVAIPSILKHAGLIGWGALALDLSSYVVFLVAILGYICIGDASDNYYSYI | Function: Involved in endosomal protein transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15025
Sequence Length: 140
Subcellular Location: Endosome membrane
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P20948 | MKRVLSNVLKAWIFTIVAFHNFSTSVTADAPVNAAEYNALCRLYNIARAGEGLKEEDWLPCAGKAACEKTAASIEDVFMKLNFSEPSAVVTTLDGTRVELQNSASTRIKRAKLAKVLAAAETIKAQQLKYHESSKSLLESAKANFTKAIVGGWGNPTTPDESGLPTTFKTNRADDCKLAGGNGGKSLVFDIACLCTTSDSASGSKYTCGPKSGDNGSGWLDNNGDNQGKPAAKEAWKNLRADCRRQSAGVRVTPELISQSLVIFEGLIGTRAASGHDNARYIFGTVATAQSCGHSTATNKGSIDYKASNAQQRGDIEWEKNLRMAEGDLRGLLTAKQLVAALQARAEHLEDAAFTIFNESVLETQIAWESSRPPSTDANTSQKGPLQRPEKSGESSHLPSGSSHGTKAIRSILHVALLM | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 44767
Sequence Length: 419
Subcellular Location: Cell membrane
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P20949 | MLDNSRARSIVHLLILLKAHVITQIIKNTQEFTSLCTFVKVTLKATDGLTSAASKSQTDWALGENPTSRIKKLITELETSSDRIRLGEEPNLTIQLPQGDPKQRLRRKLEVFLARAKYTEELVRQAQGDVGGRCNEAKAELEEAVTGRKGPDLETQATAAAAALHNKARGTACKVAGATTDTNFAGTSLVADLMCLCAAETNSREKHICGFESHASGVWANAGTNSNAGEIWGKILDACKNREIQVEVTPQFLRIAITKFEGLLGAQAHKLTSNGNAGAWLLGYSMNAGSVTCDGQSSTNGICVDYKGSSDARGPIAWLGHIKNAITALENRDKNLQRVRKLQRQAEAILMSAEDALIEANISLGGKDMVPASEVTVPNSSNPTSRQNSVVQEPTTVSAAAITPLILPWTLLI | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 44324
Sequence Length: 413
Subcellular Location: Cell membrane
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A6QLN9 | MLPWTVIGLALSLRLARSGAERGLPASALQGDLLFLLDSSASVSHYEFNRVREFLGRLAALLPVGPGALRASLVHVGSRPHTEFPFGQHSSGSAVQDAIRAAAQRMGDTNTGLALAYAKKQLFAKAAGARPGVPKVLVWVTDGGSSDPVGPPMQELKDLGVTVFIVSTGRGNLLELSAAASAPAEKHLHFVDVDDLHIITQALRGSILDAMWPQQLHASEVTSSGFRLAWPSLLTADSGYYVLELAPSTDPGAARRQQLPGNATGWAWTGLDSDTDYDVALVPESNVRLLRSQHLRVRTLPEETGPELIVVSHTRPRSLRVSWAPALGPDAALGYHVQVGPLRGGAAQSVEVPAGENSTTLQGLAPGTAYLVTVTAAFRSGRERALSAKACTPEGERSRAPRPQPQRTGGREP | Function: Promotes matrix assembly (By similarity). Involved in the organization of skeletal muscles and in the formation of neuromuscular junctions (By similarity).
PTM: N-glycosylated.
Sequence Mass (Da): 43738
Sequence Length: 413
Subcellular Location: Secreted
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Q6PCB0 | MLPWTALGLALSLRLALARSGAERGPPASAPRGDLMFLLDSSASVSHYEFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRASAQRMGDTHTGLALVYAKEQLFAEASGARPGVPKVLVWVTDGGSSDPVGPPMQELKDLGVTVFIVSTGRGNFLELSAAASAPAEKHLHFVDVDDLHIIVQELRGSILDAMRPQQLHATEITSSGFRLAWPPLLTADSGYYVLELVPSAQPGAARRQQLPGNATDWIWAGLDPDTDYDVALVPESNVRLLRPQILRVRTRPGEAGPGASGPESGAGPAPTQLAALPAPEEAGPERIVISHARPRSLRVSWAPALGSAAALGYHVQFGPLRGGEAQRVEVPAGRNCTTLQGLAPGTAYLVTVTAAFRSGRESALSAKACTPDGPRPRPRPVPRAPTPGTASREP | Function: Promotes matrix assembly (By similarity). Involved in the organization of skeletal muscles and in the formation of neuromuscular junctions (Probable).
PTM: N-glycosylated.
Sequence Mass (Da): 46804
Sequence Length: 445
Subcellular Location: Secreted
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Q8R2Z5 | MLFWTAFSMALSLRLALARSSIERGSTASDPQGDLLFLLDSSASVSHYEFSRVREFVGQLVATMSFGPGALRASLVHVGSQPHTEFTFDQYSSGQAIQDAIRVAPQRMGDTNTGLALAYAKEQLFAEEAGARPGVPKVLVWVTDGGSSDPVGPPMQELKDLGVTIFIVSTGRGNLLELLAAASAPAEKHLHFVDVDDLPIIARELRGSITDAMQPQQLHASEVLSSGFRLSWPPLLTADSGYYVLELVPSGKLATTRRQQLPGNATSWTWTDLDPDTDYEVSLLPESNVHLLRPQHVRVRTLQEEAGPERIVISHARPRSLRVSWAPALGPDSALGYHVQLGPLQGGSLERVEVPAGQNSTTVQGLTPCTTYLVTVTAAFRSGRQRALSAKACTASGARTRAPQSMRPEAGPREP | Function: Promotes matrix assembly . Involved in the organization of skeletal muscles and in the formation of neuromuscular junctions (By similarity).
PTM: N-glycosylated.
Sequence Mass (Da): 44709
Sequence Length: 415
Subcellular Location: Secreted
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Q92558 | MPLVKRNIDPRHLCHTALPRGIKNELECVTNISLANIIRQLSSLSKYAEDIFGELFNEAHSFSFRVNSLQERVDRLSVSVTQLDPKEEELSLQDITMRKAFRSSTIQDQQLFDRKTLPIPLQETYDVCEQPPPLNILTPYRDDGKEGLKFYTNPSYFFDLWKEKMLQDTEDKRKEKRKQKQKNLDRPHEPEKVPRAPHDRRREWQKLAQGPELAEDDANLLHKHIEVANGPASHFETRPQTYVDHMDGSYSLSALPFSQMSELLTRAEERVLVRPHEPPPPPPMHGAGDAKPIPTCISSATGLIENRPQSPATGRTPVFVSPTPPPPPPPLPSALSTSSLRASMTSTPPPPVPPPPPPPATALQAPAVPPPPAPLQIAPGVLHPAPPPIAPPLVQPSPPVARAAPVCETVPVHPLPQGEVQGLPPPPPPPPLPPPGIRPSSPVTVTALAHPPSGLHPTPSTAPGPHVPLMPPSPPSQVIPASEPKRHPSTLPVISDARSVLLEAIRKGIQLRKVEEQREQEAKHERIENDVATILSRRIAVEYSDSEDDSEFDEVDWLE | Function: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation . The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex (By similarity). As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). Also involved in the regulation of mitochondrial dynamics .
PTM: Phosphorylated on tyrosine residues by ABL1 and dephosphorylated by PTPN12.
Sequence Mass (Da): 61652
Sequence Length: 559
Domain: Binds the Arp2/3 complex through the C-terminal region and actin through verprolin homology (VPH) domain.
Subcellular Location: Cytoplasm
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Q9Y6W5 | MPLVTRNIEPRHLCRQTLPSVRSELECVTNITLANVIRQLGSLSKYAEDIFGELFTQANTFASRVSSLAERVDRLQVKVTQLDPKEEEVSLQGINTRKAFRSSTIQDQKLFDRNSLPVPVLETYNTCDTPPPLNNLTPYRDDGKEALKFYTDPSYFFDLWKEKMLQDTKDIMKEKRKHRKEKKDNPNRGNVNPRKIKTRKEEWEKMKMGQEFVESKEKLGTSGYPPTLVYQNGSIGCVENVDASSYPPPPQSDSASSPSPSFSEDNLPPPPAEFSYPVDNQRGSGLAGPKRSSVVSPSHPPPAPPLGSPPGPKPGFAPPPAPPPPPPPMIGIPPPPPPVGFGSPGTPPPPSPPSFPPHPDFAAPPPPPPPPAADYPTLPPPPLSQPTGGAPPPPPPPPPPGPPPPPFTGADGQPAIPPPLSDTTKPKSSLPAVSDARSDLLSAIRQGFQLRRVEEQREQEKRDVVGNDVATILSRRIAVEYSDSEDDSSEFDEDDWSD | Function: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex.
Sequence Mass (Da): 54284
Sequence Length: 498
Domain: Binds and activates the Arp2/3 complex via the C-terminal domain. Interacts with actin via the WH2 domain.
Subcellular Location: Cytoplasm
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Q8BH43 | MPLVTRNIEPRHLCRQTLPSDTSELECRTNITLANVIRQLGSLSKYAEDIFGEICTQASAFASRVNSLAERVDRVQVKVTQLDPKEEEVSLQGINTRKAFRSSTTQDQKLFDRNSLPVPVLETYNSCDAPPPLNNLSPYRDDGKEALKFYTNPSYFFDLWKEKMLQDTKDIMKEKRKHRKEKKDNPNRGNVNPRKIKTRKEEWEKMKMGQEFVESKERLGPSGYSSTLVYQNGSIGSVENVDAASYPPPPQSDSASSPSPSFSEDNLPPPPAEFSYPADNQRGSVLAGPKRTSMVSPSHPPPAPPLSSPPGPKPGFAPPPAPPPPPPMSVPPPLPSMGFGSPGTPPPPSPPSFPPHPDFAAPPPPPPPPAADYPMPPPPLSQPSGGAPPPPPPPPPPGPPPLPFSGADGQPAAPPPPPPSEATKPKSSLPAVSDARSDLLSAIRQGFQLRRVEEQREQEKRDVVGNDVATILSRRIAVEYSDSEDDSSEFDEDDWSD | Function: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex (By similarity).
Sequence Mass (Da): 54074
Sequence Length: 497
Domain: Binds and activates the Arp2/3 complex via the C-terminal domain. Interacts with actin via the WH2 domain (By similarity).
Subcellular Location: Cytoplasm
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Q9UPY6 | MPLVKRNIEPRHLCRGALPEGITSELECVTNSTLAAIIRQLSSLSKHAEDIFGELFNEANNFYIRANSLQDRIDRLAVKVTQLDSTVEEVSLQDINMKKAFKSSTVQDQQVVSKNSIPNPVADIYNQSDKPPPLNILTPYRDDKKDGLKFYTDPSYFFDLWKEKMLQDTEDKRKEKRRQKEQKRIDGTTREVKKVRKARNRRQEWNMMAYDKELRPDNRLSQSVYHGASSEGSLSPDTRSHASDVTDYSYPATPNHSLHPQPVTPSYAAGDVPPHGPASQAAEHEYRPPSASARHMALNRPQQPPPPPPPQAPEGSQASAPMAPADYGMLPAQIIEYYNPSGPPPPPPPPVIPSAQTAFVSPLQMPMQPPFPASASSTHAAPPHPPSTGLLVTAPPPPGPPPPPPGPPGPGSSLSSSPMHGPPVAEAKRQEPAQPPISDARSDLLAAIRMGIQLKKVQEQREQEAKREPVGNDVATILSRRIAVEYSDSDDDSEFDENDWSD | Function: Downstream effector molecules involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape.
PTM: Phosphorylation by ABL1 promotes lamellipodia formation and cell migration.
Sequence Mass (Da): 55293
Sequence Length: 502
Domain: Binds the Arp2/3 complex through the C-terminal region and actin through verprolin homology (VPH) domain.
Subcellular Location: Cytoplasm
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A7Z063 | MTPTGTQHSLAGQTYAVPLIQPDLRREEAIQQVADALQYLQKVSGDIFSRISQRVELSRSQLQAIGERVSLAQAKIEKIKGSKKAIKVFSSAKYPAPERLQEYGSIFMGAQDPGLQRRPRHRIQSKHRPLDERALQEKLKFFPVCVNTKPEPEDEAEEGLGGLPSNISSVSSLLLFNTTENLYKKYVFLDPLAGAVTKTHVMLGAETEEKLFDAPLSISRREQLERQVPENYFYVPDLGQVPDIDVPSYLPDLPGVADDLMYSADLGPGIAPSAPGAIPELPTFHTEVAQPFKPDLEDGVLTARPPPPPPPPPPPAPAVLMSVPPPPPPPQAPPGQPAKGDDSGGASPSAPVQGAPKEVVDPSSGRATLLESIRQAGGIGKAKLRSVKERKLEKKKQKEQEQVRATSQGGDLMSDLFNKLAMRRKGISGKGPGSGASEGPGGAFARMSDSIPPLPPPQQPPGEEDEDDWES | Function: Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. Involved in endocytic trafficking of EGF. Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration. In T-cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T-cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T-cell activation. Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity).
Sequence Mass (Da): 50773
Sequence Length: 471
Domain: The VCA (verprolin, cofilin, acidic) domain promotes actin polymerization by the Arp2/3 complex in vitro.
Subcellular Location: Early endosome membrane
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Q8TAF3 | MAAHHRQNTAGRRKVQVSYVIRDEVEKYNRNGVNALQLDPALNRLFTAGRDSIIRIWSVNQHKQDPYIASMEHHTDWVNDIVLCCNGKTLISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTASNNTVTTSSLSGNKDSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQVNDAFTHVYSGGRDRKIYCTDLRNPDIRVLICEEKAPVLKMELDRSADPPPAIWVATTKSTVNKWTLKGIHNFRASGDYDNDCTNPITPLCTQPDQVIKGGASIIQCHILNDKRHILTKDTNNNVAYWDVLKACKVEDLGKVDFEDEIKKRFKMVYVPNWFSVDLKTGMLTITLDESDCFAAWVSAKDAGFSSPDGSDPKLNLGGLLLQALLEYWPRTHVNPMDEEENEVNHVNGEQENRVQKGNGYFQVPPHTPVIFGEAGGRTLFRLLCRDSGGETESMLLNETVPQWVIDITVDKNMPKFNKIPFYLQPHASSGAKTLKKDRLSASDMLQVRKVMEHVYEKIINLDNESQTTSSSNNEKPGEQEKEEDIAVLAEEKIELLCQDQVLDPNMDLRTVKHFIWKSGGDLTLHYRQKST | Function: Regulator of deubiquitinating complexes, which acts as a strong activator of USP1, USP12 and USP46 . Enhances the USP1-mediated deubiquitination of FANCD2; USP1 being almost inactive by itself . Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate . Also activates deubiquitinating activity of complexes containing USP12 . In complex with USP12, acts as a potential tumor suppressor by positively regulating PHLPP1 stability . Docks at the distal end of the USP12 fingers domain and induces a cascade of structural changes leading to the activation of the enzyme . Together with RAD51AP1, promotes DNA repair by stimulating RAD51-mediated homologous recombination . Binds single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) . DNA-binding is required both for USP1-mediated deubiquitination of FANCD2 and stimulation of RAD51-mediated homologous recombination: both WDR48/UAF1 and RAD51AP1 have coordinated role in DNA-binding during these processes . Together with ATAD5 and by regulating USP1 activity, has a role in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA . Together with ATAD5, has a role in recruiting RAD51 to stalled forks during replication stress .
Sequence Mass (Da): 76210
Sequence Length: 677
Domain: N-terminal WD region interacts with TIP and C-terminal region mediates lysosomal localization (Probable). The WD repeats are required for the interaction with deubiquitinating enzymes USP1, USP12 and USP46.
Subcellular Location: Nucleus
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A7E3S5 | MASSAGLALCGHALVVRGGSRLLATSTSSSDGDSLFIYDCSAAEKKSQENKGEDGQPVDQGSDTVLASTFSKSGSYFVLTDDSKRLILFRTNPWQCLSVRTVVRRCTALTFTASEEKILVADKSGDVYSFSVLEPHGGGRLELGHLSMLLDVAVSPDDRFVLTADRDEKIRVSWAAAPHSIESFCLGHTEFVSRIFVVPNHPELLLSSSGDCTLRLWEYRSGRELHCCPLTSLQEPTEPWSDKRFAVSRITYWSQEDCVALSCDGLPVVYIFQLDAAQRQLVPRQLLTFQHRVWDAAFEEGHGLWVLQDCREDPLVLYRPVGGQWQSAPESAELRRVCAHVRVNWAMLEGCAGVDSGFSSLYKATCDNMTTYLKKKEERLQQQLEKKRRQAPPPGPNGPTKKMRAGELAQGCSS | Function: Non-catalytic component of the METTL1-WDR4 methyltransferase complex required for the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs). In the METTL1-WDR4 methyltransferase complex, WDR4 acts as a scaffold for tRNA-binding. Required for the formation of N(7)-methylguanine at position 46 (m7G46) in a large subset of tRNAs that contain the 5'-RAGGU-3' motif within the variable loop. M7G46 interacts with C13-G22 in the D-loop to stabilize tRNA tertiary structure and protect tRNAs from decay. Also required for the formation of N(7)-methylguanine at internal sites in a subset of mRNAs. Also required for methylation of a specific subset of miRNAs, such as let-7. Independently of METTL1, also plays a role in genome stability: localizes at the DNA replication site and regulates endonucleolytic activities of FEN1.
Sequence Mass (Da): 45858
Sequence Length: 414
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Subcellular Location: Nucleus
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Q23232 | MSFITAFRERVFIASGDLIRTFRISEETELKNFISWSKINPERIQKPSFDIEKELKAVEKRVILCLAHSNVLTTHGRRLVAVGTNEKQIHVFEYFVNDKGDIVTAEHIVTSVVPKAPTAIVFDKEDAYVVVGDRAGDVHRFSVLNGSAIEMAGAISMILDVAFSPDGKRLLMADRDEKVRALRYPATSVIDSFFLGHTEYVKTLAVQDNDSLWSSGGDKNLYNWSIAKCSAPRRTLDLSQFDAPIRKISINLQHKKIAVIFEKIETVVIVDLNQESLQTTSVSIVGESQCLDIASTKDYFAVLGRSTVHLIDLNNMEQKFVPIDEELTITLTSTNDAIDNLFKNVTHNNQQEYEKRKADKFEQIEKKKRRLNEDINGDDGEGPGPSNS | Function: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
Sequence Mass (Da): 43639
Sequence Length: 388
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Subcellular Location: Nucleus
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A4IGH4 | MAVVCSKADWFVTSCSTTLVAVNLKQSREPFVFDCSKAEKKPKEADVDNKSAGEGSEEKDSDSILAFAISASGKHVALTDDHKRLVLFCTEPSWKCISTRWVVRRCTSLAFTQAEDELYVADKSGDVYSFSILEPHKAGELKLGHLSMLLDVALSPDDKYIITADRDEKIRVSFRRSPYNIQAFCLGHTEFVSSLLVPAGHPDWLLSGSGDGTVNVWHYETGRRLHSVDMRKFGLDSENTEKRFAVSRIISSPDGQHVAVQCEGFPSVQLFTVDCGTEGLLKPADTLTLPLSPWDVTFDSENQLWVLLESEDMKVLLYRHSEQHWRLCDSESPELKKVTNALQTQWHLFKGSVGLESQFKHLYKVNFDNMASYLQKKQERLDLEHKKRAAAANGSKPNKKSKTESGAVPQSTS | Function: Non-catalytic component of the METTL1-WDR4 methyltransferase complex required for the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs). In the METTL1-WDR4 methyltransferase complex, wdr4 acts as a scaffold for tRNA-binding. Required for the formation of N(7)-methylguanine at position 46 (m7G46) in a large subset of tRNAs that contain the 5'-RAGGU-3' motif within the variable loop. M7G46 interacts with C13-G22 in the D-loop to stabilize tRNA tertiary structure and protect tRNAs from decay. Also required for the formation of N(7)-methylguanine at internal sites in a subset of mRNAs. Also required for methylation of a specific subset of miRNAs.
Sequence Mass (Da): 46240
Sequence Length: 413
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Subcellular Location: Nucleus
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Q54UI3 | MSTTAVFIPPQIMVTSNVEKVPISIITHSSDSNFIAYRLNNKLNIFDNKLNKLGELESGSQHTGIIRSIEFTKNNQSLITSSSDKFLKIWDTTNNFKNIKSINTNKKIICSILNKDDSEILVSDKCGDVFKYSLIDDSKNKIEVSGDKSAKHDEKESDKNLVFGHYSSIVDIKFSPCFNYLLSADRDEKIRVSHYPNCFDIESFCLGHTKYVTEILLVPGRDDLLISGSGDGTIKLWNWKQGKCLQTVDFNSKHENAITIPQVVFKVDATTTTNQLIFSIENSNNIYILPMNVEKGEFNQSELKTIPLTQSSPISIDLIDNGKTILASLLPTTKEVDVAIAFDSTTLSQQSDNKVVIAINSVDASTTLKPAELKSVLESIEKKQYRKHVSYSKQMMNSTDNKNKEDDDLSLDEQDIDDTTDINNNNKNKNQETIQDSRPLKLRKMTIEGDKEIQKELEEKESKKQEE | Function: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
Sequence Mass (Da): 52703
Sequence Length: 467
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Subcellular Location: Nucleus
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P57081 | MAGSVGLALCGQTLVVRGGSRFLATSIASSDDDSLFIYDCSAAEKKSQENKGEDAPLDQGSGAILASTFSKSGSYFALTDDSKRLILFRTKPWQCLSVRTVARRCTALTFIASEEKVLVADKSGDVYSFSVLEPHGCGRLELGHLSMLLDVAVSPDDRFILTADRDEKIRVSWAAAPHSIESFCLGHTEFVSRISVVPTQPGLLLSSSGDGTLRLWEYRSGRQLHCCHLASLQELVDPQAPQKFAASRIAFWCQENCVALLCDGTPVVYIFQLDARRQQLVYRQQLAFQHQVWDVAFEETQGLWVLQDCQEAPLVLYRPVGDQWQSVPESTVLKKVSGVLRGNWAMLEGSAGADASFSSLYKATFDNVTSYLKKKEERLQQQLEKKQRRRSPPPGPDGHAKKMRPGEATLSC | Function: Non-catalytic component of the METTL1-WDR4 methyltransferase complex required for the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs) . In the METTL1-WDR4 methyltransferase complex, WDR4 acts as a scaffold for tRNA-binding . Required for the formation of N(7)-methylguanine at position 46 (m7G46) in a large subset of tRNAs that contain the 5'-RAGGU-3' motif within the variable loop . M7G46 interacts with C13-G22 in the D-loop to stabilize tRNA tertiary structure and protect tRNAs from decay . Also required for the formation of N(7)-methylguanine at internal sites in a subset of mRNAs . Also required for methylation of a specific subset of miRNAs, such as let-7 . Independently of METTL1, also plays a role in genome stability: localizes at the DNA replication site and regulates endonucleolytic activities of FEN1 .
Sequence Mass (Da): 45490
Sequence Length: 412
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Subcellular Location: Nucleus
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Q9EP82 | MASSAGLALCAQTLVVRGGSRFLAFSTTGSDDDCVFTYDCSTAEKKATPEDKGEDGQPADTGSDSILASTFSKSGRYFALTDDSKRLILFRTKPWQCLSVRMVVRRCTALTFTASEDRVLVADKSGDVYSFSVLEPDGCGRLELGHLSMLLDVAVSPDDQFVLTADRDEKIRVSWAAAPHSIESFCLGHTEFVSRILVVPSHPELLLSSSGDGTLRLWEYRSGRQLQCCDLAGLQEPGEQPGHKGLAASRIAFWGQESYVVLLCECVPVVFVFQLDASRQQLVFRQRLTFPHRVWDVVFEEARGLWVLQDCRDAPLVLWRPVGGEWQAAPDGAVSPRLCSHLRESWAMLEGSVGTDDSFRSLYKATFDNMTSYLKKKEERLQQQLKKKRQRSPFPGSPEQTKKACPGQSALSC | Function: Non-catalytic component of the METTL1-WDR4 methyltransferase complex required for the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs) . In the METTL1-WDR4 methyltransferase complex, WDR4 acts as a scaffold for tRNA-binding (By similarity). Required for the formation of N(7)-methylguanine at position 46 (m7G46) in a large subset of tRNAs that contain the 5'-RAGGU-3' motif within the variable loop . M7G46 interacts with C13-G22 in the D-loop to stabilize tRNA tertiary structure and protect tRNAs from decay (By similarity). Also required for the formation of N(7)-methylguanine at internal sites in a subset of mRNAs (By similarity). Also required for methylation of a specific subset of miRNAs, such as let-7 (By similarity). Acts as a regulator of embryonic stem cell self-renewal and differentiation . Independently of METTL1, also plays a role in genome stability: localizes at the DNA replication site and regulates endonucleolytic activities of FEN1 .
Sequence Mass (Da): 45756
Sequence Length: 413
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Subcellular Location: Nucleus
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Q7ZY78 | MLRVGPGSLAITGGSRLLGHRVGSECCPFHLDCSLLEKQSAAPGQEGSADSHGSDKILAAAFSPSGEYFALTDDNKRLVLFRTKPAWEKISVRWVSRRCTALTFSPCGNHILVADKSGDVFSFSVPRALEQGRLELGHLSMLLDVTVSLDGKHIITCDRDEKIRVSCWGAPHVIMSFCLGHTEFVSQLLPLPGQEKLLLSGSGDGTLRLWEYESGKEVHSVTLRSLAHELEDQENKRFAVSRISCCSCNGIQLAVLCEGVPGIFLFSVSPEPRLTFTQYIALTHTPIDLDFDGSAFLWVLSGVREEPLLKYKELDDQWQSVSNDEELTRLTGIIQENWGDLEGAGAPESRFVGLYKAVFDNMATYLQKKELRLESEKRKAADGQVVLASKVQKTES | Function: Non-catalytic component of the METTL1-WDR4 methyltransferase complex required for the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs). In the METTL1-WDR4 methyltransferase complex, wdr4 acts as a scaffold for tRNA-binding. Required for the formation of N(7)-methylguanine at position 46 (m7G46) in a large subset of tRNAs that contain the 5'-RAGGU-3' motif within the variable loop. M7G46 interacts with C13-G22 in the D-loop to stabilize tRNA tertiary structure and protect tRNAs from decay. Also required for the formation of N(7)-methylguanine at internal sites in a subset of mRNAs. Also required for methylation of a specific subset of miRNAs.
Sequence Mass (Da): 43646
Sequence Length: 396
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Subcellular Location: Nucleus
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P27833 | MIPFNAPPVVGTELDYMQSAMGSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGGEGGATLINDKALIERAEIIREKGTNRSQFFRGQVDKYTWRDIGSSYLMSDLQAAYLWAQLEAADRINQQRLALWQNYYDALAPLAKAGRIELPSIPDGCVQNAHMFYIKLRDIDDRSALINFLKEAEIMAVFHYIPLHGCPAGEHFGEFHGEDRYTTKESERLLRLPLFYNLSPVNQRTVIATLLNYFS | Function: Catalyzes the synthesis of dTDP-4-amino-4,6-dideoxy-D-galactose (dTDP-Fuc4N) from dTDP-4-keto-6-deoxy-D-glucose (dTDP-D-Glc4O) and L-glutamate.
Catalytic Activity: 2-oxoglutarate + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + L-glutamate
Sequence Mass (Da): 41901
Sequence Length: 376
Pathway: Bacterial outer membrane biogenesis; enterobacterial common antigen biosynthesis.
EC: 2.6.1.59
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Q84LH3 | MSSSNWIDDAFTEEELLAIDAIEASYNFSRSSSSSSSAAPTVQATTSVHGHEEDPNQIPNNIRRQLPRSITSSTSYKRFPLSRCRARNFPAMRFGGRILYSKTATEVDKRAMQLIKVLDTKRDESGIAFVGLDIEWRPSFRKGVLPGKVATVQICVDSNYCDVMHIFHSGIPQSLQHLIEDSTLVKVGIGIDGDSVKLFHDYGVSIKDVEDLSDLANQKIGGDKKWGLASLTETLVCKELLKPNRIRLGNWEFYPLSKQQLQYAATDAYASWHLYKVLKDLPDAVSGS | Function: Exonuclease that digests recessed strands of DNA duplexes in the 3' to 5' direction but hardly single-stranded DNA or blunt-ended duplexes. Also able to digest 3'-protruding strands and 3'-recessed strand termini of duplexes containing mismatched bases.
Sequence Mass (Da): 32090
Sequence Length: 288
Subcellular Location: Nucleus
EC: 3.1.-.-
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Q077R2 | MELVSIIIAAYNCKDTIYATVESALSQTYKNIEIIICDDSSTDDTWDIINKIKDSRIICIKNNYCKGAAGARNCALKIAKGRYIAFLDSDDYWVTTKISNQIHFMETEKVFFSYSNYYIEKDFVITGVFSSPPEINYGAMLKYCNIACSTVILDRTGVKNISFPYIDKEDYALWLNILSKGIKARNTNLVDTYYRVHAGSVSANKFKELIRQSNVLKSIGIKAHHRIICLFYYAINGLIKHCFSYRDKRNA | Function: Catalyzes the addition of Glc, the second sugar moiety of the O56-antigen repeating unit, to GlcNAc-pyrophosphate-undecaprenol.
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UDP-alpha-D-glucose = beta-D-Glc-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28706
Sequence Length: 251
Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.305
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Q5R9R3 | MAGAIIENMGTKKLCIVGGILLVFQIIAFLVGGLIAPGPTTAVSYMSVKCVDARKNHHKTKWFVPWGPNHCDKIRDIEEAIPREIEANDIVFSVHIPLPHMEMSPWFQFMLFILQLDIAFKLNNQIRENAEVSMDVSLAYRDDAFAEWTEMAHERVPRKLKCTFTSPKTPEHEGRYYECDVLPFMEIGSVAHKFYLLNIRLPVNEKKKINVGIGEIKDIRLVGIHQNGGFTKVWFAMKTFLTPSIFIIMVWYWRRITMMSRPPVLLEKVIFALGISMTFINIPVEWFSIGFDWTWMLLFGDIRQGIFYAMLLSFWIIFCGEHMMDQHERNHIAGYWKQVGPIAVGSFCLFIFDMCERGVQLTNPFYSIWTTDIGTELAMAFIIVAGICLCLYFLFLCFMVFQVFRNISGKQSSLPAMSKVRRLHYEGLIFRFKFLMLITLACAAMTVIFFIVSQVTEGHWKWGGVTVQVNSAFFTGIYGMWNLYVFALMFLYAPSHKNYGEDQSNGDLGVHSGEELQLTTTITHVDGPTEIYKLTRKEAQE | Function: Regulates Wnt proteins sorting and secretion in a feedback regulatory mechanism. This reciprocal interaction plays a key role in the regulation of expression, subcellular location, binding and organelle-specific association of Wnt proteins. Also plays an important role in establishment of the anterior-posterior body axis formation during development (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62223
Sequence Length: 541
Subcellular Location: Golgi apparatus membrane
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P43446 | MSSHDISWHSPASVYFSSDLDVKRIAGKLRGCWTDLLLRQESCCERVLQKSSSSMDYFLFRLFCSLALASLLVQRADSNEILGLKIPFDPILNANTVCLTLPGLTKKQLDVCMRNPDVTASAIQGIQIAIHECQHQFRGHRWNCSSLETRNKIPYESVVFSRGFRESAFAYAIAAAGVVHAVSNACAMGKLKACGCDEKRRGDEEALRIKLNRLQLEAINRGKGMVHGVMEHFPAEALGPQDSWEWGGCSPNVEYGERFSKDFLDSRETYRDIHSRMRLHNNRVGRQVVVDHMRRKCKCHGTSGSCQLKTCWQVTPEFRTVGSLLKERLNVATLIKAHNRNTGQVENAHHTHRRRANINDLVYFEKSPDFCERDLGSDSAGTQGRICNKTSQGMDNCESLCCGRGHNILQQTRSERCNCKFHWCCYVVCEECRITEWVSVCK | Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Required for normal tooth development . Regulates the expression of genes involved in tooth development .
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 50047
Sequence Length: 442
Subcellular Location: Secreted
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Q9GZT5 | MGSAHPRPWLRLRPQPQPRPALWVLLFFLLLLAAAMPRSAPNDILDLRLPPEPVLNANTVCLTLPGLSRRQMEVCVRHPDVAASAIQGIQIAIHECQHQFRDQRWNCSSLETRNKIPYESPIFSRGFRESAFAYAIAAAGVVHAVSNACALGKLKACGCDASRRGDEEAFRRKLHRLQLDALQRGKGLSHGVPEHPALPTASPGLQDSWEWGGCSPDMGFGERFSKDFLDSREPHRDIHARMRLHNNRVGRQAVMENMRRKCKCHGTSGSCQLKTCWQVTPEFRTVGALLRSRFHRATLIRPHNRNGGQLEPGPAGAPSPAPGAPGPRRRASPADLVYFEKSPDFCEREPRLDSAGTVGRLCNKSSAGSDGCGSMCCGRGHNILRQTRSERCHCRFHWCCFVVCEECRITEWVSVCK | Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). Plays a role in normal ectoderm development . Required for normal tooth development . Required for normal postnatal development and maintenance of tongue papillae and sweat ducts . Required for normal proliferation of basal cells in tongue filiform papillae, plantar epithelium and sweat ducts. Required for normal expression of keratins in tongue papillae (By similarity). Required for normal expression of KRT9 in foot plant epithelium . Required for normal hair follicle function .
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 46444
Sequence Length: 417
Subcellular Location: Secreted
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P70701 | MGSAHPRPWLRLPQGPQPRPEFWALLFFLLLLAAAVPRSAPNDILGLRLPPEPVLNANTVCLTLPGLSRRQMEVCVRHPDVAASAIQGIQIAIHECQHQFRDQRWNCSSLETRNKVPYESPIFSRGFRESAFAYAIAAAGVVHAVSNACALGKLKACGCDASRRGDEEAFRRKLHRLQLDALQRGKGLSHGVPEHPAILPASPGLQDSWEWGGCSPDVGFGERFSKDFLDSREPHRDIHARMRLHNNRVGRQAVMENMRRKCKCHGTSGSCQLKTCWQVTPEFRTVGALLRNRFHRATLIRPHNRNGGQLEPGPAGAPSPAPGTPGLRRRASHSDLVYFEKSPDFCEREPRLDSAGTVGRLCNKSSTGPDGCGSMCCGRGHNILRQTRSERCHCRFHWCCFVVCEECRITEWVSVCK | Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt/beta-catenin signaling pathway. Plays a role in normal ectoderm development. Required for normal tooth development. Required for normal postnatal development and maintenance of tongue papillae and sweat ducts. Required for normal proliferation of basal cells in tongue filiform papillae, plantar epithelium and sweat ducts. Required for normal expression of keratins in tongue papillae. Required for normal expression of KRT9 in foot plant epithelium. Required for normal hair follicle function.
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 46454
Sequence Length: 417
Subcellular Location: Secreted
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P28131 | SGSCQLKTCWQVTPEFRVVGNLLKERFYGATLIKPHNRNTGQLDHSHIPHRRRTSINSLVYFEKSPDFCEREPQLDSTGTQGRICNKTSPGMDNCESLCCGRGHNILRQTPSERCNCKF | Function: Ligand for members of the frizzled family of seven transmembrane receptors. Required for normal tooth development. Regulates the expression of genes involved in tooth development.
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 13570
Sequence Length: 119
Subcellular Location: Secreted
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Q801F7 | MELPHRQCLGRVLIVTAALLSPAFTVLGNDILGLKVAGEPVLTPNAVCLRLAGLTKKQMRLCVRSPDVTASALQGIQVAIHECQHQLRDQRWNCSSLENHGKLPHQSAILNRGFRESAFSLSLLAAGVVHSVASACSLGKLRGCGCEAKRRLDDDKIRLKLTQLQLQTFQRSGVSLAGAGENTPELSSLHGSLPANLHSSHPMSLLKPLPDEVTMLQDTWEWGGCSHDIRFGVRFSRDWLDSRGSPRDIHARTRIHNNRVGRQVVTDNMRRKCKCHGTSGSCQFKTCWYVSPEFRLVGSLLREKFLTAIFINSQNKNNGVFNSRTGGSTGSDPLRGQRRRSISRELVYFEKSPDFCDREPAVDSLGTQGRICNKSSPGMDGCGSLCCGRGHNILKQARSERCHCRFHWCCYVLCEECKVTEWVNVCK | Function: Member of the Wnt ligand gene family that encodes for secreted proteins, which activate the Wnt signaling cascade. Involved in neurogenesis. Performs a partially redundant function with wnt1 in the formation of the midbrain-hindbrain boundary (MHB) organizer.
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 47407
Sequence Length: 427
Subcellular Location: Secreted
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P48614 | MLEEPRSRPPPLGLAGLLFLALFSRALSNEILGLKLPGEPPLTANTVCLTLSGLSKRQLGLCLRSPDVTASALQGLHIAVHECQHQLRDQRWNCSALEGGGRLPHHSAILKRGFRESAFSFSMLAAGVMHAVATACSLGKLVSCGCGWKGSGEQDRLRAKLLQLQALSRGKTFPISQPSPVPGSVPSPGPQDTWEWGGCNHDMDFGEKFSRDFLDSREAPRDIQARMRIHNNRVGRQVVTENLKRKCKCHGTSGSCQFKTCWRAAPEFRAIGAALRERLSRAIFIDTHNRNSGAFQPRLRPRRLSGELVYFEKSPDFCERDPTLGSPGTRGRACNKTSRLLDGCGSLCCGRGHNVLRQTRVERCHCRFHWCCYVLCDECKVTEWVNVCK | Function: Member of the Wnt ligand gene family that encodes for secreted proteins, which activate the Wnt signaling cascade. Specifically activates canonical Wnt/beta-catenin signaling and thus triggers beta-catenin/LEF/TCF-mediated transcriptional programs. Involved in signaling networks controlling stemness, pluripotency and cell fate decisions. Acts in the immune system, mammary gland, adipose tissue, bone and skin.
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 43119
Sequence Length: 389
Subcellular Location: Secreted
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P49893 | MAPTRHWVTPLLLLCCSGICGAIQWLGLTVNGSRVAWNESEHCRLLDGLVPDQSQLCKRNLELMQSVVNAAKQTKLTCQMTLSDMRWNCSSVENAPSFTPDLSKGTRESAFVYALASATLSHTIARACASGELPTCSCGATPAEVPGTGFRWGGCGDNLHYGLNMGSAFVDAPMKSSKSAGTQATKIMNLHNNAVGRQVLMDSLETKCKCHGVSGSCSVKTCWKGLQDLPHIANELKSKYLGATKVIHRQTGTRRQLVPRELDIRPVRESELVYLVSSPDYCTKNPKLGSYGTQDRLCNKTSVGSDSCNLMCCGRGYNAYTETIVERCQCKYHWCCYVMCKKCERTVERYVCK | Function: Ligand for the frizzled7 transmembrane receptor. Primarily acts via non-canonical Wnt pathways mediated by either Ca(2+) and PKC, or by JNK and dvl2/dsh. Depending on the cellular context, can also signal via the canonical Wnt pathway mediated by beta-catenin and dvl2/dsh. May also inhibit canonical Wnt signaling. Maternally initiates dorsal/ventral axis formation by a canonical route, which signals via lrp6. In a complex with wnt5a, activates the canonical and non-canonical processes involved in axis formation. In the non-canonical pathway, acts through fzd7/fz7 to induce phosphorylation of dvl2/dsh. Signals through a non-canonical Wnt pathway to regulate convergent extension movements during gastrulation. Interactions with the secreted Wnt antagonist sfrp5 to coordinate foregut development, acting via a non-canonical Wnt pathway whereby sfrp5 restricts wnt11b activity to prevent inappropriate foregut formation. Mediates cardiogenesis via non-canonical Wnt signaling involving JNK-activation and PKC. Acts redundantly with wnt11/wnt11r during pronephros induction.
PTM: Glycosylation is required for protein secretion.
Sequence Mass (Da): 38785
Sequence Length: 353
Subcellular Location: Secreted
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P31283 | QECKCHVSGSCTLRTCWRALSDFRRTGDYLRRRMNGAVQVMATQDGANFTSARQGYRRATRTDLVYFDNSPDYCVLDKAAGSLGTAGRVCSKTSKGTDGCEIMCCGRGYDTTRVTRVTQCECKFHWCC | Function: Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt/beta-catenin signaling pathway.
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 14312
Sequence Length: 128
Subcellular Location: Secreted
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A0A7J6K7Y0 | MPEQDLASGFLLRFQNARPVCLSVGSFVSFRTVQPRKMRDRGWRCVWHRMAGVGALFGIFGVLCTVEAGATVAAPQVETGPLLSVRAPRSPLHLRDVDAPEVTHASSEGSPQFESSLSQQRLRRPADRGEAHNGEEPRKDAATQTVRGYGGQSTEPPPASIVPVSSEAPQDGAEQRQASSAAESLAGLDPDAGDTGLRSQEMDEEGSGAAQDMERAHAAQPTVSTWDDAHLVQVSTSHPDMFPVDGSFSKKQEGRRERRLAVRGDDSFARGHNRDRDASNGRSILRRAPGWAKIAALATGLLVSAFGYSSYKHGGPRVALRIHKLHLKRKLPISWRRYLNNLPVLDERLFPEFEDILPWLRRGARLVKRVPHVSEALADFIGLDEETRRTGIVIKVKSSTDAEARRLVYEVNAHANMVPDNPFFLPIIGAYQGASKRAVYMILPRARADVADYVRARPYDVDVRLAAAEMVYSNYILHTHGFLHRDIKAHNYFVTFDGHVVLADFEGVGVLQQRTPVVGTRGYFAPELSRATDHTEKSDVFALGQTLKRLVKYMRPTVRVPHLRELWALTKRMTAKDPEERPTLKQVMEDPYFDGIDFERLEAKDQGVPFRGDFSIDDPDAGGKMYIPPSKEQDHEQENE | Function: Serine/threonine-protein kinase which, at the tachyzoite stage, phosphorylates several parasitophorous vacuole (PV)-resident proteins such as GRA2, GRA6 and GRA7 . By phosphorylating GRA2 and GRA6, regulates the formation of a functional intravacuolar network (IVN); IVN is composed of membranous tubules that bud from the PV membrane into the vacuolar lumen . Plays a role in the establishement of chronic infection in the host by controlling cyst formation in the host tissues .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 71272
Sequence Length: 640
Domain: The protein kinase domain has an atypical kinase fold which lacks the glycine-rich loop that is critical for ATP binding in canonical protein kinase domains.
Subcellular Location: Cytoplasmic granule
EC: 2.7.11.1
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A0A7J6K7I9 | MMFPAVAAPPRRLPGERLQRSQNPVETSWLSFRILATRGPCVTSTFLFLTVAFLGLSWVSVAVAAHAEHPEDSATNFLFSFAENSLANREPPEDSAARPSSRSGGAERRRLDSLIPGFLKRRRIFKQLRPVDEFQLREFQEASSKVKAQFFSAGHSKVTFVDRPSAALLSFLHLEEEDVPYGVVIKAIPYDAFDFYESVAEPYIHRMFDDPRKFPYVVPVLAALRSTSKRVLYLVLPLYRELPETVDEEARSLDFVLLLAEMAMAVCQLHERNLAHRDLKEDNFLVSPEGHIVVSDLATLDITDNKSFLIGTSGYMPPETRSSYLLRKGYKRSRYGEKTDVYSLGVAFRHLAFMLEGLGVQVPHRTQLAKLIKKMTSPDPEKRPLIGEVMEDPFFASVDFRLVRQRAGKHPFKKLPGADLLAERQRARLEAREKADAAAKAADNAEVPAAKSPAGKTGGAGTLSGDRDRAGSGEKPAERAEEEKGRGRGAQTHEGNHDRTDDAGREELREGPGDQKPSGEENREGGQPPGQREEQREGTGLEEGFNKEDAQES | Function: Probable serine/threonine-protein kinase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 61601
Sequence Length: 553
Domain: The protein kinase domain has an atypical kinase fold which lacks the glycine-rich loop that is critical for ATP binding in canonical protein kinase domains.
Subcellular Location: Cytoplasmic granule
EC: 2.7.11.1
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Q8RXE5 | MEEADFVQKDPTGRYIRYNDVLGRGAFKTVYKAFDEVEGIEVAWNLMSIEDVLQMPGQLDRLYSEVHLLNSLKHDNIIKLFYSWVDDHNKSINMITELFTSGSLTLYRKKHRKVDPKAIMNWARQILKGLHYLHSQTPPVIHRDLKCDNIFVNGNTGKVKIGDLGLAAVMQQPTARSVIGTPEFMAPELYEEEYNELVDIYSFGMCMLEMVTCEYPYRECRNQAQIYKKVTSGIKPQSLSKVDDPQVKQFIEKCLLPAPSRPTALELLKDQLLAVDGAKDSTLTASSNTTFKPAMPPQCEYRPMDVEYKKNTSVSICSSAKSSQECALLQTMEVQRVAESTEFKLSGERRDDVAASMALRIAGSSGQARKVDFDFNLKTDTARAVTGEMVEELDLSSHEVTVIAEMIDELIMKLKANRSLPNANSVYQSKDEEAGESMKSEISADYYHRVSSNEGSRLGCCCEAVESLLSSFLDSCSMVSNKQSEDLKTELNVIESQYNQSCQRLLRMKEEAIEKAKRKWMKLS | Function: May regulate flowering time by modulating the photoperiod pathway.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 59246
Sequence Length: 524
EC: 2.7.11.1
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Q6ICW6 | MMTCASSDDNESEKDKDSESFVEVDPTGRYGRYGELLGSGAVKKVYRAFDQEEGIEVAWNQVKLRCFSDDPAMTERLYSEVRLLKNLKNSNIITLYKVWRDERNNTLNFITEICTSGNLREYRKKHRHVSMRALKKWSKQILKGLDYLHTHDPCIIHRDLNCSNIFVNGNIGQVKIGDLGLAAIVGKNHLAHSILGTPEFMAPELYEENYTEMVDIYSYGMCVLELVSLEIPYSECDSVAKIYKRVSKGLKPEALNKVNDPEAKAFIEKCIAQPRARPSAAELLCDPFFDGILDDDDEDGENNDNNGAGRIVVS | Function: May regulate flowering time by modulating the photoperiod pathway.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 35531
Sequence Length: 314
EC: 2.7.11.1
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Q9CAV6 | MNNLSYLEPDYSEFVEVDPTGRYGRYNEVLGKGASKTVYRAFDEYEGIEVAWNQVKLYDFLQSPEDLERLYCEIHLLKTLKHKNIMKFYTSWVDTANRNINFVTELFTSGTLRQYRLRHKRVNIRAMKHWCRQILRGLHYLHSHDPPVIHRDLKCDNIFVNGNQGEVKIGDLGLAAILRKSHAAHCVGTPEFMAPEVYEEAYNELVDIYSFGMCILEMVTFDYPYSECTHPAQIYKKVMSGKKPDALYKVKDPEVKCFIEKCLATVSLRVSARELLDDPFLRIDDGEFDLRSVDMEDSVGPLYRQPHHLPDYYNYPSNSSSLNRQYSNGNYPSNSSSLNRQYSNGYNSHHEYQNGWAYNPAETEETHGIELFESRNNDDQEEEKKSGNVDITIKGKRRDDGGLFLRLRIADKEGRVRNIYFPFDIETDTALSVATEMVAELDMDDHGVTKIANMIDGEISSLVPSWRPGPEFEECLAAAAAANAASICNNCVSNRTSMGSVMDFLRTNPGANVIQCCRNGCGETHGRFEEITIRETEVRLRELWKLQQQQESRELSSIDSGHNHSEEEEEEEVLYEDPENMFSCEAGNEINHISGSGSFSFMPSKYCDEPSEKTENQVQQELRWLKAKCQIELRDIQDEQLKTRWPESGEEVEISPKDGFLGSVSGLGREEDTVKEMFGERLVPKCLKRTTSLPVDAIDS | Function: Regulates flowering time by modulating the photoperiod pathway. Phosphorylates APRR3.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 80208
Sequence Length: 700
EC: 2.7.11.1
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Q9FMH6 | MAETETESITTSSPPPISETENSTTLPTTETEKNPNPVTISLRIWPPTQKTRDAVINRLIETLSTESILSKRFGSLESEEASSVAKSIEDEAYAIASATVFGDDDGIEILKAYSKEISKRMLESVKAKSNVASPPPKDGDGIESAVDSKIDSSEA | Function: Regulates the mitotic activity in roots. Plays a role with HSP70-1 in facilitating WIT1 nuclear envelope targeting.
Sequence Mass (Da): 16634
Sequence Length: 155
Domain: The WPP domain is required for the nuclear envelope localization.
Subcellular Location: Nucleus envelope
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Q9C500 | MAETAETINTTISSPPPESESSTTISAMTDPTSQEAASKDTDLTKEAESEKKPGGISLRIWPPTQKTRDAVLNRLIETLSTESILSKRYGTLKSDDATTVAKLIEEEAYGVASNAVSSDDDGIKILELYSKEISKRMLESVKARSNASVGNGSVEDANTDASEVSKDDAGPASEEEKSEA | Function: Regulates the mitotic activity in roots. Plays a role with HSP70-1 in facilitating WIT1 nuclear envelope targeting.
Sequence Mass (Da): 19134
Sequence Length: 180
Domain: The WPP domain is required for the nuclear envelope localization.
Subcellular Location: Nucleus envelope
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P54423 | MKRRKFSSVVAAVLIFALIFSLFSPGTKAAAAGAIDQAAALENGKEQTGAMKEPEQVKWYKVTPGATDIQKNSHMALTVKSDSVLNVSVYPSKEKALKDETFEMYRSFTAEDGKSEVIFPYAWSGPYYVKVEYLGEEEPEDGGTAEAAAEAKYTIGYKGTKKQPSDLEEEEACPVEMSVDQKKSGKGILDKLRSIRDEQLSQTAEGKELTSLYYKAAPFIVAKLALNKTARNEIYQDLVTLKPLFDDVSENGASSSYKVTEKDQKAINRLYDKALQSVPSFLKEEIKKQADRLNMKQLQGKTAGAILTENNIAAKSEVQTTKVIFKVKDNKSLSSVHNEMKGFSASAQSKKDISNVKKAKKLFDNLYSFELPKDEKQNGAYTASAKRVKSAAATLSKMSNVEFAEPVQEYKSLANDIQYPYQWPLKNNGENGGVKNADVKYEPANTLLSKRKLNDTLIAVVDTGVDSTLADLKGKVRTDLGHNFVGRNNNAMDDQGHGTHVAGIIAAQSDNGYSMTGLNAKAKIIPVKVLDSAGSGDTEQIALGIKYAADKGAKVINLSLGGGYSRVLEFALKYAADKNVLIAAASGNDGENALSYPASSKYVMSVGATNRMDMTADFSNYGKGLDISAPGSDIPSLVPNGNVTYMSGTSMATPYAAAAAGLLFAQNPKLKRTEVEDMLKKTADDISFESVDGGEEELYDDYGDPIEIPKTPGVDWHSGYGRLNVMKAVSAADLQLKVNKLESTQTAVRGSAKEGTLIEVMNGKKKLGSAKAGKDNAFKVNIATQKQDQVLYLKATKGDAKTSYKVVVVKGKPSGTPKVNAVKTKDTAVKGKANSKAMIRVKNKSKKVIASAKADAKGTFSVKIKKQKAGTVLYVTAVDTDKKESKEAKVVVEK | Function: CWBP52 is a serine-type protease that could be involved in proteoglycan peptide bridges.
PTM: Proteolytically cleaved to yield CWBP23 and CWBP52.
Sequence Mass (Da): 96488
Sequence Length: 894
Subcellular Location: Secreted
EC: 3.4.21.-
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P50902 | QGYSTVAFDGPPSYGHAPSHHAAQFSNHSFKHEDPIAQQTSLGDQQYSVPPPVYGCHTPTDSCTGSQALLLRTPYNSDNLYQMTSQLECMTWNQMNLGSTLKGHATGYENENHTAPMLYSCGAQYRIHTHGVFRGIQDVRRVPGVAPTIVRSASETNEKRPFMCAYPGCNKRYFKLSHLQMHSRKHTGEKPYQCDFKDCERRFSRSDQLKRHQRRHTGVKPFQCKTCQRKFSRSDHLKTHTRTHTGKTSEKPFSCRWPSCQKKFARSDELVRHHNMHQRNMTKLQLAL | Function: Transcription factor that plays an important role in cellular development and cell survival. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'. Regulates the expression of numerous target genes. Plays an essential role for development of the urogenital system. It has a tumor suppressor as well as an oncogenic role in tumor formation. Function may be isoform-specific: isoforms lacking the KTS motif may act as transcription factors. Isoforms containing the KTS motif may bind mRNA and play a role in mRNA metabolism or splicing.
Sequence Mass (Da): 33111
Sequence Length: 288
Domain: Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3' via its C2H2-type zinc fingers. Starting from the N-terminus, the second zinc finger binds to the 3'-GCG motif, the middle zinc finger interacts with the central TGG motif, and the C-terminal zinc finger binds to the 5'-GCG motif. Binds double-stranded target DNA, irrespective of the cytosine methylation status. Has reduced affinity for target DNA where the cytosines have been oxidized to 5-hydroxymethylcytosine, 5-formylcytosine or 5-carboxylcytosine.
Subcellular Location: Nucleus speckle
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P19544 | MGSDVRDLNALLPAVPSLGGGGGCALPVSGAAQWAPVLDFAPPGASAYGSLGGPAPPPAPPPPPPPPPHSFIKQEPSWGGAEPHEEQCLSAFTVHFSGQFTGTAGACRYGPFGPPPPSQASSGQARMFPNAPYLPSCLESQPAIRNQGYSTVTFDGTPSYGHTPSHHAAQFPNHSFKHEDPMGQQGSLGEQQYSVPPPVYGCHTPTDSCTGSQALLLRTPYSSDNLYQMTSQLECMTWNQMNLGATLKGVAAGSSSSVKWTEGQSNHSTGYESDNHTTPILCGAQYRIHTHGVFRGIQDVRRVPGVAPTLVRSASETSEKRPFMCAYPGCNKRYFKLSHLQMHSRKHTGEKPYQCDFKDCERRFSRSDQLKRHQRRHTGVKPFQCKTCQRKFSRSDHLKTHTRTHTGKTSEKPFSCRWPSCQKKFARSDELVRHHNMHQRNMTKLQLAL | Function: Transcription factor that plays an important role in cellular development and cell survival . Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3' . Regulates the expression of numerous target genes, including EPO. Plays an essential role for development of the urogenital system. It has a tumor suppressor as well as an oncogenic role in tumor formation. Function may be isoform-specific: isoforms lacking the KTS motif may act as transcription factors . Isoforms containing the KTS motif may bind mRNA and play a role in mRNA metabolism or splicing . Isoform 1 has lower affinity for DNA, and can bind RNA .
Sequence Mass (Da): 49188
Sequence Length: 449
Domain: Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3' via its C2H2-type zinc fingers. Starting from the N-terminus, the second zinc finger binds to the 3'-GCG motif, the middle zinc finger interacts with the central TGG motif, and the C-terminal zinc finger binds to the 5'-GCG motif. Binds double-stranded target DNA, irrespective of the cytosine methylation status. Has reduced affinity for target DNA where the cytosines have been oxidized to 5-hydroxymethylcytosine, 5-formylcytosine or 5-carboxylcytosine.
Subcellular Location: Nucleus
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O62651 | MGSDVRDLNALLPAVPSLGGGGGCALPVSGAAEWAPVLDFAPPGASAYGSLGGPAPPPAPPPPPPPPPHSFIKQEPSWGGAEPHEEQCLSAFTVHFSGQFTGTAGACRYEPFGPPPPSQASSGQARMFPNAPYLPSCLESQPAIRNQGYSTVTFDGTPSYGHTPSHHAAQFPNHSFKHEDPMGQQGSLGEQQYSVPPPVYGCHTSTDSCTGSQALLLRTPYSSDNLYQMTSQLECMTWNQMNLGATLKGVAAGTSSSMKWTEGQSNHGAGYESDSHATPILCGAQYRIHTHGVFRGIQDVRRVPGVAPTLVRSASETSEKRPFMCAYPGCNKRYFKLSHLQMHSRKHTGEKPYQCDFKDCERRFSRSDQLKRHQRRHTGVKPFQCKTCQRKFSRSDHLKTHTRTHTGKTSEKPFSCRWPSCQKKFARSDELVRHHNMHQRNMSKLQLAL | Function: Transcription factor that plays an important role in cellular development and cell survival. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'. Regulates the expression of numerous target genes, including EPO. Plays an essential role for development of the urogenital system. It has a tumor suppressor as well as an oncogenic role in tumor formation. Function may be isoform-specific: isoforms lacking the KTS motif may act as transcription factors. Isoforms containing the KTS motif may bind mRNA and play a role in mRNA metabolism or splicing. Isoform 1 has lower affinity for DNA, and can bind RNA.
Sequence Mass (Da): 49166
Sequence Length: 449
Domain: Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3' via its C2H2-type zinc fingers. Starting from the N-terminus, the second zinc finger binds to the 3'-GCG motif, the middle zinc finger interacts with the central TGG motif, and the C-terminal zinc finger binds to the 5'-GCG motif. Binds double-stranded target DNA, irrespective of the cytosine methylation status. Has reduced affinity for target DNA where the cytosines have been oxidized to 5-hydroxymethylcytosine, 5-formylcytosine or 5-carboxylcytosine.
Subcellular Location: Nucleus speckle
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Q96WS1 | MNSNYVPLTSSVDVEEKMESENGVDLGNDIDLEKGLPLKYNSENESGLPSNSASSYLINPDPTMDLEAQTFNHNESTTSVGHDNSNSPPKCRKTCSSNKVYSNEVPLLFVFVISISIVCIFDLVIFGCLQYNMVSMDDLHVMQRLSWFCASLALLFILMRYYDFWTKACKDGIKHIFKKWKNTPLAFLQVLIFNIIGFFVRKGLKDSFGEQWGLKTSLFAHVSFATMSIFIFIFETLKPGSCSVDWIARILKAVVYFLEDSDEL | Function: May act in meiotic drive.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29937
Sequence Length: 264
Subcellular Location: Membrane
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O74512 | MENNHHLAKDSLDELNPKRGKGEHETQVSQYTVVEEATIPQSLVKTSRPADHKVMEASKVADTRTAWSTKIPAVLLPVFVINIALFKYLVFANFSTKDRVLFGLGNGGINIFSMWLLLATYETWFRSIKEVIVACGAGIRSFPQKRGVNMLYAILKLTFVNAFAIPLLMFFRSHFEQWRLGCPLVERVIGVMLNVAYFIIEIENPGLFTRVFNKYCDCLFAIRDILNRN | Function: May act in meiotic drive.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26109
Sequence Length: 229
Subcellular Location: Endoplasmic reticulum membrane
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G2TRU7 | MSNNYTSLSSSLDEEMGLKAGHEIDLEGSPPSEHNSEEKSTLPSNSDILTSANPVSQASETPDHSIESNTGSTQSPTSHSLLLKFSFCIVYYSYFAIVVLGCVLPFEHTHTFLIAFLVIFGIISVILFSGSIYYYETWTKTVKHFLKKVISPFKKEYIVCAFLKTFVFYGLLKTIEHFLVLLSGDKWGWKCSTLSSILTPVSCISFCLNESVQLRSCSTHLFINTVAWIKSLGGGKNAFENNYNQLNETSPEDLV | Function: May act in meiotic drive.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28404
Sequence Length: 255
Subcellular Location: Spore membrane
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Q94CT7 | MGHGLSCSRDTDEYDLFRAAQLGDIHALSALLAADPALARRATVYDRFTALHIAAANGRLQVLSMLLDRDGDVDVLSRKKQTPLMVAAMRGNTECVVRLLRGGANVLTFDSPRARTCLHHAAYYGHAECLQAILGAAAQAQGPVAASWGFARFVNVRDERGATPLHLAARHARASCVRLLLDKGAIVSAPTAVYGFPGSTALHLAARAGSMECIRELLAWGADRLQRDSAGRIAYAVAMRRGHRACAALLNPAAAEPIVWPSPLKFIGELEADAKALLEAALMEANREREKRILHGSDINIKGGDEEEESEDEEEACNICFEQACSMEVKECGHQMCAACTLAICCHSKPNPKTLLLHPPACPFCRTTISRLVVATTNSNKTNSRRRSRSRSSSFKGGLSSAMGSFSRIGRGSGRLVVDGSSVGELADKPDHDFSSVAAAAAICDT | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 47701
Sequence Length: 446
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q6NLQ8 | MRFLSLVGNSFGCSASGERLVSAARDGDLQEAKALLDYNPRLARYSTFGVRNSPLHYSAAQGHHEIVSLLVESGVDINLRNYRGQTALMQACQHGHWEVVLILILFGANIHRSDYLNGGTALHLAALNGHPRCIRILLSEYIPSVPNCWSLLKNKKTSVAGFDSSVLHEVINRAADGGITPLHVAALNGHIETVQLLLDLGASVTQVTVEDGTTIDLIGAGSTALHYASCGGNTQCCQLLISKGACLAAVNSNGWTPMMVARSWHRNWLEEILNPTTEQPQLHLPNVPSPFLCLPLMSIVNIAQECGWRENDCLTPCRDPCAVCLERKCTVAADGCAHEFCTNCALYLSTTSITSSKTSNVTPGSVPCPLCRNGIVSFTKLPHTTATTRTSTSSRTSISLSFCTCSSDVLDTALLTNPHYSCKPVVSRTGSRTPQSARSSAFRSLSCRRFPPSLCLGGSDVDEPRSRLIGGSYSRSGVGFRRSTSQVEGKRSWFSALNHCVTTGGSAC | Function: E3 ubiquitin-protein ligase that mediates ubiquitination of ACC synthases (ACS). Negatively regulates ethylene biosynthesis probably via ubiquitin-dependent degradation of ACS4 and ACS7 enzymes. Regulates lateral root formation and development by controlling ethylene production which inhibits lateral root formation at high concentration.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 54586
Sequence Length: 508
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q6KAE5 | MGFLSLVGNSFGCSASGERLVSAARDGDLQEARALLEYNPRLARYSTFGGRNSPLHYAAAQGHHEIVSLLLESGVEINLRNYRGQTALMQACQYGHWEVVQTLMLFNANVHRTDYLNGGSALHFAALHGHARCLRLVLADYVPSMPNFWNSMKDSLSEEGPSADLDEDGLFKMVNQKADGGLTPLHMAALNGHVECVQLLLDLGASVIEATIEDGTTIDLIGAGSTPLHYAACGGNAVCCQLLIARGASLSAQNASGWTPLMVARSWHRNSLEEILSKEPESRIRTVPSPYLCLPLMSIMSIAREFGWRYLNQSPVCIDPCAVCLEGSCSVAAEGCKHEFCTRCALYLCSTSYTSVSPAGAIPCPLCRHPIIAFTALPGTSPIRELPRNSLSLSFCTTCPAVNSDSTPSIASHLYRTEFQCARMPPMGSSSFRSLSCQRLPAMKLNPSFCMGAMDTNPCLIRCSRFGPSFRRSASQGESSRRAWPLTFDPIAATGS | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 53617
Sequence Length: 496
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q4FE45 | MGNSFGCSASGERLVSAARDGDFVEAKMLLDCNPCLAKYSTFGGLNSPLHFAAAKGHNEIVGLLLENGADVNSRNYCGQTALMQACRYGHWEVVQTLLLFRCNVTRADYLAGRTALHFAAVNGHARCIRLVLADFLPSDKLNSLPETGVVTAKNKSEQSALSKFVNKAADGGITALHMAALNGLFDCVQLLLDLEANVSAVTFHYGTSMDMIGAGSTPLHYAACGGNLKCCQILLARGARKMTLNCNGWLPIDIARMWSRHWLEPLLSPNSDVVIPAFPHSNYLSLPLLSILNIAREFGLQSATIGDEVDICAVCLERTCTVAAEGCEHQLCVRCALYLCSSSNVPSVTVGPPGSIPCPLCRHGITAFKRLPSSLTREMKLPMSLGFCAPCMLHTGDTTDQSSPTCPPTEQRSSKTRAASVSSDIFCPVTCSPFPSVNIPMCTCNEGTCPNFETHGTERHSEEHVESSPSRTTTEQEKIEEGQRLGKTTTCSSMFWGRRSCSRENQCNSEINA | Function: Possesses E3 ubiquitin-protein ligase activity when associated with the E2 enzyme UBC8 in vitro.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 55347
Sequence Length: 513
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q9FPH0 | MGQQQSQSKDEMLFQEVSNNNVEGIKSLHHEGAGLEGVDKLGRTPLILACTNDDLYDVAKTLLELGSNVNAYRSGCNGGTPLHHAAKRGLVHTVKLLLSHGANPLVLDDDVKTALEVARDEGYSNVVRAIESHICLFSGCMREYSGSSLLNLFAPQLLSRKVWVVVVPTGSRNPTKPLKLELVLYDSIQDAQPRMVIPLWKANLEEPKSFRCDDSVMIIDDSRSPKSMRQRRESGFISQARRWAQVDRQIRLKLAAEIKGDMKQMNWFSEACKGVPQPMNPPRFMKTSQATTTTTNVPALSDDALTRVAMSLPSPKTANKEDGLCVICVDAPSEAVCVPCGHVAGCISCLKEIENKKMGCPVCRANIDQVIKLYHV | Function: No E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 41383
Sequence Length: 376
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q7XI08 | MGLQQSKEELVYQQVNYGNADGIRALRAQGAGLEWIDKEGKTPLMVASMRPDLINVVQVLIELGANVNAYRPGSYCGTALHHAAKKGLEQTVHLLLSHGANPFITNDDCHTALDLAREKGHVNVVRAIEGRISLFCGWMRENYGPGFLEAFAPQFLTRKIWAVILPREARNQTRPLKLELTIYPELQASKPQAVIKLWKCQLEEPKFNQANPSVTIFDKGTRTRYKLLPVCEGDKQQLQWFYSACCGIPQVASMVPAQPANAPLPNPSSASSLPSVISTPSKEDAELAMAINASILSAIAEGVPDVQPITTTTATNDWGNPPSNSLNGWGPPDTSAPSKTSGQVPVVTSSSSTYNGWDVPGTSSGQSSSKHNKSQNSTFVVPQEALPSLPVPTAPPLAVGTFYDGPIQYPSIDSTPVDVTMPSADGGTAVSSAKPAENEGDAKPAESDANASNSGNTPPGTCVICLDAPVEGACIPCGHMAGCMSCLKDIESKKWGCPICRAKINQIIRLYAV | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 54729
Sequence Length: 513
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q4FE47 | MGQQQSKGELLYQQVSYGNSEGIRALHRDGGDLEWMDREGKTPLILACMNSELFDVAKTLIELGSNVNAYRPGRHAGTPLHHAAKRGLENTVKLLLSHGANPLVLNDDCQTPLEVARVKGFSNVVRAIEKHICLFSGWMREFYGPTFLDLFAPQLLSRRVWVVIVPTGSRNPTKPFKLELVVYASLQDAQPRTVMPLWKANLEEPKAKQSDTSVMIVDNSTIPSRRMKKRRVCASHGRRRPQVVRQTRLKFAPSTEGDSQQLKWFCDACKGIPQPMHPPVFLQAPPSAPPPPSEDGLAMGMNASLHTTMSDPSNLNHHSIGQASSSSGPSSSTAPPSGKASAFGFNSHGIGIVLESSPSAPPLTDDDIATVDDGPIHYPSIDSTPVDLPSAASLPASTEGERKEDGNTGTCAICLDAPSEAVCVPCGHVAGCMSCLKEIKSKNWGCPVCRAKIDQVIKLYRV | Function: No E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 50055
Sequence Length: 462
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q7EZ44 | MGLLGMVGDSFGCSATGERLVSAARDGDIQEAMALLELNPRLARYSTFGIRNSPLHYSAAKGHHEIVSLLIESGVDINLRNCRGQTALMQACLYGHWKVVQILVLFKANIHKKDCFSGATAIHFAALKGHTRCLRLLVADYVPSLPEFWSVMHAKCTDETNKEAFDAVALRRLINNKSDGGVTPLHLAALHGHAECVQLLLDLGASVSEVTINDGSTIDLIGSGSTPLHYAACGGSAVCCQLLVAAGANMRAQNTNGLTPLMVARSWHKSSVEGILTKRSEVPVRILPSSYLSLPLMSIVKIARECGWRKTSVSSVCHDPCAICLDTECTVSAEGCGHEFCTKCALYLCATASSSTSIRGVPGSIPCPLCRHTIVSFVRLTSTTPIKELPWTNKSLALCAAGASTGSKYAGPAAITSSKYAGSLHRRSEMRSLRSSSVDLGCSSFRTASSGKLSSIKLNCTGADETMPCLVNCFRPDVQRSSSYRERIRRYSQFS | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 53082
Sequence Length: 495
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q4JHE0 | MGNSLGCVGLGERLAAAAKDGDAAEAQRLLAANPGLARCTTFGNLNSPLHVAAAKGHHEIAALLLENGADVNARNIYGQTPLMQACRFGHWEVVQTLLVFRCNVWRVENLSGRTALHMAAAGGHVKCVRLLVADAAGDRDGYVNKAANGGVTALHLAALHGHVECVHLLIDERASLAAQTLPCAAPPMASIGAGSTPLHYAACGGEVKCCQILVSRGADRTAINCNGWLPIDAARIWGCNWLEHVLSPKSHLPIPKFPPSGYLSQPLPSLIAIAREQGLNLSSEVSDGFDEGADACAVCLERPCTVAAEGCDHELCVKCAMDLCSVIKSYDSAGIAGEIPCPLCRTGIASFRTTAAPPPPSLAGSPARRSRRNNSGGGGGEHEASNSGGSEKGYGSIDPDAGAVVPLYYAPPFAPSAILT | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 43457
Sequence Length: 420
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q65XV2 | MGHGVSCARTGDEHDFFRAAQLGDLDALAALLAADPSLARRATLYDRLSVLHIAAANGRIEVLSMFLDRGAPPDAVNRHKQTPLMLAAMHGKIDCVLKLLQADANILMFDSVHARTCLHHAAYYGHVDCLQAILAAAQTTPVADSWGFARFVNVRDDHGATPLHLAARQGRPGCVQVLLENGAIVSALTGSYGFPGSTSLHLAARSGNLDCIRKLLAWGADRLQRDSAGRIPYSVALKRNHGACAALLNPTSAEPMVWPSPLKFISELEPEAKALLEAALMEANREREKKILNGTKYSLPSPSPGDDSADDDACSEVSDTELCCICFDQACTIEVQDCGHQMCAPCTLALCCHNKPNPTTLTPPSPACPFCRGSISRLVVAQTRSACDPDKPSSLQLTRKRSRRSHNLSEGSSSFKGLPSAMGSFSKLGRGSSRMADSDSSNLDKPEHDL | Function: E3 ubiquitin-protein ligase required for full accumulation of the LRR receptor kinase XA21 and XA21-mediated disease resistance. Binding to XA21 may stabilize the receptor kinase and maintain its protein level. Autoubiquitinated in vitro.
PTM: Phosphorylated by XA21.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 48203
Sequence Length: 450
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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G5EE07 | MSNYPKRIYVLPARHVAAPQPQRMAPKRALPTEQVVAQLLGDDMGPSGPRKRERLNHLSQEEKMDRRKLKNRVAAQNARDKKKERSAKIEDVMRDLVEENRRLRAENERLRRQNKNLMNQQNESVMYMEENNENLMNSNDACIYQNVVYEEEVVGEVAPVVVVGGEDRRAFESAAFINEPQQWEQARSTSINNNISNQLRRMDSKKNNTISVDMYLTIISILCNHMDRNKKMDTSNKSSNISRAQAESSIDSLLATLRKEQTVMQRLVQADPCTHLQKRVKHFRRIP | Function: Required for transcriptional regulation of the unfolded protein response (UPR) in the endoplasmic reticulum (ER) under stressed conditions, acting downstream of ire-1, and also maintaining ER homeostasis via a negative feedback loop, in parallel with ER kinase pek-1 . May also regulate Golgi protein trafficking distal to the ER . Protects the host organism from the detrimental effects of mounting an innate immune response to microbes, such as the Gram-negative bacterium P.aeruginosa, probably by modulating the UPR .
PTM: Sumoylated . Sumoylation may negatively modulate the transcription of genes involved in the ER-stress-response .
Sequence Mass (Da): 33326
Sequence Length: 287
Subcellular Location: Nucleus
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P17861 | MVVVAAAPNPADGTPKVLLLSGQPASAAGAPAGQALPLMVPAQRGASPEAASGGLPQARKRQRLTHLSPEEKALRRKLKNRVAAQTARDRKKARMSELEQQVVDLEEENQKLLLENQLLREKTHGLVVENQELRQRLGMDALVAEEEAEAKGNEVRPVAGSAESAALRLRAPLQQVQAQLSPLQNISPWILAVLTLQIQSLISCWAFWTTWTQSCSSNALPQSLPAWRSSQRSTQKDPVPYQPPFLCQWGRHQPSWKPLMN | Function: Functions as a transcription factor during endoplasmic reticulum (ER) stress by regulating the unfolded protein response (UPR). Required for cardiac myogenesis and hepatogenesis during embryonic development, and the development of secretory tissues such as exocrine pancreas and salivary gland (By similarity). Involved in terminal differentiation of B lymphocytes to plasma cells and production of immunoglobulins . Modulates the cellular response to ER stress in a PIK3R-dependent manner . Binds to the cis-acting X box present in the promoter regions of major histocompatibility complex class II genes . Involved in VEGF-induced endothelial cell (EC) proliferation and retinal blood vessel formation during embryonic development but also for angiogenesis in adult tissues under ischemic conditions. Functions also as a major regulator of the UPR in obesity-induced insulin resistance and type 2 diabetes for the management of obesity and diabetes prevention (By similarity).
PTM: Acetylated by EP300; acetylation positively regulates the transcriptional activity of XBP1 isoform 2 . Isoform 2 is deacetylated by SIRT1; deacetylation negatively regulates the transcriptional activity of XBP1 isoform 2 .
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 28695
Sequence Length: 261
Domain: Isoform 1 and isoform 2 N-terminus domains are necessary for nuclear localization targeting. Isoform 1 C-terminus domain confers localization to the cytoplasm and is sufficient to impose rapid degradation (By similarity). Isoform 1 transmembrane signal-anchor domain is necessary for its own mRNA to be recruited to the endoplasmic reticulum (ER) which will undergo unconventional ERN1-dependent splicing in response to ER stress . Isoform 1 N-terminus and C-terminus regions are necessary for DNA-binding and weak transcriptional activity, respectively. Isoform 2 N-terminus and C-terminus regions are necessary for DNA-binding and strong transcriptional activity upon ER stress, respectively . Isoform 2 C-terminus region contains a nuclear exclusion signal (NES) at positions 186 through 208. Isoform 2 C-terminus region contains a degradation domain at positions 209 through 261 .
Subcellular Location: Endoplasmic reticulum
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Q5BG78 | MKLLALSLASLASAATITRRADFCGQWDTATAGNFIVYNNLWGQDNADSGSQCTGVDSANGNSVSWHTTWSWSGGSSSVKSYANAAYQFTATQLSSLSSIPSTWEWQYSTTDVVANVAYDLFTSSSIGGDSEYEIMIWLAALGGAGPISSTGSSIATVTLGGVTWNLYSGPNGSMQVYSFVASSTTESFSADLMDFINYLVENQGLSNSQYLTHVQAGTEPFTGSDATLTVSSYSVSVS | Function: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues. Specific for xyloglucan and does not hydrolyze other cell wall components. Active against tamarind xyloglucan.
Catalytic Activity: xyloglucan + H2O = xyloglucan oligosaccharides.
Sequence Mass (Da): 25150
Sequence Length: 239
Subcellular Location: Secreted
EC: 3.2.1.151
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Q4WBT4 | MLYPRNLALFSLLSLSSAAPSQVERSPDAVLKPRAVCTPTAGGSPSIDDVPAIRKAIASCGNGGTIVFPAGSTYYLNSVLDLAGCSNCDIQVEGVLKFSGSTEYWGGKTAMLNIDMINGLRLRSLTGSGVIDGNGQNAYDRFASDKNYKRPTLLYITGGSNIEVSGLRQKNPPNVFNSVKGDTQHVTFKNLRMDATSNSQNPPKNTDGFDIGASTHVTISSVSVTNDDDCVAFKPGSNYVTVEDVTCTGSHGISVGSLGKSGPDVVQNILAHRITMIESTKAAGIKTYPSGNGHGLSTVKNVTFSDFNVRGCDYAFQIESCYGESESYCESNPGNAILQGIVVKGFSGTTSGKYDPVVANLNCGARGTCDVSMSAFSVKAPSGKATVLCDNTPSSLGVSCTSGASG | Function: Pectinolytic enzyme involved in the degradation of xylogalacturonan (xga), a galacturonan backbone heavily substituted with xylose, and which is one important component of the hairy regions of pectin. Activity requires a galacturonic acid backbone substituted with xylose (By similarity).
Sequence Mass (Da): 42267
Sequence Length: 406
Subcellular Location: Secreted
EC: 3.2.1.-
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A0KNR2 | MPKKFYVSWDNLQREARRLARRQLPVSQWKGIIAVSRGGLVPAALMARELGIRNVETLCISSYDHNNQRDLVVVKAATTAGDGEGWLVVEDLVDTGTTAKAIRELYPKAKFIAIFAKPMGEQLLDDFEVAIPQDTWIEQPWDMALEFATPICDEE | Function: Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine.
Catalytic Activity: diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate + guanine
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17447
Sequence Length: 155
Pathway: Purine metabolism; GMP biosynthesis via salvage pathway; GMP from guanine: step 1/1.
Subcellular Location: Cell inner membrane
EC: 2.4.2.-
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P55808 | MESWWGLPCLAFLCFLMHARGQRDFDLADALDDPEPTKKPNSDIYPKPKPPYYPQPENPDSGGNIYPRPKPRPQPQPGNSGNSGGYFNDVDRDDGRYPPRPRPRPPAGGGGGGYSSYGNSDNTHGGDHHSTYGNPEGNMVAKIVSPIVSVVVVTLLGAAASYFKLNNRRNCFRTHEPENV | PTM: O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 19723
Sequence Length: 180
Subcellular Location: Cell membrane
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P39798 | MQQEADVNVFQQDLADMKGEHKALEQRVSALERVSDRQDQQIMTLNEKLNKIEENTTWIKRTITGAIITAVSTGIIGGAIAIMYSLLQH | Function: Associated with cell lysis upon induction of PbsX.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9997
Sequence Length: 89
Subcellular Location: Cell membrane
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Q99163 | MNTFDKGTVIRTVLLLIALINQTMLMLGKSPLDIQEEQVNQLADALYSAGSIAFTIGTTLAAWFKNNYVTEKGKKQRDLLRDNNLTK | Function: Involved in cell lysis upon induction of PbsX.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9731
Sequence Length: 87
Subcellular Location: Membrane
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P98170 | MTFNSFEGSKTCVPADINKEEEFVEEFNRLKTFANFPSGSPVSASTLARAGFLYTGEGDTVRCFSCHAAVDRWQYGDSAVGRHRKVSPNCRFINGFYLENSATQSTNSGIQNGQYKVENYLGSRDHFALDRPSETHADYLLRTGQVVDISDTIYPRNPAMYSEEARLKSFQNWPDYAHLTPRELASAGLYYTGIGDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNLNIRSESDAVSSDRNFPNSTNLPRNPSMADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLEQKGQEYINNIHLTHSLEECLVRTTEKTPSLTRRIDDTIFQNPMVQEAIRMGFSFKDIKKIMEEKIQISGSNYKSLEVLVADLVNAQKDSMQDESSQTSLQKEISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS | Function: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis . Acts as a direct caspase inhibitor . Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry . Inactivates CASP9 by keeping it in a monomeric, inactive state . Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS, PTEN and BIRC5/survivin . Acts as an important regulator of innate immunity by mediating 'Lys-63'-linked polyubiquitination of RIPK2 downstream of NOD1 and NOD2, thereby transforming RIPK2 into a scaffolding protein for downstream effectors, ultimately leading to activation of the NF-kappa-B and MAP kinases signaling . 'Lys-63'-linked polyubiquitination of RIPK2 also promotes recruitment of the LUBAC complex to RIPK2 . Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation . Ubiquitination of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation . Ubiquitination of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation . Plays a role in copper homeostasis by ubiquitinating COMMD1 and promoting its proteasomal degradation . Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation . Ubiquitinates and therefore mediates the proteasomal degradation of BCL2 in response to apoptosis . Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner . Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8 . Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES . Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program .
PTM: S-Nitrosylation down-regulates its E3 ubiquitin-protein ligase activity.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 56685
Sequence Length: 497
Domain: The first BIR domain is involved in interaction with TAB1/MAP3K7IP1 and is important for dimerization . The second BIR domain is sufficient to inhibit CASP3 and CASP7, while the third BIR is involved in CASP9 inhibition . The interactions with DIABLO/SMAC and HTRA2/PRSS25 are mediated by the second and third BIR domains.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q60989 | MTFNSFEGTRTFVLADTNKDEEFVEEFNRLKTFANFPSSSPVSASTLARAGFLYTGEGDTVQCFSCHAAIDRWQYGDSAVGRHRRISPNCRFINGFYFENGAAQSTNPGIQNGQYKSENCVGNRNPFAPDRPPETHADYLLRTGQVVDISDTIYPRNPAMCSEEARLKSFQNWPDYAHLTPRELASAGLYYTGADDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNVNVRSESGVSSDRNFPNSTNSPRNPAMAEYEARIVTFGTWTSSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLDEKGQEYINNIHLTHSLEESLGRTAEKTPSLTKKIDDTIFQNPMVQEAIRMGFSFKDIKKTMEEKIQTSGSSYLSLEVLIADLVSAQKDNTEDESSQTSLQKDISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS | Function: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis (By similarity). Acts as a direct caspase inhibitor (By similarity). Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry (By similarity). Inhibits apoptosis in intestinal crypt cells, its activity is mitigated via its interaction with SEPTIN4 isoform ARTS . Inactivates CASP9 by keeping it in a monomeric, inactive state (By similarity). Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS, PTEN and BIRC5/survivin . Acts as an important regulator of innate immunity by mediating 'Lys-63'-linked polyubiquitination of RIPK2 downstream of NOD1 and NOD2, thereby transforming RIPK2 into a scaffolding protein for downstream effectors, ultimately leading to activation of the NF-kappa-B and MAP kinases signaling . 'Lys-63'-linked polyubiquitination of RIPK2 also promotes recruitment of the LUBAC complex to RIPK2 (By similarity). Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation (By similarity). Ubiquitination of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation (By similarity). Ubiquitination of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation (By similarity). Plays a role in copper homeostasis by ubiquitinating COMMD1 and promoting its proteasomal degradation (By similarity). Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation (By similarity). Ubiquitinates and therefore mediates the proteasomal degradation of BCL2 in response to apoptosis (By similarity). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner (By similarity). Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8 (By similarity). Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES (By similarity). Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program (By similarity). Positive regulator of dermal wound repair, potentially via its interaction with SEPTIN4 .
PTM: S-Nitrosylation down-regulates its E3 ubiquitin-protein ligase activity.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 56079
Sequence Length: 496
Domain: The first BIR domain is involved in interaction with TAB1/MAP3K7IP1 and is important for dimerization. The second BIR domain is sufficient to inhibit caspase-3 and caspase-7, while the third BIR is involved in caspase-9 inhibition. The interactions with DIABLO/SMAC and HTRA2/PRSS25 are mediated by the second and third BIR domains (By similarity).
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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A5D8Q0 | MEPQIVKFVFKEEMTCQCPKMSDSACDVDTDQNYFEEEVRLASFANFSSSYPVSAPALARAGFYYTGDGDRVKCFSCMAMVEDWQHGDTAIGKHRKISPNCKFINGFNNFRSDCIQTQAPVMQNSHANGFPNSAEDPGEKSSSEIMADYMLRTGRVVDMSKPKYPRHMAMCSEEARLQTFQNWPGYSPLMPKELANAGLFYTGINDQVKCFCCGGKLMNWEPSDRAWTEHKKHFPECYFVLGRDVGNVTRDASVQGSTYMNSYNARLETFSSWPFPIDKETLAKAGFYRIGDEDATKCFSCGGMLNCWAANDDPWEEHAKAYPGCQFLIEEKGQQFINNAQLQRPILHKANSGEASPALPKDTSFLKNPLVIYAQQMGFPLEEIKKVMGQKLKTTGNNYTCVEEFVSDLLCAQSETIADKPMKREISIEEKLRQLEEEKVCKVCMDRRITIVFIPCGHLVACAVCADVLDKCPICCTIIERRQKIFMS | Function: Multi-functional protein which regulates not only caspases and apoptosis, but also acts as an E3 ubiquitin-protein ligase mediating ubiquitination and subsequent proteasomal degradation of its target proteins (By similarity). Acts as a direct caspase inhibitor (By similarity). E3 ubiquitin-protein ligase that acts as an important regulator of innate immunity by mediating 'Lys-63'-linked polyubiquitination of ripk2 downstream of NOD1 and NOD2, thereby transforming ripk2 into a scaffolding protein for downstream effectors, ultimately leading to activation of the NF-kappa-B and MAP kinases signaling (By similarity). A key apoptotic suppressor in eggs . Acts as a positive regulator of Wnt signaling .
PTM: Degraded in a 2-step mechanism; a caspase-independent first step and a caspase-dependent second step . Stabilized indirectly by MAPK, which acts to delay caspase activation, rather than directly phosphorylating xiap .
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 55129
Sequence Length: 488
Domain: The BIR and RING-type domains are dispensable for anti-apoptotic function.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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D0U690 | MPSTALSPPSRPPAQSYDSYSSSLSPSSPRFHAAAGSHGRRSPSPSRLESLLDGPHVPPRSPSRKIRSALSRHIRPHITPRTLTPVFLWTLALWLIHHFLFPLSSPFAKLAKPKAEEHFLSTTFPPPAQRLGDDRLDSVDPRWRAYHPLPAPEPPFPRLRPTRFLPPQCLEQWFAEGETLCGAKEMGEEETLDATWLWVNGSDHRWRDSMVEWREKENVNSPERHYREQNELVHSMRSVLDALPGHLRTFHLILADYPFNYPEDLELVPSSIIPDLEVAASKSKGRRHPRELPGAPASLANLTERVTPESISPTLASHLQSEWRILQTPTWLDFSRRDPSDPSHPFHPYSVSKAGEIRQHYAEASYPTLRYASHWEVFHIPSVDRDGRQELMGEREWRENEWKKKALPSFNSMAIESRIGWLPGLADAIIALNDDFFLLRPHAVSDFHSPLYGSVIRFEHGYNQQVKPDVEKNHINDPGEMGGLYHANALLSRRFPRRLRPYFAHVPKVITRGLHHEASLMFQEALTESSTRRFREMKIGEGDVQMQWLLTSLRVERWREALLWTWTVANMGTLGGSQDHWDNDTRRAIKNLFGFTENDDDVVKIEVHRGERWTLEPGRMQRVFRQAGWEAPKATEFLFSSMDGIMPPLLRSGEDPAQNDRCIIDLNRCFGLFWTREEDVLSSDMMKRLTFQYPECGDCMIMALVTASGTLGLNAFFPPKETTITAPELGPGDAYPKFLPPPHLPLTPTWHEADFSLANILSTTALPGEQVDIRQYCMRLLSRYLYLDAKSVSHFHMMKSAEHARRVFRMIQGDPKVSILGMNDDIESDYDEVRGLMNEWFEMRWPRKAVWERDWDPVKDRYND | Function: Xylosylphosphotransferase that is specific for UDP-xylose as a donor and mannose as an acceptor to form a xylose-alpha-1-phosphate-6-mannose linkage. Functions in the O-glycosylation of proteins en route through the secretory pathway.
Catalytic Activity: 3-alpha-D-mannopyranosyl-alpha-D-mannopyranose + UDP-alpha-D-xylose = 3-O-(6-O-alpha-D-xylosylphospho-alpha-D-mannopyranosyl)-alpha-D-mannopyranose + H(+) + UMP
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 99527
Sequence Length: 864
Subcellular Location: Golgi apparatus membrane
EC: 2.7.8.32
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A7GCI1 | MKLLEDKILKEGILLEGNILKVDSFLNHQMDVKLFNEIGKEFKRRFEGCNINKILTIEASGIGIATIVSQYFDFCPVVFAKKVDAANMDKDTYESKVHSFTKNKTYNVRVSKKYINKGDKILLIDDFLANGCAALGLIDIIKQGGAELAGVGIAIEKGFQKGRKELEKVGAKVESLAILDKIENDKVYFK | Function: Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis.
Catalytic Activity: diphosphate + XMP = 5-phospho-alpha-D-ribose 1-diphosphate + xanthine
Sequence Mass (Da): 21225
Sequence Length: 190
Pathway: Purine metabolism; XMP biosynthesis via salvage pathway; XMP from xanthine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.4.2.22
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Q5AY46 | MLKHSSAATKENDSPKLKVLDIVSKLEPSLDHSHTHWWKLTSPQLALMLEAADYSIEKQFETLLFHYHWVVPYLGPKPDADGNFKWRSLVSDVGIPLEYSWKWDTATSGPDVRLTIEPINELSGTRVDPLNQAPSLELLHRLAEILPRLDVSWASHFLSTFYDHDKLKYIKESESETGMPLRSTMLVCFEFGRNGITTKTYMSPRKLGQQGFAPLSDYHSAIAALGPSCALDAVTEFLNNSPEGPHLSPFMLAVDNIIPCSSRLKLYFATPRTSYNSIREVLTLGGRLSTVTLESKLRAIHELVKAIMPFPPDLPDDADIPFPEQVLSPTVQDLAESSDMANQRPAFVAGYQYYFDIAPGASLPDIKFYIPIRKAQMNDQAVATGLTNWMRAQGRGAFCNAYTRVLEGLAGGRDLSKCHGLHTHICVMLKGNGEFDVTSYLAPGCK | Function: Dehydrogenase involved in the conversion of monodictyphenone to the prenyl xanthones such as emericellin, shamixanthone and epishamixanthone . Monodictyphenone is first converted to variecoxanthone A via a paeciloxanthone intermediate by the consecutive actions of the FAD-dependent monooxygenase mdpD and the xanthone prenyltransferase xptB . XptB catalyzes regular O-prenylation at the hydroxy group of C-7 of the xanthone ring . Variecoxanthone A is further prenylated to emericellin by xptA before being reduced to shamixanthone and epishamixanthone by the dehydrogenase xptC .
Sequence Mass (Da): 49673
Sequence Length: 446
Pathway: Secondary metabolite biosynthesis.
EC: 2.5.1.-
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P0DP82 | MATDGMVLHKRSLSEGGTSTQAWKVLSQTLPSRGPDVDAWWQLTGRHLAVLLDAAAYPIEKQYECLLYHYHYAAPYLGPAPREGASPPTWKSMLQLDGTPFEFSWKWNNPGGEPDVRFGLEPIGPMAGTSLDPLNHLAMREILYKLSSAVPGSDLTWTHHFLATLFDHDYAKYTQKAATMGSSIGTSLVYSLEFQRKSTGLKTYFHPRKLDQQAFLDIPSWEASFRGLHPNSPSRTAVHEFLSTNPEGKLLKPFCLSVDNCSPAKARIKWYFNSPHTNFRAIREIMTLGGRIADTETRTKQFSELFNLLKTVTEEHADFPETSEFPYVPNNGDSIIPNFADAPDMLKGCVYFFDIAPGRNLPAIKVYFPVRNHCRNDLAVTQNLNRWLESRGRGQYGAAFGRALETIADYRRLEDSGGLLSFLSCQFMEDGELDLTSYFNPQAFHSGRLTHRRATRRRGDDRW | Function: Dehydrogenase involved in the conversion of monodictyphenone to the prenyl xanthones such as emericellin, shamixanthone and epishamixanthone . Monodictyphenone is first converted to variecoxanthone A via a paeciloxanthone intermediate by the consecutive actions of the FAD-dependent monooxygenase mdpD and the xanthone prenyltransferase xptB . XptB catalyzes regular O-prenylation at the hydroxy group of C-7 of the xanthone ring . Variecoxanthone A is further prenylated to emericellin by xptA before being reduced to shamixanthone and epishamixanthone by the dehydrogenase xptC .
Sequence Mass (Da): 52371
Sequence Length: 463
Pathway: Secondary metabolite biosynthesis.
EC: 2.5.1.-
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Q5AUN2 | MAKLSVILLFRSLLLCGALTVSRHATLVTEREVQSSKYDFIVVGGGVSGLTVADRLTEIPDVSVLVIEAGPVDRGEDFVYVPGSYERDPYIWPGLTNEPSAELNNRVFDSVVARVAGGGSIVNAMIFLRGTALDFDGWESLGNHGWGWEGMLPYFIKSENFTRPTPELAHEGNITWDDSVRGHDGPVRYSYPNYIYPGLGRLYEAALHIGIQPRLDPNGGQNTGVFNQPFAIDAATWTRSSARRNHYDPAVSRPNYHFLSDTTVARVIFDGTRAVGVEYLPSRGGGISTAFAAKEVLVAAGALHTPQVLQLSGVGPRDLLEALNIPIISDLPGVGSNLQDQTTFPFVYTWDSAVTPNVTTFLTNTTWATEQRVLYDQHLPSVWTLTRPLAPKFAFLSYEDATANTAYASILDDAQARDPADSLPGDIHPTVLAGYAVQRQIMFNEFRDAGLAVGGMSWDTDANVQVFNVKPFSRGYVYINQTDPLANPVIDFRTASDPTDFQLHIALLHKQRELFNAPSLAALGPTEVVPGPAVQTDEDIIKLMREILQPSNGHQCCSAPMMPRELGGVLSPEMKVYGTTGLRVIDISHWPKELSGPPMASIYAAGEKAADIIKGEHGWLGN | Function: Dehydrogenase involved in the conversion of monodictyphenone to the prenyl xanthones such as emericellin, shamixanthone and epishamixanthone . Monodictyphenone is first converted to variecoxanthone A via a paeciloxanthone intermediate by the consecutive actions of the FAD-dependent monooxygenase mdpD and the xanthone prenyltransferase xptB . XptB catalyzes regular O-prenylation at the hydroxy group of C-7 of the xanthone ring . Variecoxanthone A is further prenylated to emericellin by xptA before being reduced to shamixanthone and epishamixanthone by the dehydrogenase xptC .
Sequence Mass (Da): 67812
Sequence Length: 622
Pathway: Secondary metabolite biosynthesis.
EC: 1.1.-.-
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Q5BGA7 | MSPPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYEAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKRSDLFIVSKLWNSFHDGERVEPIARKQLSDWGIDYFDLYIVHFPVSLKYVDPEVRYPPGWENAEGKVELGKATIQETWTAMESLVDKGLARSIGISNFSAQLLLDLLRYARIRPATLQIEHHPYLTQERLVTFAQREGIAVTAYSSFGPLSFLELSVKQAEGAPPLFEHPVIKDIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPARLLQNLDVVGFDLEDGELKAISDLDKGLRFNDPPNYGLPITIF | Function: Catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters pentose phosphate pathway (By similarity).
Catalytic Activity: NAD(+) + xylitol = D-xylose + H(+) + NADH
Sequence Mass (Da): 35604
Sequence Length: 319
Pathway: Carbohydrate metabolism; D-xylose degradation.
EC: 1.1.1.307
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Q876L8 | MASPTLKLNSGYDMPQVGFGLWKVDNAVCADTVYNAIKAGYRLFDGACDYGNEKECGEGVARAIKDGLVKREDLFIVSKLWQTFHDEDKVEPITRRQLADWQIDYFDLFLVHFPAALEYVDPSVRYPPGWFYDGKSEVRWSKTTTLQQTWGAMERLVDKGLARSIGVSNYQAQSVYDALIYARIKPATLQIEHHPYLQQPDLVSLAQTEGIVVTAYSSFGPTGFMELDMPRAKSVAPLMDSPVIKALADKHRRTPAQVLLRWATQRGIAVIPKTSRPEVMAQNLDNTSFDLDSEDLAKIADMDLNIRFNKPTNYFSANKLYLFG | Function: Catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters pentose phosphate pathway. Also major aldose reductase in pentose and D-galactose catabolism. Reduces the pentose L-arabinose and the hexose D-galactose to their respective polyols. Responsible for extracellular beta-galactosidase formation and cellulase induction during growth on lactose.
Catalytic Activity: an alditol + NAD(+) = an aldose + H(+) + NADH
Sequence Mass (Da): 36565
Sequence Length: 324
Pathway: Carbohydrate metabolism; D-xylose degradation.
EC: 1.1.1.-
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P86450 | GVQRYTFDAVVSQQDTILSGLDLDCGSYLGYTSPLQGLTAFVPTS | Function: A bifunctional beta-xylosidase/alpha-L-arabinosidase, exo-enzyme that acts synergistically with endohydrolases. Releases xylose and arabinose from cell walls (By similarity).
Catalytic Activity: Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.
Sequence Mass (Da): 4785
Sequence Length: 45
Subcellular Location: Secreted
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A5JTQ2 | ANTKNREPKVSSVFLCFSIFYVTVLLNCNHVYGQTSTVFACDVAKNTNVSSYGFCDNSLSVEDRVSDLVKRLTLQEKIGNLGNSAVEVSRLGIPKYEWWSEALHGVSNIGPGTHFSSLVPGATNFPMPILTAASFNTSLFQAIGSVVSNEARAMYNVGLAGLTYWSPNINIFRDPRWGRGQETPGEDPLLSSKYAAGYVKGLQQTDDGDSDKLKVAACCKHYTAYDVDNWKGVQRYTFDAVVSQQDLDDTFQPPFKSCVIDGNVASVMCSYNKVNGKPTCADPDLLKGVIRGKWKLNGYIVSDCDSVEVLYKDQHYTKTPEEAAAKTILSGLDLDCGSYLGQYTGGAVKQGLVDEASITNAVSNNFATLMRLGFFDGDPSKQPYGNLGPKDVCTPENQELAREAARQGIVLLKNSPRSLPLSSKAIKSLAVIGPNANATRVMIGNYEGIPCKYTSPLQGLTAFVPTSYAPGCPDVQCANAQIDDAAKIAASADATIIVVGANLAIEAESLDRVNILLPGQQQQLVNEVANVSKGPVILVIMSGGGMDVSFAKTNDKITSILWVGYPGEAGGAAIADVIFGSYNPSGRLPMTWYPQSYVEKVPMTNMNMRADPATGYPGRTYRFYKGETVFSFGDGMSFGTVEHKIVKAPQLVSVPLAEDHECRSLECKSLDVADKHCQNLAFDIHLSVKNMGKMSSSHSVLLFFTPPNVHNAPQKHLLGFEKVQLAGKSEGMVRFKVDVCNDLSVVDELGNRKVPLGDHMLHVGNLKHSLSVRI | Function: A bifunctional beta-xylosidase/alpha-L-arabinosidase, exo-enzyme that acts synergistically with endohydrolases. Releases xylose and arabinose from cell walls. Does not cleave xylan from oat spelts although xylan from oat spelts was degraded to xylose when this enzyme was used in combination with xylanase. Also releases xylose and arabinose from aryl glycosides, xylo-oligosaccharides, arabinan from sugar beet and arabino-oligosaccharides, arabinan from sugar beet and arabinoxylan from wheat.
PTM: Proteolytically cleaved in roots to form a 65 kDa protein.
Catalytic Activity: Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.
Sequence Mass (Da): 83727
Sequence Length: 774
Subcellular Location: Secreted
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A1CFY8 | MATSSTTPQNLSFVLEGIHQVKFEDRPIPELRDPHDVIVNVKYTGICGSDVHYWEHGAIGHFVVKDPMVLGHESSGVVAKVGSAVTSLKVGDRVAMEPGVPCRRCEPCKAGKYNLCEKMAFAATPPYDGTLAKYYPLPEDFCYKLPENISLQEGALMEPLGVAVHITRQASIKPGESVVVFGAGPVGLLCCAVARAFGASKIIAVDIQKTRLDFAKKYAATAIFEPAKVSAVANADQMREENDLGPGADVVIDASGAEPSVHTGIHVLRPGGTYVQGGMGRNEINFPIMAACTKELTIKGSFRYGSGDYKLAVDLVASGKVNVKDLITGVVEFQEAEQAFKEVKAGKGIKTLIAGVRD | Cofactor: Binds 1 zinc ion per subunit.
Function: Xylitol dehydrogenase which catalyzes the conversion of xylitol to D-xylulose. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters pentose phosphate pathway (By similarity).
Catalytic Activity: NAD(+) + xylitol = D-xylulose + H(+) + NADH
Sequence Mass (Da): 38179
Sequence Length: 358
Pathway: Carbohydrate degradation; L-arabinose degradation via L-arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route): step 4/5.
EC: 1.1.1.9
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P27156 | MSAAEGPLVVGVDTSTQSTKALVVDVATGRVVASGQAPHTVTSGAGRESDPRQWWDALCEALRQCGEAAHEAAAVSIGGQQHGLVTLDGHGEPVRPALLWNDVRSAPQGHRLIEELGGAKFWAERTGSVPAASFTVTKWAWLAEHEPEAVRATRAVRLPHDYLTERLTGQGTTDRGDASGTGWWASGTEAYDEEILGHVGLDPALLPRVVRPGEVAGTVRDSHELPFSKGTLVACGTGDNAAAALGLGVRPGTPVMSLGTSGTVYAVTQRRPADPTGTVAGFADARGDWLPLACTLNCTLAVDRVAALLGLDREAVEPGHGVTLLPFLDGERTPNLPRSSGLLHGLRHDTTGGQLLQAAYDGAVYSLLAALDLVLDEDADPSAPLLLIGGGARGTAWQQTVRRLSGRAVQVPRAAELVALGAAAQAAGLLTGEDPAAVARRWETAAGPVLEAVERDEETLDRLAGVLSDAAPLLERGTGAG | Function: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate.
Catalytic Activity: ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+)
Sequence Mass (Da): 49822
Sequence Length: 481
EC: 2.7.1.17
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Q9A9Z1 | MTAQVTCVWDLKATLGEGPIWHGDTLWFVDIKQRKIHNYHPATGERFSFDAPDQVTFLAPIVGATGFVVGLKTGIHRFHPATGFSLLLEVEDAALNNRPNDATVDAQGRLWFGTMHDGEENNSGSLYRMDLTGVARMDRDICITNGPCVSPDGKTFYHTDTLEKTIYAFDLAEDGLLSNKRVFVQFALGDDVYPDGSVVDSEGYLWTALWGGFGAVRFSPQGDAVTRIELPAPNVTKPCFGGPDLKTLYFTTARKGLSDETLAQYPLAGGVFAVPVDVAGQPQHEVRLV | Cofactor: Binds 1 Fe(2+) per subunit.
Function: Involved in the degradation of D-xylose . Catalyzes the hydrolysis of D-xylonolactone to D-xylonate .
Catalytic Activity: D-xylono-1,5-lactone + H2O = D-xylonate + H(+)
Sequence Mass (Da): 31586
Sequence Length: 289
EC: 3.1.1.110
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Q8U7Y1 | MKALVLEEKGKLSLRDFDIPGGAGSGELGPKDVRIRTHTVGICGSDVHYYTHGKIGHFVVNAPMVLGHEASGTVIETGSDVTHLKIGDRVCMEPGIPDPTSRASKLGIYNVDPAVRFWATPPIHGCLTPEVIHPAAFTYKLPDNVSFAEGAMVEPFAIGMQAALRARIQPGDIAVVTGAGPIGMMVALAALAGGCAKVIVADLAQPKLDIIAAYDGIETINIRERNLAEAVSAATDGWGCDIVFECSGAAPAILGMAKLARPGGAIVLVGMPVDPVPVDIVGLQAKELRVETVFRYANVYDRAVALIASGKVDLKPLISATIPFEDSIAGFDRAVEARETDVKLQIVMPQ | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: NAD(+) + xylitol = D-xylulose + H(+) + NADH
Sequence Mass (Da): 36776
Sequence Length: 350
EC: 1.1.1.9
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Q9A9Z2 | MRSALSNRTPRRFRSRDWFDNPDHIDMTALYLERFMNYGITPEELRSGKPIIGIAQTGSDISPCNRIHLDLVQRVRDGIRDAGGIPMEFPVHPIFENCRRPTAALDRNLSYLGLVETLHGYPIDAVVLTTGCDKTTPAGIMAATTVNIPAIVLSGGPMLDGWHENELVGSGTVIWRSRRKLAAGEITEEEFIDRAASSAPSAGHCNTMGTASTMNAVAEALGLSLTGCAAIPAPYRERGQMAYKTGQRIVDLAYDDVKPLDILTKQAFENAIALVAAAGGSTNAQPHIVAMARHAGVEITADDWRAAYDIPLIVNMQPAGKYLGERFHRAGGAPAVLWELLQQGRLHGDVLTVTGKTMSENLQGRETSDREVIFPYHEPLAEKAGFLVLKGNLFDFAIMKSSVIGEEFRKRYLSQPGQEGVFEARAIVFDGSDDYHKRINDPALEIDERCILVIRGAGPIGWPGSAEVVNMQPPDHLLKKGIMSLPTLGDGRQSGTADSPSILNASPESAIGGGLSWLRTGDTIRIDLNTGRCDALVDEATIAARKQDGIPAVPATMTPWQEIYRAHASQLDTGGVLEFAVKYQDLAAKLPRHNH | Function: Catalyzes the dehydration of D-xylonate to 2-dehydro-3-deoxy-D-arabinonate during D-xylose degradation. Can also dehydrate D-gluconate, with similar catalytic efficiency. Has weak activity with D-galactonate, D-fuconate and L-arabinonate.
Catalytic Activity: D-xylonate = 2-dehydro-3-deoxy-D-arabinonate + H2O
Sequence Mass (Da): 64626
Sequence Length: 595
Pathway: Carbohydrate metabolism; D-xylose degradation.
EC: 4.2.1.82
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Q59545 | MIMKALVLEKAGKIAIQDWQSNEVLGDDDVEIKIHTVGICGSDVHYYQHGRIGPFVVDEPMVLGHEASGVITAAGKNVKHLKVGDRVCMEPGIPDLQSPQSRAGIYNLDPAVRFWATPPIDGCLRESVIHPAAFTFKLPDNVSFAQGAMVEPLAIGMQSATKAGIKPGDIGLVIGAGTIGIITQSALAGGCSDVIICDVFDEKLKVAEKYQGLHAVNSKDQQALADKVRELTGGEGVNVLFECSGAKPVIASISDHIAPGGTAVLVGMPIDPAPLDIVAAQAKEVTFKTILRYANMYPRTIRLLSSGKLNVAPLLSATYKFKDSVEAYERAAEPVRLM | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: NAD(+) + xylitol = D-xylulose + H(+) + NADH
Sequence Mass (Da): 35952
Sequence Length: 338
EC: 1.1.1.9
|
P06622 | MNKGVMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQGRVYLKAWTEVDKFSLVLREADEPGMDFMGFKVVDEDALRQLERDLMAYGCAVEQLPAGELNSCGRRVRFQAPSGHHFELYADKEYTGKWGLNDVNPEAWPRDLKGMAAVRFDHALMYGDELPATYDLFTKVLGFYLAEQVLDENGTRVAQFLSLSTKAHDVAFIHHPEKGRLHHVSFHLETWEDLLRAADLISMTDTSIDIGPTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPVTWTTDQLGKAIFYHDRILNERFMTVLT | Catalytic Activity: catechol + O2 = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate + H(+)
Sequence Mass (Da): 35156
Sequence Length: 307
Pathway: Xenobiotic degradation; toluene degradation.
EC: 1.13.11.2
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P0AGF5 | MNTQYNSSYIFSITLVATLGGLLFGYDTAVISGTVESLNTVFVAPQNLSESAANSLLGFCVASALIGCIIGGALGGYCSNRFGRRDSLKIAAVLFFISGVGSAWPELGFTSINPDNTVPVYLAGYVPEFVIYRIIGGIGVGLASMLSPMYIAELAPAHIRGKLVSFNQFAIIFGQLLVYCVNYFIARSGDASWLNTDGWRYMFASECIPALLFLMLLYTVPESPRWLMSRGKQEQAEGILRKIMGNTLATQAVQEIKHSLDHGRKTGGRLLMFGVGVIVIGVMLSIFQQFVGINVVLYYAPEVFKTLGASTDIALLQTIIVGVINLTFTVLAIMTVDKFGRKPLQIIGALGMAIGMFSLGTAFYTQAPGIVALLSMLFYVAAFAMSWGPVCWVLLSEIFPNAIRGKALAIAVAAQWLANYFVSWTFPMMDKNSWLVAHFHNGFSYWIYGCMGVLAALFMWKFVPETKGKTLEELEALWEPETKKTQQTATL | Function: Uptake of D-xylose across the boundary membrane with the concomitant transport of protons into the cell (symport system).
Catalytic Activity: D-xylose(in) + H(+)(in) = D-xylose(out) + H(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53608
Sequence Length: 491
Subcellular Location: Cell inner membrane
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P23106 | MNAPQQSPEIGREILAAGYRTNLHDQGEGFPALLIHGSGPASPPGPTGAGSFRSSQTRRVIAPDMLGFGYSERPADGKYSQARWVEHAIGVLDALGIQQGDIVGNSFGGGLALALAIRHPERVRRLVLMGSVGVSFPITAGLETAWGYTPSLANMRRLLDLFAHDRTLVNDELAELRYQASIRPGFQESFAAMFPPPRQNGVDDLASNETDIRALPNETLVIHGREDRIIPLQASLTLAQWIPNAQLHVFGQCGHWTQIEHAERFARLVENFLAEADALHS | Function: Catalyzes the conversion of 2-hydroxymuconate semialdehyde to 2-hydroxypent-2,4-dienoate.
Catalytic Activity: (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate + H2O = 2-oxopent-4-enoate + formate + H(+)
Sequence Mass (Da): 30598
Sequence Length: 281
Pathway: Aromatic compound metabolism; benzoate degradation via hydroxylation.
EC: 3.7.1.9
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Q4J710 | MAKSKDEIKEEIAKAIINQVSKTDLSRRRALSTLAKGGIIAGVLAAFGAGFGSGYVTAPKGSSSSGVAPPQPGFMYGQVPEHPTWKIVFINHVTTNPFFVPTQYGIQDACLLLDCNYQWTGSETSDTTTMVNDMEAAISQGANGIAVSVISPNAFDKPTQDALNAGIPVFAYNAYIPTDDPSYSQYHNPPYLGYIGQSLYASGQLFGQRILNLVPSGSRVALFIATPGTANIQPRIDGIQSVIEGHYTIDVVATGALVSDEQSAIESYFNSHPDVKGMFAVDAGSTQGVGNVLREHGIKTVSNGGTIAAGGYDLLPATIQNIVDGYLDFTIDQQPYLQGFLPTLAIYLYLISDTLVYPLNIDTGSKFITNSNIQPYLLASRYEGSSTAYKPTSTTSSSSSSG | Function: Part of the ABC transporter complex XylFGH involved in the uptake of xylose and arabinose.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 42695
Sequence Length: 402
Subcellular Location: Cell membrane
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Q2YJE7 | MSEYLLEMRNIGKEFNGVKALDGIYLKVRAGECVGLCGENGAGKSTLMKVLSGVYPHGTWTGEIFWEGKELKASGIRDTEAAGIVIIHQELMMVPHLSVAENIFLGCEPTTGGFIDYDQMNARAAELLARLKINDINVALPVYHYSGGKQQLIEIAKAINKNAKLLILDEPTSALTASETRVLIDLIKDFKKQGMACVYISHKLDEVAEISDTVTVIRDGAHIATRPMSELTTPDIITMMVGREMKNLFPREPHDIGEVMFEARNISCWDVTNPGRKVVDDVSFALRRGEILGIAGLVGAGRTELVSSLFGVWPGACQGQVFLEGKEIKIRTPRDAVRQGICMVPEDRKRDGILPIMPVGHNMTISVLDRFSLRGLIDKDAELVAIQREILRLKVKTADPMLAIASLSGGNQQKAVLSKMMLPDPKVLILDEPTRGVDVGAKYEIYKLIFALARQGVSILMVSSEMPEVLGISDRVLVIGEGKLRGDFPNENLTQEKVLAAAIGKPATNAA | Function: Part of the ABC transporter complex XylFGH involved in xylose import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-xylose(out) + H2O = ADP + D-xylose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55814
Sequence Length: 511
Subcellular Location: Cell inner membrane
EC: 7.5.2.10
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D7EZJ3 | MHDAPAQRKRRRPGRIGPLPRSSRFARLKLLIASACAALLATLALPPGAAHAQTVTSNQTGNHNGYFYSFWTDAPGTVSATMGSGGNYSTSWRNTGNFVIGKGWSTGGRRTVTYSGSFNPSGNAYLTLYGWSRNPLVEYYIVDNWGTYRPTGTFKGTVTTDGGTYDIYQTTRYNAPSIEGNKTFNQYWSVRQQKRTGGTITTGNHFDAWARAGMQLGSHDYMIMATEGYQSSGSSNITVGGTSGGGGGGGGGGGCTATLSAGERWDDRYNLNVSVSGSSNWTVTMNVPSPATILSTWNITATWPSSQVLVARPNGSGNNFGVTIKHNGNWTWPTVSCSTG | Function: Endo-acting xylanase which specifically cleaves internal linkages on the xylan backbone, releasing xylooligosaccharides. Is able to hydrolyze oat spelt xylan and birchwood xylan, releasing xylobiose and xylotriose as the major products.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence Mass (Da): 36245
Sequence Length: 340
Pathway: Glycan degradation; xylan degradation.
Subcellular Location: Secreted
EC: 3.2.1.8
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Q8J0K5 | MGISSILLSALIAGGALALPAAEPVSFDIRDENITLARRAEAINYNQDYIASGANVQYSPNMAAGSFSINYNTQGDFVVGLGWQPGDANPITYSGSFSASGVGILAVYGWSTNPLVEYYVMEVHDGYQTAGTHKGTVTTDGGTYDIWEHQQVNQPSILGTSTFNQYISIRQSPRTSGTVTVQNHFNAWAQAGMNLGTLNYQVMAVESWSGSGSGQISLSKGTGGGSTTTTPTGPTSTSTAPSSGGTGAAQWGQCGGIGWTGPTTCVAPYTCKYENAYYSQCQ | Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence Mass (Da): 29475
Sequence Length: 282
Pathway: Glycan degradation; xylan degradation.
Subcellular Location: Secreted
EC: 3.2.1.8
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P36906 | MIKVRVPDFSDKKFSDRWRYCVGTGRLGLALQKEYIETLKYVKENIDFKYIRGHGLLCDDVGIYREDVVGDEVKPFYNFTYIDRIFDSFLEIGIRPFVEIGFMPKKLASGTQTVFYWEGNVTPPKDYEKWSDLVKAVLHHFISRYGIEEVLKWPFEIWNEPNLKEFWKDADEKEYFKLYKVTAKAIKEVNENLKVGGPAICGGADYWIEDFLNFCYEENVPVDFVSRHATTSKQGEYTPHLIYQEIMPSEYMLNEFKTVREIIKNSHFPNLPFHITEYNTSYSPQNPVHDTPFNAAYIARILSEGGDYVDSFSYWTFSDVFEERDVPRSQFHGGFGLVALNMIPKPTFYTFKFFNAMGEEMLYRDEHMLVTRRDDGSVALIAWNEVMDKTENPDEDYEVEIPVRFRDVFIKRQLIDEEHGNPWGTWIHMGRPRYPSKEQVNTLREVAKPEIMTSQPVANDGYLNLKFKLGKNAVVLYELTERIDESSTYIGLDDSKINGY | Function: Has hydrolytic activity towards xylopentaose, xylotriose, xylobiose and P-nitrophenyl-beta-D-xylopyranoside, but has no activity toward xylan.
Catalytic Activity: Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.
Sequence Mass (Da): 58606
Sequence Length: 500
Pathway: Glycan degradation; xylan degradation.
EC: 3.2.1.37
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Q45070 | MIPRIKKTICVLLVCFTMLSVMLGPGATEVLAASDVTVNVSAEKQVIRGFGGMNHPAWAGDLTAAQRETAFGNGQNQLGFSILRIHVDENRNNWYKEVETAKSAVKHGAIVFASPWNPPSDMVETFNRNGDTSAKRLKYNKYAAYAQHLNDFVTFMKNNGVNLYAISVQNEPDYAHEWTWWTPQEILRFMRENAGSINARVIAPESFQYLKNLSDPILNDPQALANMDILGTHLYGTQVSQFPYPLFKQKGAGKDLWMTEVYYPNSDTNSADRWPEALDVSQHIHNAMVEGDFQAYVWWYIRRSYGPMKEDGTISKRGYNMAHFSKFVRPGYVRIDATKNPNANVYVSAYKGDNKVVIVAINKSNTGVNQNFVLQNGSASNVSRWITSSSSNLQPGTNLTVSGNHFWAHLPAQSVTTFVVNR | Function: Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA).
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosyl links in some glucuronoarabinoxylans.
Sequence Mass (Da): 47337
Sequence Length: 422
Pathway: Glycan degradation; xylan degradation.
Subcellular Location: Secreted
EC: 3.2.1.136
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