ids
stringlengths 6
10
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stringlengths 11
1.02k
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stringlengths 108
11.1k
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Q9JLK4 | MGNCAKTPWHRGSKERWQWPGSPLGGSRPSPGPRTEEQEGTQGYSVLGSLVGPACIFLRPSIAATQLDRELRPEEIEELQIAFQEFDRDRDGYIGYRELGACMRTLGYMPTEMELIEISQQISGGKVDFEDFVELMGPKLLAETADMIGVRELRDAFREFDTNGDGCISVGELRAALKALLGERLSQREVDEILQDIDLNGDGLVDFEEFVRMMSR | Function: Required for sound encoding at inner hair cells (IHCs) synapses, likely via inhibition of the inactivation of voltage-gated calcium channel of type 1.3 (Cav1.3) in the IHCs . Required for the normal transfer of light signals through the retina .
Location Topology: Lipid-anchor
Sequence Mass (Da): 24223
Sequence Length: 216
Subcellular Location: Cytoplasm
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Q8HZJ4 | MAEEQGRGRHGPDPAPRPQKPPVEVLASSSGAEGPPLMRKRSSKREKGLRGSRKGPSSSGEQTPMQGPEAPGSSKNPSRTREGQEGPIPSASGLAPRRQSHRHRPGPQHDAAQRMYGPLLNRIFGKDRELGPEELDELQAAFEEFDTDHDGYIGYRDLGECMRTLGYMPTEMELIEVSQHVKMRMGGRVDFEEFVEMMGPKLREETAHMLGLRELRIAFREFDRDRDGRITVAELREAAPALLGEPLVGPELEEMLQEVDLNGDGTVDFNEFVMMLSRH | Function: May play a role in normal synaptic function, probably through regulation of Ca(2+) influx and neurotransmitter release in photoreceptor synaptic terminals and in auditory transmission. Modulator of CACNA1F, shifting the activation range to more hyperpolarized voltages (By similarity).
PTM: Phosphorylated. Phosphorylation levels change with the light conditions and regulate the activity (By similarity).
Sequence Mass (Da): 31164
Sequence Length: 279
Subcellular Location: Cytoplasm
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P45594 | MASGVTVSDVCKTTYEEIKKDKKHRYVIFYIRDEKQIDVETVADRNAEYDQFLEDIQKCGPGECRYGLFDFEYMHQCQGTSESSKKQKLFLMSWCPDTAKVKKKMLYSSSFDALKKSLVGVQKYIQATDLSEASREAVEEKLRATDRQ | Function: Exhibits F-actin depolymerizing activity and regulates actin cytoskeleton dynamics . Required for cytokinesis in both mitotic and meiotic cells and for aster migration and separation . Promotes cell motility during ovary development and oogenesis . During larval development, required for the cell rearrangement needed for formation of terminal filaments which are stacks of somatic cells that are important for the initiation of ovarioles . Also required for border cell migration during oogenesis . During border cell migration, required for actin turnover and lamellipodial protrusion . Required for the establishment of planar cell polarity (PCP) where cells adopt a uniform orientation within the plane of an epithelium . During establishment of PCP, required for the redistribution of the PCP core proteins fz and stan/fmi to the proximodistal cell boundary . During pupal development, required for elongation of the retinal cell body and for rhabdomere morphogenesis . Required for mushroom body neuroblast proliferation and axon growth . Plays a role in the positive regulation of protein secretion . Plays a role in the regulation of nuclear localization of actin . Required for the maintenance of epithelial integrity by controlling cell junctions and is also necessary for cell survival and tissue growth through regulation of JNK and yki signaling .
PTM: Phosphorylated in vitro by protein kinase LIMK1 . Phosphorylation is required for inactivation of tsr and for cell proliferation and axon growth . Phosphorylation is negatively regulated by the panthothenate kinase fbl which catalyzes the first step in the conversion of panthothenic acid to coenzyme A .
Sequence Mass (Da): 17153
Sequence Length: 148
Subcellular Location: Cytoplasm
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P42495 | MGSLEAERKTTGWAARDPSGVLSPYTYTLRETGPEDVFIKIIYCGICHTDIHQIKNDLGASNYPMVPGHEVVGEVVEVGSDVTKFKVGDCVGDGTIVGCCKTCRPCKADVEQYCNKKIWSYNDVYTDGKPTQGGFSGHMVVDQKFVVKIPDGMAPEQAAPLLCAGVTVYSPLTHFGLKEISGLRGGILGLGGVGHMGVKLAKAMGHHVTVISSSDKKKEEAIDHLGADAYLVSSDATQMQEAADSLDYIIDTVPVFHPLEPYLSLLKLDGKLILMGVINTPLQFISPMVMLGRKAITGSFIGSMKETEEMLDFCNEKGITSTIEVVKMDYINTAFERLEKNDVRYRFVVDVAGSKLDQET | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols.
Catalytic Activity: (E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) + NADPH
Sequence Mass (Da): 39129
Sequence Length: 360
Pathway: Aromatic compound metabolism; phenylpropanoid biosynthesis.
EC: 1.1.1.195
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Q9CAI3 | MSSSESVENECMCWAARDPSGLLSPHTITRRSVTTDDVSLTITHCGVCYADVIWSRNQHGDSKYPLVPGHEIAGIVTKVGPNVQRFKVGDHVGVGTYVNSCRECEYCNEGQEVNCAKGVFTFNGIDHDGSVTKGGYSSHIVVHERYCYKIPVDYPLESAAPLLCAGITVYAPMMRHNMNQPGKSLGVIGLGGLGHMAVKFGKAFGLSVTVFSTSISKKEEALNLLGAENFVISSDHDQMKALEKSLDFLVDTASGDHAFDPYMSLLKIAGTYVLVGFPSEIKISPANLNLGMRMLAGSVTGGTKITQQMLDFCAAHKIYPNIEVIPIQKINEALERVVKKDIKYRFVIDIKNSLK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols.
Catalytic Activity: (E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) + NADPH
Sequence Mass (Da): 38671
Sequence Length: 355
Pathway: Aromatic compound metabolism; phenylpropanoid biosynthesis.
EC: 1.1.1.195
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P08641 | MGRRWGSPALQRFPVLVLLLLLQVCGRRCDEAAPCQPGFAAETFSFSVPQDSVAAGRELGRVSFAACSGRPWAVYVPTDTRFKVNGDGVVSTKRPLTLYGRKISFTIYAQDAMGKRHSARVTVGRHRHRRHHHNHHLQDTTPAVLTFPKHDPGFLRRQKRDWVIPPISCLENHRGPYPMRLVQIKSNKDKESKVYYSITGQGADSPPVGIFIIERETGWLEVTEQLDREKIDRYTLLSHAVSASGQPVEDPMEIIITVMDQNDNKPVFIKEVFVGYIEENAKPGTSVMTVNATDADDAVNTDNGIVSYSIVSQQPPRPHPQMFTIDPAKGIISVLGTGLDRETTPNYTLIVQATDQEGKGLSNTATAIIEVTDANDNIPIFNPTMYEGVVEENKPGTEVARLTVTDQDAPGSPAWQAVYHIKSGNLDGAFSIITDPSTNNGILKTAKGLDYETKSRYDLVVTVENKVPLSVPITLSTASVLVTVLDVNEPPVFVPPIKRVGVPEDLPVGQQVTSYTAQDPDRDMRQKITYRMGSDPAGWLYIHPENGIVTATQPLDRESVHAINSTYKAIILAVDNGIPDTTGTGTLLLLLQDVNDNGPTPEPRSFEICSRQPEKQILSIVDKDLPPHTYPFKAALEHGSSNNWTVEIRGQDELAMGLKKELEPGEYNIFVKLTDSQGKAQVTQVKAQVCECEGTAKNCERRSYIVGGLGVPAILGILGGILALLILLLLLLLFARRRKVEKEPLLPPEDDMRDNVYNYDEEGGGEEDQDYDLSQLHRGLDARPEVIRNDVAPPLMAAPQYRPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGGGSEATSLSSLNSSASDQDQDYDYLNEWGNRFKKLAELYGGGEDDE | Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. E-cadherin is a ligand for integrin alpha-E/beta-7.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 97783
Sequence Length: 887
Domain: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.
Subcellular Location: Cell membrane
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P12830 | MGPWSRSLSALLLLLQVSSWLCQEPEPCHPGFDAESYTFTVPRRHLERGRVLGRVNFEDCTGRQRTAYFSLDTRFKVGTDGVITVKRPLRFHNPQIHFLVYAWDSTYRKFSTKVTLNTVGHHHRPPPHQASVSGIQAELLTFPNSSPGLRRQKRDWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTINRNTGVISVVTTGLDRESFPTYTLVVQAADLQGEGLSTTATAVITVTDTNDNPPIFNPTTYKGQVPENEANVVITTLKVTDADAPNTPAWEAVYTILNDDGGQFVVTTNPVNNDGILKTAKGLDFEAKQQYILHVAVTNVVPFEVSLTTSTATVTVDVLDVNEAPIFVPPEKRVEVSEDFGVGQEITSYTAQEPDTFMEQKITYRIWRDTANWLEINPDTGAISTRAELDREDFEHVKNSTYTALIIATDNGSPVATGTGTLLLILSDVNDNAPIPEPRTIFFCERNPKPQVINIIDADLPPNTSPFTAELTHGASANWTIQYNDPTQESIILKPKMALEVGDYKINLKLMDNQNKDQVTTLEVSVCDCEGAAGVCRKAQPVEAGLQIPAILGILGGILALLILILLLLLFLRRRAVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD | Function: Cadherins are calcium-dependent cell adhesion proteins . They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells . Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7.
PTM: During apoptosis or with calcium influx, cleaved by a membrane-bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3 . Processing by the metalloproteinase, induced by calcium influx, causes disruption of cell-cell adhesion and the subsequent release of beta-catenin into the cytoplasm . The residual membrane-tethered cleavage product is rapidly degraded via an intracellular proteolytic pathway . Cleavage by caspase-3 releases the cytoplasmic tail resulting in disintegration of the actin microfilament system . The gamma-secretase-mediated cleavage promotes disassembly of adherens junctions . During development of the cochlear organ of Corti, cleavage by ADAM10 at adherens junctions promotes pillar cell separation (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 97456
Sequence Length: 882
Domain: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.
Subcellular Location: Cell junction
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P09803 | MGARCRSFSALLLLLQVSSWLCQELEPESCSPGFSSEVYTFPVPERHLERGHVLGRVRFEGCTGRPRTAFFSEDSRFKVATDGTITVKRHLKLHKLETSFLVRARDSSHRELSTKVTLKSMGHHHHRHHHRDPASESNPELLMFPSVYPGLRRQKRDWVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQGADKPPVGVFIIERETGWLKVTQPLDREAIAKYILYSHAVSSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGAVPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKNMFTVNRDTGVISVLTSGLDRESYPTYTLVVQAADLQGEGLSTTAKAVITVKDINDNAPVFNPSTYQGQVPENEVNARIATLKVTDDDAPNTPAWKAVYTVVNDPDQQFVVVTDPTTNDGILKTAKGLDFEAKQQYILHVRVENEEPFEGSLVPSTATVTVDVVDVNEAPIFMPAERRVEVPEDFGVGQEITSYTAREPDTFMDQKITYRIWRDTANWLEINPETGAIFTRAEMDREDAEHVKNSTYVALIIATDDGSPIATGTGTLLLVLLDVNDNAPIPEPRNMQFCQRNPQPHIITILDPDLPPNTSPFTAELTHGASVNWTIEYNDAAQESLILQPRKDLEIGEYKIHLKLADNQNKDQVTTLDVHVCDCEGTVNNCMKAGIVAAGLQVPAILGILGGILALLILILLLLLFLRRRTVVKEPLLPPDDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPQYRPRPANPDEIGNFIDENLKAADSDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDQDQDYDYLNEWGNRFKKLADMYGGGEDD | Function: Cadherins are calcium-dependent cell adhesion proteins . They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells . Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7 (By similarity).
PTM: During apoptosis or with calcium influx, cleaved by a membrane-bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3 (By similarity). Processing by the metalloproteinase, induced by calcium influx, causes disruption of cell-cell adhesion and the subsequent release of beta-catenin into the cytoplasm (By similarity). The residual membrane-tethered cleavage product is rapidly degraded via an intracellular proteolytic pathway (By similarity). Cleavage by caspase-3 releases the cytoplasmic tail resulting in disintegration of the actin microfilament system (By similarity). The gamma-secretase-mediated cleavage promotes disassembly of adherens junctions (By similarity). During development of the cochlear organ of Corti, cleavage by ADAM10 at adherens junctions promotes pillar cell separation .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 98256
Sequence Length: 884
Domain: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.
Subcellular Location: Cell junction
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Q8H859 | MAAECGSGNCDAWAARDPSGILSPYKFNRRAVQSDDVSLRITHCGVCYADVAWTRNILNNSMYPLVPGHEIAGVVTEVGADVKSFKVGDHVGVGTYVNSCRDCENCNSSLENYCSQHVFTFNGVDTDGTVTKGGYSTHIVVHERYCFKIPDGYPLEKAAPLLCAGITVYSPMMRHNMNQPGKSLGVIGLGGLGHMAVKFGKAFGLKVTVISTSESKRKEAIDLLGADNFVVSSDENQMETLKSSLNFIIDTASGDHPFDPYLTLLKVGGVMALLSFPSEIKVHPANLNLGGRSLSGSVTGGTKDIQEMINFCAANKIYPDIEMIKIDYINEALQRLVDRDVRFRFVIDIENSFK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols.
Catalytic Activity: (E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) + NADPH
Sequence Mass (Da): 38512
Sequence Length: 354
Pathway: Aromatic compound metabolism; phenylpropanoid biosynthesis.
EC: 1.1.1.195
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P85913 | MGSLESERFVVDVAASNLDK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers, like coniferyl alcohol, sinapyl alcohol and 4-coumaryl alcohol (By similarity).
Catalytic Activity: (E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) + NADPH
Sequence Mass (Da): 2167
Sequence Length: 20
Pathway: Aromatic compound metabolism; phenylpropanoid biosynthesis.
EC: 1.1.1.195
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Q9SJ25 | MVDQNKAFGWAANDESGVLSPFHFSRRENGENDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVGKNVTKFKEGDRVGVGVIIGSCQSCESCNQDLENYCPKVVFTYNSRSSDGTSRNQGGYSDVIVVDHRFVLSIPDGLPSDSGAPLLCAGITVYSPMKYYGMTKESGKRLGVNGLGGLGHIAVKIGKAFGLRVTVISRSSEKEREAIDRLGADSFLVTTDSQKMKEAVGTMDFIIDTVSAEHALLPLFSLLKVNGKLVALGLPEKPLDLPIFSLVLGRKMVGGSQIGGMKETQEMLEFCAKHKIVSDIELIKMSDINSAMDRLAKSDVRYRFVIDVANSLLPESSAEILTEQVDHGVSITSRF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols.
Catalytic Activity: (E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) + NADPH
Sequence Mass (Da): 40909
Sequence Length: 376
Pathway: Aromatic compound metabolism; phenylpropanoid biosynthesis.
EC: 1.1.1.195
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Q13111 | MLEELECGAPGARGAATAMDCKDRPAFPVKKLIQARLPFKRLNLVPKGKADDMSDDQGTSVQSKSPDLEASLDTLENNCHVGSDIDFRPKLVNGKGPLDNFLRNRIETSIGQSTVIIDLTEDSNEQPDSLVDHNKLNSEASPSREAINGQREDTGDQQGLLKAIQNDKLAFPGETLSDIPCKTEEEGVGCGGAGRRGDSQECSPRSCPELTSGPRMCPRKEQDSWSEAGGILFKGKVPMVVLQDILAVRPPQIKSLPATPQGKNMTPESEVLESFPEEDSVLSHSSLSSPSSTSSPEGPPAPPKQHSSTSPFPTSTPLRRITKKFVKGSTEKNKLRLQRDQERLGKQLKLRAEREEKEKLKEEAKRAKEEAKKKKEEEKELKEKERREKREKDEKEKAEKQRLKEERRKERQEALEAKLEEKRKKEEEKRLREEEKRIKAEKAEITRFFQKPKTPQAPKTLAGSCGKFAPFEIKEHMVLAPRRRTAFHPDLCSQLDQLLQQQSGEFSFLKDLKGRQPLRSGPTHVSTRNADIFNSDVVIVERGKGDGVPERRKFGRMKLLQFCENHRPAYWGTWNKKTALIRARDPWAQDTKLLDYEVDSDEEWEEEEPGESLSHSEGDDDDDMGEDEDEDDGFFVPHGYLSEDEGVTEECADPENHKVRQKLKAKEWDEFLAKGKRFRVLQPVKIGCVWAADRDCAGDDLKVLQQFAACFLETLPAQEEQTPKASKRERRDEQILAQLLPLLHGNVNGSKVIIREFQEHCRRGLLSNHTGSPRSPSTTYLHTPTPSEDAAIPSKSRLKRLISENSVYEKRPDFRMCWYVHPQVLQSFQQEHLPVPCQWSYVTSVPSAPKEDSGSVPSTGPSQGTPISLKRKSAGSMCITQFMKKRRHDGQIGAEDMDGFQADTEEEEEEEGDCMIVDVPDAAEVQAPCGAASGAGGGVGVDTGKATLTASPLGAS | Function: Core component of the CAF-1 complex, a complex that is thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. It may play a role in heterochromatin maintenance in proliferating cells by bringing newly synthesized cbx proteins to heterochromatic DNA replication foci.
Sequence Mass (Da): 106910
Sequence Length: 956
Domain: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain.
Subcellular Location: Nucleus
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Q9QWF0 | MLEEPEAATRTAAAVDCKDRPGFPVKRLIQARLPFKRLNLVPKEKVEEDTSPKAAVESKVPDLQLSLGTFESQCHTGSHVGLSTKLVGGQGPIDSFLRATIKPVPSVVIIDLTENCSDIPDSPEGHSELSPDTAGVVTTVEGAAKQQEHSAAELCLLETPSDITCHMEEEPGSPGDPKRTGDCQAGSLQSCPELTPGSRTCPTKELSSWSKAGDLLFIEKVPVVVLEDILATKPSIASLPMMSLDRSVTSESEILESCPEDDSILSHSSTNSSSPTSSPEGPSTPPEHRGGRSSPSTPACRVAKNFVKGSTEKGRSKLHRDREQQREEKEKLREEIRRAKEEARKKKEEEKELKEKERREKREKDEKEKAEKQRLKEEKRKERQEALEAKLEEKRKKEEEKRLREEEKRLREEEKRIKAEKAEITRFFQKPKTPQAPKTLAGSCGKFAPFEIKEHMVLAPRCRAALDQDLCDQLDQLLQQQSVASTFLSDLKSRLPLRSGPTRVCGHDTDIMNRDVVIVESSKVDGVSERKKFGRMKLLQFSENHRPAYWGTWNKKTAIIRPRNPWAQDKDLLDYEVDSDDEWEEEEPGESLSHSEGDEDDDVGEDEDEDDGFFVPHGYLSEDEGVTEECADPENHKVHQKLKAKEWDELLAKGKRFRVLQPVHVGCVWASEAANCTSSDLKLLQQFTACLLDVASPDEPEPGASRREKRDQHILAQLLPLLHGNVNGSKVIIHEFQEQCRRGLLTLPSPTPHLQMPNLEDAVAVPSKARLKRLISENSAYEKRPNFRMCWYVHPEVLKSFGQECLPVPCQWTYITTMPSAPREDSGSASTEGPGQSTPMLLKRKPAATMCITQFMKKRRYDGQVGSGDMDGFQADTEEDEEDDTDCMIIDVPDVGSDVSEAPIPAPTLCK | Function: Core component of the CAF-1 complex, a complex that is thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. It may play a role in heterochromatin maintenance in proliferating cells by bringing newly synthesized cbx proteins to heterochromatic DNA replication foci.
Sequence Mass (Da): 101936
Sequence Length: 911
Domain: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain.
Subcellular Location: Nucleus
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P26949 | MRYSKLFLCAGLTLATLPCWGRAYTFDSTMLDTNSGESIDVSLFNQGLQLPGNYFVNVFVNGRKVDSGNIDFRLEKHNGKELLWPCLSSLQLTKYGIDIDKYPDLIKSGTEQCVDLLAIPHSDVQFYFNQQKLSLIVPPQALLPRFDGIMPMQLWDDGIPALFMNYNTNMQTRKFREGGKSLDSYYAQLQPGLNIGAWRFRSSTSWWKQQGWQRSYIYAERGLNTIKSRLTLGETYSDSSIFDSIPIKGIKIASDESMVPYYQWNFAPVVRGIARTQARVEVLRDGYTVSNELVPSGPFELANLPLGGGSGELKVIIHESDGTKQVFTVPYDTPAVALRKGYFEYSMMGGEYRPANDLTQTSYVGALGMKYGLPRNLTLYGGLQGSQNYHAAALGIGAMLGDFGAISTDVTQADSQKNKQKKESGQRWRVRYNKYLQSGTSLNIASEEYATEGFNKLADTLNTYCKPNTRNDCRFDYAKPKNKVQFNLSQSIPGSGTLNFSGYRKNYWRDSRSTTSFSVGYNHFFRNGMSLTLNLSKTQNINKYGEKTSELLSNIWLSFPLSRWLGNNSINSNYQMTSDSHGNTTHEVGVYGEAFDRQLYWDVRERFNEKGRKYTSNALNLNYRGTYGEISGNYSYDQTQSQLGIGVNGNMVITQYGITAGQKTGDTIALVQAPDISGASVGYWPGMKTDFRGYTNYGYLTPYRENKVEINPVTLPNDAEITNNIVSVIPTKGAVVLAKFNARIGGRLFLHLKRSDNKPVPFGSIVTIEGQSSSSGIVGDNSGVYLTGLPKKSKILVKWGRDKNQSCSSNVVLPEKTDISGAYRLSTTCILNN | Function: A probable role in capsular biogenesis. It is likely that the caf1A molecule binds F1 antigen subunits during the extracellular secretion process.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 93003
Sequence Length: 833
Subcellular Location: Cell outer membrane
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Q9S9P2 | MSQAPNPEEEDDTIEIREVWNHNLEQEMALIEQSIDDFPYVAMDTEFPGIVCKTVTANPNPNPYSIHYEYNYDTLKANVNMLKLIQLGLTLSDEKGNLPTCGTNKQCIWQFNFREFNVISDMFALDSIELLRKSAIDLEKNNECGVDAKRFAELLMGSGVVLNDKIHWVTFHCGYDFGYLLKLLSGKELPEEISDFFDQMEKFFPVVYDIKYLMGFCTNLYGGLEKIAELLGVKRVGISHQAGSDSLLTLRTFIKMKEFFFTGSLLKYSGFLFGLDNPRLLTGSKN | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 32635
Sequence Length: 286
Subcellular Location: Nucleus
EC: 3.1.13.4
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Q13112 | MKVITCEIAWHNKEPVYSLDFQHGTAGRIHRLASAGVDTNVRIWKVEKGPDGKAIVEFLSNLARHTKAVNVVRFSPTGEILASGGDDAVILLWKVNDNKEPEQIAFQDEDEAQLNKENWTVVKTLRGHLEDVYDICWATDGNLMASASVDNTAIIWDVSKGQKISIFNEHKSYVQGVTWDPLGQYVATLSCDRVLRVYSIQKKRVAFNVSKMLSGIGAEGEARSYRMFHDDSMKSFFRRLSFTPDGSLLLTPAGCVESGENVMNTTYVFSRKNLKRPIAHLPCPGKATLAVRCCPVYFELRPVVETGVELMSLPYRLVFAVASEDSVLLYDTQQSFPFGYVSNIHYHTLSDISWSSDGAFLAISSTDGYCSFVTFEKDELGIPLKEKPVLNMRTPDTAKKTKSQTHRGSSPGPRPVEGTPASRTQDPSSPGTTPPQARQAPAPTVIRDPPSITPAVKSPLPGPSEEKTLQPSSQNTKAHPSRRVTLNTLQAWSKTTPRRINLTPLKTDTPPSSVPTSVISTPSTEEIQSETPGDAQGSPPELKRPRLDENKGGTESLDP | Function: Complex that is thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer.
PTM: Differentially phosphorylated during cell cycle. During mitosis the p60 subunit of inactive CAF-1 is hyperphosphorylated and displaced into the cytosol. Progressivly dephosphorylated from G1 to S and G2 phase. Phosphorylated p60 is recruited to chromatin undergoing DNA repair after UV irradiation in G1, S or G2 phases.
Sequence Mass (Da): 61493
Sequence Length: 559
Subcellular Location: Nucleus
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Q9SFX6 | MKQISSGEVWRWNKEVEMNSIRDCLKHCSSIAIDTEFPGCLKETPMDASEEIRYRDMKFNVDNTHLIQLGFTLFDRRGFAKTWEINLSDFDEHKCFKNDKSIAFLKSNGLNLDKIREEGIGIDEFFRDFSQILTEKDGKITWVNFQGSYDNAYLVKGLTGGKPLPETKEEFHETVQQLLGKFVFDVKKIAESCSGLSSQFGLQRIADVLQMKRVGKAHHAGSDSELTARVFTKLTFDLLNSRKQSVRRVDHQQFQLEQQQHQQFMMTRCYIPIPMPIPRPRPVMFAAHHQNPYFGGGYFRMPVQGMNYVL | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 35923
Sequence Length: 310
Subcellular Location: Nucleus
EC: 3.1.13.4
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Q9SAI2 | MSLFLKDDSIQIREVWNDNLQEEMDLIRDVVDDFPYVAMDTEFPGIVVRPVGTFKSNADYHYETLKTNVNILKMIQLGLTFSNEQGNLPTCGTDKYCIWQFNFREFDLDSDIFALDSIELLKQSGIDLAKNTLDGIDSKRFAELLMSSGIVLNENVHWVTFHSGYDFGYLLKLLTCQNLPDSQTDFFKLINVYFPTVYDIKHLMKFCNSLHGGLNKLAELLEVERVGICHQAGSDSLLTSCTFRKLKENFFVGPLHKYSGVLYGLGVENGQVAI | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 31201
Sequence Length: 274
Subcellular Location: Nucleus
EC: 3.1.13.4
|
Q9SKZ2 | MSLFLKDDSIQIREVWNDNLESEMALIREVVDDFPFVAMDTEFPGIVCRPVGTFKTNTEYHYETLKTNVNILKMIQLGLTFSDEKGNLPTCGTDNKYCIWQFNFREFDLESDIYATDSIELLRQSGIDFVKNNEFGIDSKRFAELLMSSGIVLNENVHWVTFHSGYDFGYLLKLLTCQNLPETQTGFFEMISVYFPRVYDIKHLMKFCNSLHGGLNKLAELLDVERVGICHQAGSDSLLTSCTFRKLQENFFIGSMEKYSGVLYGLGVENGQIVH | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 31543
Sequence Length: 275
Subcellular Location: Nucleus
EC: 3.1.13.4
|
Q9LXM4 | MSLIEDCLRSYRFIAIDTEFPSTLRETTQHATDEERYMDMSFSVDRAKLIQLGLTLFDINGRIGGTWEINFSDFGVDDARNEKSIEFLRRNGLDLRKIREEGIRIEGFFSEMFWMLKKTRRNITWVTFHGSYDIAYLLKGFTGEALPVTSERFSKAVARVLGSVYDLKVMAGRCEGLSSRLGLETLAHEFGLNRVGTAHHAGSNNELTAMVFAKVLSPFPLFLRFGSLELRTIESEAIV | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 27213
Sequence Length: 239
Subcellular Location: Nucleus
EC: 3.1.13.4
|
Q9LXM2 | MAIIKPNRDLKPDGVTVVTREVWAENLESEFELISEIIDDYPFISMDTEFPGVIFKSDLRFTNPDDLYTLLKANVDALSLIQVGLTLSDVNGNLPDLGDDLHRGFIWEFNFRDFDVARDAHAPDSIELLRRQGIDFERNCRDGVESERFAELMMSSGLVCNEEVSWVTFHSAYDFGYLMKILTRRELPGALGEFKRVMRVLFGERVYDVKHMMKFCERRLFGGLDRVARTLEVNRAVGKCHQAGSDSLLTWHAFQRMRDLYFVQDGPEKHAGVLYGLEVF | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 32233
Sequence Length: 280
Subcellular Location: Nucleus
EC: 3.1.13.4
|
Q9LEU4 | MAETLKEDSIMIREVWDYNLVEEFALIREIVDKFSYIAMDTEFPGVVLKPVATFKYNNDLNYRTLKENVDLLKLIQVGLTFSDENGNLPTCGTDKFCIWQFNFREFNIGEDIYASESIELLRQCGIDFKKNIEKGIDVVRFGELMMSSGIVLNDAISWVTFHGGYDFGYLVKLLTCKELPLKQADFFKLLYVYFPTVYDIKHLMTFCNGLFGGLNRLAELMGVERVGICHQAGSDSLLTLGSFRKLKERYFPGSTEKYTGVLYGLGVEDGTTTTVAN | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 31533
Sequence Length: 277
Subcellular Location: Nucleus
EC: 3.1.13.4
|
Q9FMS6 | MIKSEADLSDVIVIRDVWAYNLESEFDLIRGIVEDYPFISMDTEFPGVIYKADLDVLRRGNPNYLYNLLKSNVDALSLIQVGLTLSDADGNLPDLGGQKNRRYIWEFNFRDFDVERDPHAPDSIELLRRHGIDFERNRREGVESERFAELMMSSGLICNESVSWVTFHSAYDFGYLVKILTRRQLPVALREFLGLLRAFFGDRVYDVKHIMRFCEQRLYGGLDRVARSLEVNRAVGKCHQAGSDSLLTWQAFQRMRDLYFVEDGAEKHAGVLYGLEVF | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 32169
Sequence Length: 278
Subcellular Location: Nucleus
EC: 3.1.13.4
|
P54212 | MGSRRITLLGALFAVLAVAIEGRTLLTHNLKAEAAETVDAVSSVVAGSAGRQLLVSEPHDYNYEKVGFDWTGGVCVNTGTSKQSPINIETDSLAEESERLGTADDTSRLALKGLLSSSYQLTSEVAINLEQDMQFSFNAPDEDLPQLTIGGVVHTFKPVQIHFHHFASEHAIDGQLYPLEAHMVMASQNDGSDQLAVIGIMYKYGEEDPFLKRLQETAQSNGEAGDKNVELNSFSINVARDLLPESDLTYYGYDGSLTTPGCDERVKWHVFKEARTVSVAQLKVFSEVTLAAHPEATVTNNRVIQPLNGRKVYEYKGEPNDKYNYVQHGFDWRDNGLDSCAGDVQSPIDIVTSTLQAGSSRSDVSSVNLMTLNTDAFTLTGNTVNIGQGMQINFGDPPAGDLPVIRIGTRDVTFRPLQVHWHFFLSEHTVDGVHYPLEAHIVMKDNDNLGDSAGQLAVIGIMYKYGDADPFITDMQKRVSDKIASGAITYGQSGVSLNNPDDPFNVNIKNNFLPSELGYAGYDGSLTTPPCSEIVKWHVFLEPRTVSVEQMEVFADVTLNSNPGATVTTNRMIQPLEGRTVYGYNGAAA | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 64258
Sequence Length: 589
EC: 4.2.1.1
|
O52535 | MKTSLGKAALLALSMMPVTVFASHWSYEGEGSPEHWGALNEEYKTCQNGMNQSPINIDATFKTHLSPLDTHYIDGPITLINNGHTIQAALKTTTADTITIDGTPFILQQFHFHAPSENTVHGKHYAMEMHLVHKNAKGAVAVVAVMFEQGAENTELNKLWATMPEQAEQTAKIVTQMDLNALLPIDKTYWRFSGSLTTPPCSEGVTRIVLKHPLTLSSAQLAKFSHAMHHDNNRPVQPLNGRVVIE | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 27145
Sequence Length: 246
Subcellular Location: Periplasm
EC: 4.2.1.1
|
P84537 | DELNKKVDSDETISDDGVVAHGASMDEKHDYMDNGVRHVHNGRTRRKGSEHEVDGRFTPMEARLVFHLTTPPCTESVLWVVQKDDDEHHTRREEGPHWHDTHSFKHAEDLDVHLTPEDDLEDDKRHDDTYTYEGSLTTEEVQVEGYKDEPEELEMVDNWRPAQKNKVTVYKASEH | Function: Reversible hydration of carbon dioxide. Also acts as a structural protein, having a role in calcium carbonate crystal formation in the bio-calcification process.
PTM: Glycosylated.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 20383
Sequence Length: 175
EC: 4.2.1.1
|
Q57752 | MISKNVRIAKGAVIVGDVTIGDYSSVWYNAVIRGDVDKIIIGNYSNIQDCCVVHCSKGYPTIIGDYVSIGHGAVIHGCRIEDNVLVGMNATILNGAKIGENCIIGANALVTQNKEIPPNSLVLGVPGRVVRELTEEEIKSIKENALRYVKLSETLESYK | Function: Probably reversibly hydrates carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 17174
Sequence Length: 159
EC: 4.2.1.1
|
P40881 | MMFNKQIFTILILSLSLALAGSGCISEGAEDNVAQEITVDEFSNIRENPVTPWNPEPSAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVLHALETINEEGEPIEDNIVEVDGKEYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVTIPDGRYIPAGMVVTSQAEADKLPEVTDDYAYSHTNEAVVYVNVHLAEGYKETS | Cofactor: Binds 1 Zn(2+) per subunit, at the subunit interface.
Function: Reversible hydration of carbon dioxide. Important for growth on acetate . As a probably extracellular enzyme, it may support a H(+)/CH(3)COO(-) symport mechanism and/or conversion of CO(2) to HCO(3)(-), removing excess CO(2) produced by growth on acetate (Probable).
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 26414
Sequence Length: 247
Subcellular Location: Secreted
EC: 4.2.1.1
|
Q2RGM7 | MQKVEVFRIPTASPDDISGLATLIDSGKINPAEIVAILGKTEGNGCVNDFTRGFATQSLAMYLAEKLGISREEVVKKVAFIMSGGTEGVMTPHITVFVRKDVQEPAKPGKRLAVGVAFTRDFLPEELGRMEQVNEVARAVKEAMKDAQIDDPRDVHFVQIKCPLLTAERIEDAKRRGKDVVVNDTYKSMAYSRGASALGVALALGEISADKISNEAICHDWNLYSSVASTSAGVELLNDEIIVVGNSTNSASDLVIGHSVMKDAIDADAVRAALKDAGLKFDCCPPAEELAKIVNVLAKAEAASSGTVRGRRNTMLDDSDINHTRSARAVVNAVIASVVGDPMVYVSGGAEHQGPDGGGPIAVIARV | Function: Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret.
Catalytic Activity: cyanurate + H2O = 1-carboxybiuret + H(+)
Sequence Mass (Da): 38900
Sequence Length: 367
Domain: The monomer structure is formed from three repeating units (RUs) that share the same structure as one another. The monomer, the active site and substrate all possess threefold rotational symmetry, to the extent that the active site possesses three potential Ser-Lys catalytic dyads. It is possible that any or all of the three active-site serines may act as nucleophile (albeit only one can do so per catalytic cycle).
Pathway: Xenobiotic degradation; atrazine degradation; biuret from cyanurate: step 1/1.
EC: 3.5.2.15
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Q50940 | MPRFPRTLPRLTAVLLLACTAFSAAAHGNHTHWGYTGHDSPESWGNLSEEFRLCSTGKNQSPVNITETVSGKLPAIKVNYKPSMVDVENNGHTIQVNYPEGGNTLTVNGRTYTLKQFHFHVPSENQIKGRTFPMEAHFVHLDENKQPLVLAVLYEAGKTNGRLSSIWNVMPMTAGKVKLNQPFDASTLLPKRLKYYRFAGSLTTPPCTEGVSWLVLKTYDHIDQAQAEKFTRAVGSENNRPVQPLNARVVIE | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 28085
Sequence Length: 252
Subcellular Location: Periplasm
EC: 4.2.1.1
|
P94170 | MSSTLYRRQLLKLLGMSVLGTSFSSCVTSPARAKTVNWGYIGKVGPEHWGELSPDFALCQIGRKQTPIDLQIADVKDVHSSSQDLLVTNYQPTALHLINNGKTVQVNYQPGSYLKYAHQKFELLQFHFHHFSEHRVDGKLYDMELHLVHRSKSGDLAVMGIFLQAGAFNPTLQIIWDATPQNQGTDKRIEDINIDASQFLPAQHRFFTYSGSLTTPPCSENVLWCVMATPIEASPAQIAKFSQMFPQNARPVQPLNDRLVIEAI | Function: Reversible hydration of carbon dioxide.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 29639
Sequence Length: 264
EC: 4.2.1.1
|
Q6DAJ6 | MKGKFSIALMLSACFSASASDSVHWGYEGSGDPAHWGKLSPDFSLCETGKNQSPVNIQQALNAQHDPLQLAFQSGTQQIINNGHTVQVNVSSGNTLLLDNETFALQQFHFHAPSENEIDGKQFPLEGHFVYKNADGALTVIALMFQEGAANPQLATAWQQIPAHVDQAEDVRTPIAIQALLPTSLNYYRFSGSLTTPPCSEGIRWLVLDHPVTASAEQINQFSSVMHHANNRPIQPLNGRIIIH | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 26664
Sequence Length: 244
Subcellular Location: Periplasm
EC: 4.2.1.1
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H8ZKW0 | MSSTALYTVPTAGPDDVAALKALDGHSASDILAVIGKTEGNGCVNDFSRTLSAAVWHPLLEDSAITVFSGGAEGVISPHVNIFVRDERQYSGHPRGLVTAVGRTRVIGPEEIGRPAQVDAVHETVVALLTELGVGPDDVHLVLIKCPLLSSDAIAGVHRRGLRPVTTDTYESMSRSRAASALGIAMALKECDRDRALLALEGRDDVWSARASASSGAELDDCHILVVAESDAAANPLRAAHTAMRDALDIQALTEVFDRIAAEGGTVRQIFAKAEADPSGAIRGYRHTMLTDSDVNATRHARAAVGGLIAALHGNGAVYVSGGAEHQGPSGGGSVTVIYDVPATANATGEASR | Function: Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret (By similarity). Required for growth on melamine or cyanuric acid as sole nitrogen source .
Catalytic Activity: cyanurate + H2O = 1-carboxybiuret + H(+)
Sequence Mass (Da): 36576
Sequence Length: 353
Domain: The monomer structure is formed from three repeating units (RUs) that share the same structure as one another. The monomer, the active site and substrate all possess threefold rotational symmetry, to the extent that the active site possesses three potential Ser-Lys catalytic dyads. It is possible that any or all of the three active-site serines may act as nucleophile (albeit only one can do so per catalytic cycle).
Pathway: Xenobiotic degradation; atrazine degradation; biuret from cyanurate: step 1/1.
EC: 3.5.2.15
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U3N9N6 | MAPIEILKFPISSPGDISPLKKLQDAGYDPSNILAVVGKTEGNGCVNDFSRTLASAVWEPRIPSDAVTIFSGGTEGVLSPHVTFFLRSPGDKETGLSAAVGHTRRFEPHEIGTDEQAQQVATTTSSLIEQMGVTPDQVHMVLIKCPLLTSEKLETIRALGRVPVTTDTYESMARSRYASAVGIAAAVGEIQHTRIPEAVSKAGTWSAKASCSSGAELEDCHILVLASTSAQGSRLHAVSRPMADAMDAASILALMELAKKDGGKIVQVFAKAEADPSGHVREWRHTMNTDSDIHSTRHARAAVGGLIAGLVSDAEIYVSGGAEGQGPSGGGSLCLVYETSI | Function: Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret. Only active on cyanuric acid and N-methylisocyanuric acid.
Catalytic Activity: cyanurate + H2O = 1-carboxybiuret + H(+)
Sequence Mass (Da): 35773
Sequence Length: 341
Domain: The monomer structure is formed from three repeating units (RUs) that share the same structure as one another. The monomer, the active site and substrate all possess threefold rotational symmetry, to the extent that the active site possesses three potential Ser-Lys catalytic dyads. It is possible that any or all of the three active-site serines may act as nucleophile (albeit only one can do so per catalytic cycle).
Pathway: Xenobiotic degradation; atrazine degradation; biuret from cyanurate: step 1/1.
EC: 3.5.2.15
|
Q8XA35 | MSESLHLTRNGSILEITLDRPKANAIDAKTSFEMGEVFLNFRDDPQLRVAIITGAGEKFFSAGWDLKAAAEGEAPDADFGPGGFAGLTEIFNLDKPVIAAVNGYAFGGGFELALAADFIVCADNASFALPEAKLGIVPDSGGVLRLPKILPPAIVNEMVMTGRRMGAEEALRWGIVNRVVSQAELMDNARELAQQLVNSAPLAIAALKEIYRTTSEMPVEESYSYIRSGVLKHYPSVLHSEDAIEGPLAFAEKRDPVWKGR | Function: Catalyzes the reversible dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA.
Catalytic Activity: (R)-carnitinyl-CoA = crotonobetainyl-CoA + H2O
Sequence Mass (Da): 28137
Sequence Length: 261
Pathway: Amine and polyamine metabolism; carnitine metabolism.
EC: 4.2.1.149
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A0A1V6PAA5 | MATEKTPDWKIVDLQWAPDLGPVPVQDAMRPTRESQGEQEMIARMWVMCAIQMQDKLCAAKCTKQHFERYRSWLTAEYERFKQPGYPQVPDSRELVDMSNDARLAAMNKLREGVKNTYMWPVIEGPWRVYDNVVDIVEGRVKLVKVLLQDGLLEKFYDWANGLSEVRPLFNRMGRSNSSLRILEIGAGTGGTTARALEGLKSDDGELLYSSYEFTDISPLFFDAARRRFEGYSNIEYRALDISRNAVEQGFEAGAYDLVIASNVLHATPCLVDTLKNVRLLLKPNGFLFNQELSPPGKYVDFMVGLLPGWWLGDADGRAEGPCIPPEEWHRRLEQAGFEGLHAVGFDSDPPYYYNANMIARPAVNA | Function: Methyltransferase; part of the gene cluster that mediates the biosynthesis of calbistrin A and related compounds. Calbistrin A is a secondary metabolite with an interesting structure that was recently found to have bioactivity against leukemia cells. It consists of two polyketides linked by an ester bond: a bicyclic decalin containing polyketide and a linear 12 carbon dioic acid structure . The polyketide synthase calA is probably responsible for forming the decalin moiety. Because calA lacks a designated enoylreductase (ER) domain, the required activity is provided by the trans-enoyl reductase calK . Following release from the PKS, calF then probably catalyzes the oxidation and the subsequent Diels Alder cycloisomerization that lead to the formation of the decalin moiety (Probable). The decalin polyketide backbone includes two C-methyl groups, at C7 and C11 in backbone, of which the C7 position is probably methylated by the methyltransferase domain of calA. A candidate for adding the methyl group at C11, if not done by CalA, is the cluster methyltransferase calH (Probable). Several additional tailoring enzymes within the cluster could be involved in the modification of the decalin polyketide product. Those include the 3 cytochrome P450 monooxygenases CalE, CalG and CalL, of which one might be responsible for the introduction of the extra hydroxyl group attached to the backbone of the decalin moiety, at position C9 in the backbone, that allows for attachment of the linear moiety (Probable). One tailoring enzyme activity that is expected to be involved in biosynthesis of calbistrin is an acyltransferase for connecting the two polyketide synthase products, and which could be performed by the cluster acyltransferase calJ (Probable). The enzyme responsible for the biosynthesis of the linear moiety, probably a second PKS, has not been identified yet (Probable).
Sequence Mass (Da): 41501
Sequence Length: 366
Pathway: Secondary metabolite biosynthesis.
EC: 2.1.1.-
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A0A1V6PAN1 | MALDRYAALHVSTPQGRGDGRPTADQVLRDQDPLGSHWSDKVILITGGTAGLGAESARVLHKTGAKIFIMGRDIAKGEKVAADISASNPDYPPIEVIQMDQSRLESVREGAVEFLKRSGGKLNVLMANAGIVASPVKETQDGFEAVFAINYLSTFLLVQLLAPALVASTTPEYNSRLVVVSSAGHRASNIDPDKYNLVGEGYDPSKAYARSKTASILMANEFERRYGDRGVHALSLNPGIIMDTEISRGLPGTSASRREQYYKMEPLLAQYEKDVMQGAATQVWATVAKELEGKGGLYLDDVQVAREATHEGQFCRPGWKPWIWNEDNAVRLWKDSLNMVGLESEN | Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of calbistrin A and related compounds. Calbistrin A is a secondary metabolite with an interesting structure that was recently found to have bioactivity against leukemia cells. It consists of two polyketides linked by an ester bond: a bicyclic decalin containing polyketide and a linear 12 carbon dioic acid structure . The polyketide synthase calA is probably responsible for forming the decalin moiety. Because calA lacks a designated enoylreductase (ER) domain, the required activity is provided by the trans-enoyl reductase calK . Following release from the PKS, calF then probably catalyzes the oxidation and the subsequent Diels Alder cycloisomerization that lead to the formation of the decalin moiety (Probable). The decalin polyketide backbone includes two C-methyl groups, at C7 and C11 in backbone, of which the C7 position is probably methylated by the methyltransferase domain of calA. A candidate for adding the methyl group at C11, if not done by CalA, is the cluster methyltransferase calH (Probable). Several additional tailoring enzymes within the cluster could be involved in the modification of the decalin polyketide product. Those include the 3 cytochrome P450 monooxygenases CalE, CalG and CalL, of which one might be responsible for the introduction of the extra hydroxyl group attached to the backbone of the decalin moiety, at position C9 in the backbone, that allows for attachment of the linear moiety (Probable). One tailoring enzyme activity that is expected to be involved in biosynthesis of calbistrin is an acyltransferase for connecting the two polyketide synthase products, and which could be performed by the cluster acyltransferase calJ (Probable). The enzyme responsible for the biosynthesis of the linear moiety, probably a second PKS, has not been identified yet (Probable).
Sequence Mass (Da): 37767
Sequence Length: 346
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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P0CU81 | MSDFDALLANYTSKETPKVHGVICKCVDRHGICPTPHLAKRDLRLTLLGNEIYSKVAGYDSVLPGASPLREDVVLKVASATKLITSIALLQCIDKGLIDLDEPVTKVLPEFDQKQILTDVSGSDLVLEPSKTPITARHLLTHTSGLGYPFTHRLLRLRAEVRNRAGVSPSLRVTERYEMPLVFEPGTGWLYGCSLDWAGVIVSRLHGGISLEQYFVENIWQRLGLSEPFPCFNIARHPEYNARVMGGAIQTPEGRLQPKDHWAFDNPEDQDGGSGLSCTTKDYVAVLADLVSDSPKLLKPATIAEMFTPQLEAKSPGVQMLLGLRPAWDTVSGPIAENAINHGLGGVLCMDDVPEIDQPKGMLGWGGASNIVWWVNRELRVAGFFATQQAPFGNPSVTRLVNAWKKDFWAQFKTIDHA | Function: Acyltransferase; part of the gene cluster that mediates the biosynthesis of calbistrin A and related compounds. Calbistrin A is a secondary metabolite with an interesting structure that was recently found to have bioactivity against leukemia cells. It consists of two polyketides linked by an ester bond: a bicyclic decalin containing polyketide and a linear 12 carbon dioic acid structure . The polyketide synthase calA is probably responsible for forming the decalin moiety. Because calA lacks a designated enoylreductase (ER) domain, the required activity is provided by the trans-enoyl reductase calK . Following release from the PKS, calF then probably catalyzes the oxidation and the subsequent Diels Alder cycloisomerization that lead to the formation of the decalin moiety (Probable). The decalin polyketide backbone includes two C-methyl groups, at C7 and C11 in backbone, of which the C7 position is probably methylated by the methyltransferase domain of calA. A candidate for adding the methyl group at C11, if not done by CalA, is the cluster methyltransferase calH (Probable). Several additional tailoring enzymes within the cluster could be involved in the modification of the decalin polyketide product. Those include the 3 cytochrome P450 monooxygenases CalE, CalG and CalL, of which one might be responsible for the introduction of the extra hydroxyl group attached to the backbone of the decalin moiety, at position C9 in the backbone, that allows for attachment of the linear moiety (Probable). One tailoring enzyme activity that is expected to be involved in biosynthesis of calbistrin is an acyltransferase for connecting the two polyketide synthase products, and which could be performed by the cluster acyltransferase calJ (Probable). The enzyme responsible for the biosynthesis of the linear moiety, probably a second PKS, has not been identified yet (Probable).
Sequence Mass (Da): 45973
Sequence Length: 418
Pathway: Secondary metabolite biosynthesis.
EC: 2.3.1.-
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A0A1V6PAP3 | MSSPIQTAIVQTSETSAARLPLRVDRSAPIPQVKSEHHVLVRVLAVALNPNDHKMVTHFNMPDSIAGCDFCGIVTESSSNGTSLSSSAGARLPVGTRVCGALFPYSPEDPDNGSFAQYCVVDARLLVRVPDSWSDLEAASLGVGWSTISLAFSDPNALGLEGLPTQPSHRAKEPVLVYGGGTASGTLACQLLNLMGYTPIAIASNQSSELAMKYGASATACYTSKDCVDTVKSLAGKPIRRILDCITDAESAAICYSAMARSSGTYACLEECPDACRTRRIIKVKEVMGFQVLGVDIKLGDSTYTRLGDQKLMAIGIQWANEIQALMESGQLKAHPLRELPGGWEAIIEGLEMLRNGEVRGQKLVVRIPQE | Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of calbistrin A and related compounds. Calbistrin A is a secondary metabolite with an interesting structure that was recently found to have bioactivity against leukemia cells. It consists of two polyketides linked by an ester bond: a bicyclic decalin containing polyketide and a linear 12 carbon dioic acid structure . The polyketide synthase calA is probably responsible for forming the decalin moiety. Because calA lacks a designated enoylreductase (ER) domain, the required activity is provided by the trans-enoyl reductase calK . Following release from the PKS, calF then probably catalyzes the oxidation and the subsequent Diels Alder cycloisomerization that lead to the formation of the decalin moiety (Probable). The decalin polyketide backbone includes two C-methyl groups, at C7 and C11 in backbone, of which the C7 position is probably methylated by the methyltransferase domain of calA. A candidate for adding the methyl group at C11, if not done by CalA, is the cluster methyltransferase calH (Probable). Several additional tailoring enzymes within the cluster could be involved in the modification of the decalin polyketide product. Those include the 3 cytochrome P450 monooxygenases CalE, CalG and CalL, of which one might be responsible for the introduction of the extra hydroxyl group attached to the backbone of the decalin moiety, at position C9 in the backbone, that allows for attachment of the linear moiety (Probable). One tailoring enzyme activity that is expected to be involved in biosynthesis of calbistrin is an acyltransferase for connecting the two polyketide synthase products, and which could be performed by the cluster acyltransferase calJ (Probable). The enzyme responsible for the biosynthesis of the linear moiety, probably a second PKS, has not been identified yet (Probable).
Sequence Mass (Da): 39601
Sequence Length: 371
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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Q9STD3 | MKWGVVAVLATLVVAASAKDYFKETFDGSWADRWTKSSWKVSDGSAGEFKLTAGKWYGDAEADKGIQTGPDSKFFAISAPLATVFDNTGKDTVVQFSVKHEQDLDCGGGYIKVVPATSEKQMGEFGGDTPYSIMFGPDICGYSTRKVHVILTYKGKNYLIKKDIKAETDQLTHVYTLVIKPDNTYQVLIDLKEVASGSLYEDWDMLPPKTIKDPKASKPEDWDEREEIADPEDKKPEGWDDIPATIADKDAKKPEDWDDEEDGTWEPPMIPNPEYKGEWKAKMIKNPAYKGIWVAPDIDNPDYVHDDKLYNFKDLKFVGFELWQVKSGSIFDNILVTDDLEAAKKFAEDTWGKHKDEEKAMFDKVKKEEDEKKAKDAPPPPVDAEAAEEEDDEYEDKEEPSGMGSIKIPKEEEESGHDEL | Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
Sequence Mass (Da): 47328
Sequence Length: 420
Domain: Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity (By similarity).
Subcellular Location: Endoplasmic reticulum lumen
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Q23858 | MRLLLCLIFLVFVFNFALSTVHFKDTFDNDWESRWVVSDWHKEDGKSGKLVHTAGKWFGDENQKGIQTSEDARFYAVSAKFPSFSNKGKDLVLQYTVKNEQKVDCGGSYIKLLPSKLDQSAFDGESEYSIMFGPDVCGASKRVHVILNYKGKNHLIKKEINKVETDQLTHQYTLVISPDNTYKVLVDNKEIQAGNLADDWELLPSKQIKDPKQSKPVDWVDVKEIDDPEDVKPAGHDDIPASIVDPEAVKPEDWNEEDDGEWEAPTIANPEYKGEWKAKKIPNPEYKGEWVHPLIDNPEYAEDNELYLFNDLGAIGFELWQVKSGSIFNNMIVTDSVEEAKDFSEKTFVANQEAEKKMFDDLEAAKAEERKKADEKLAAEKAAEKEAEEADEEEEEVAEEDLVKTDDKKEEVKKSTKKVDHDEL | Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
Sequence Mass (Da): 48365
Sequence Length: 424
Domain: Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity (By similarity).
Subcellular Location: Endoplasmic reticulum lumen
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P83003 | MFTLFLLIALSSAKVYFHETFENRDKWIDSTSSGKALGPFKIVSGKWYGDANNKGLQTSEDNKFYIAAAKLDEEFSNKDKNLIVQYNLKFEQGIDCGGGYIKLLPKKSIESEEKFTPESEYNIMFGPDVCGGSKRTHVIMNYKGKNNLIRKEIKCESDDISHLYTLIIRPNNTYVVKIDGVEKQEGKFDEDWDMLAPKEIDDPNVSKPADWVDEKEIDDPNDKKPEGWDDIPKTIVDPNAKKPEEWNDEDDGEWEAPTIENPEYKGEWKPKRIPNPAYKGEWVHPQIANPDYVYDPELYKYDSFAYIGIDVWQVKAGTIYDDILITDDIEEAEKEAKVILERNAAEKKMRDEIKEAEKQKEEEAKKEAEKQKEEETKEEIKKEENKEEL | Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Plays a role in host cell phagocytosis, possibly by acting as a receptor for host C1q . Binding to C1q prevents the activation of the host classical complement pathway . Also, binds to apoptotic host cells independently of host C1q and collectins .
Sequence Mass (Da): 45080
Sequence Length: 389
Domain: Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity.
Subcellular Location: Endoplasmic reticulum lumen
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Q9ZNY3 | MRKELWLGLLLSSQAVLSTIYYKETFEPDWETRWTHSTAKSDYGKFKLTSGKFYGDKAKDAGIQTSQDAKFYAISSPIASSFSNEGKDLVLQFSVKHEQDIDCGGGYLKLLPSVDAAKFTGDTPYHIMFGPDICGATKKIHFILTYKGKNLLWKKEPRCETDTLSHTYTAVIKADRTYEVLVDQVKKESGTLEEDWEILKPKTIPDPEDKKPADWVDEPDMVDPEDKKPEDWDKEPAQIPDPDATQPDDWDEEEDGKWEAPMISNPKYKGEWKAKKIPNPAYKGVWKPRDIPNPEYEADDKVHIFDEIAAVGFDLWQVKSGTIFDNIIVTDSLAEAKAFYDQTNGATKDAEKKAFDSAEADKRKKEEDERKKQEEEEKKTAEEDEDDDDEEEEEDDKKDEL | Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
Sequence Mass (Da): 45911
Sequence Length: 401
Domain: Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity (By similarity).
Subcellular Location: Endoplasmic reticulum lumen
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P27797 | MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL | Function: Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER . Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export . Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy (By similarity).
Sequence Mass (Da): 48142
Sequence Length: 417
Domain: Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity.
Subcellular Location: Endoplasmic reticulum lumen
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Q9SP22 | MAIRKGSSYAVAALLALASVAAVAGEVFFQEKFEDGWESRWVKSEWKKDENMAGEWNHTSGKWNGDAEDKGIQTSEDYRFYAISAEYPEFSNKDKTLVLQFSVKHEQKLDCGGGYVKLLGGDVDQKTLGGDTSYSIISRPDISRYSTKKVHTILTKDGKNHLIKKDVPCQTDQLTHVYTFIIRPDATYSILIDNEEKHTGSIYEHWDILPPKKIKDPEAKKPEDWDDKEYIPDPEDKKPEGYDDIPKEIPDPDAKKPEDWDDEEDGEWTAPTIPNPEYKGPWKQKKIKNPNYQGKWKAPMIDNPDFKDDPYIYAFDSLKYIGIELWQVKSGTLFDNIIITDDPALAKTFAEETWGKHKEAEKAAFDEAEKKKEEEDAAKGGDDEDDDLEDEEDDEKADEDKADSDAEDGKDSDDEKHDEL | Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
Sequence Mass (Da): 47940
Sequence Length: 420
Domain: Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity (By similarity).
Subcellular Location: Endoplasmic reticulum lumen
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Q9SLY8 | MAIRARSSSYAAAAVALALALASVAAVAGEVFFQEKFEDGWESRWVKSEWKKDENMAGEWNHTSGKWNGDPEDKGIQTSEDYRFYAISAEYPEFSNKDKTLVLQFSVKHEQKLDCGGGYVKLLGGDVDQKKFGGDTPYSIMFGPDICGYSTKKVHTIFTKNDKNHLIKKDVPCETDQLSHVYTLIIHPDATYTILIDNVEKQSGSIYEHWDILPPKQIKDPEAKKPEDWDDKEYIPDPEDKKPEGYDDIPKEIPDPDAKKPEDWDDEEDGEWTAPTIPNPEYKGPWKQKKIKNPNYQGKWKAPMIDNPDFKDDPYIYAFDSLKYIGIELWQVKSGTLFDNFLITDDPELAKTFAEETWGKHKDAEKAAFDEAEKKKEEEEAAKAGEDDDDLDDEDAEDEDKADEKADSDAEDGKDSDDEKHDEL | Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
PTM: Phosphorylated.
Sequence Mass (Da): 48309
Sequence Length: 424
Domain: Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity (By similarity).
Subcellular Location: Endoplasmic reticulum lumen
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Q9D805 | MPYLHRSLRPQPQPVPGDARTIHSSGQSFEQLRQGCLQSGTLFEDADFPASNVSLFYSERPQVPFVWKRPGEIVEKPEFILGGATRTDICQGELGDCWLLAAIASLTLNQKALTRVVPQDQGFGSGYAGIFHFQFWQHSEWLDVVIDDRLPTFKDRLVFLHSADHNEFWSALLEKAYAKLNGSYEALKGGSAIEAMEDFTGGVAENFQIREAPEDFFEILEKALKRGSLLGCSIDTLNASESEARTSLGLIKGHAYTVTGLDQVNFHGQRIKLIRVRNPWGQVEWNGPWSDSSPEWRSVDLEEQKRLGHTALDDGEFWMAFKDFKIHFDKVEICNLTPDALEDSALHRWEVTIHQGSWVRGSTAGGCRNFLDTFWTNPQIKLSLTERDEGQEGCTFLAALMQKDRRRLKRFGANMLTIGYAIYQCPDKDGHLSRDFFRYHASLARSKTFINLREVSERFQLPPGDYILIPSTFEPHQEADFCLRIFSEKRAVTRDLDENIDIDLPELPKPTPQEEETEEEQQFRALFQRVAGEDMEVSAEELEYVLNAVLQKKTALKFKRLSLLSCRNIISLMDTSGNGKLEFEEFRVFWDKLKHWMDLFLQFDVDKSGTMSSYELRTALKAAGFQLGGHLLQLIVLRYADEDLQLDFDDYLNCLVRLENASRVFQSLSVKNKDFIHLNINEFISLTMNI | Function: Calcium-regulated non-lysosomal thiol-protease.
Sequence Mass (Da): 78977
Sequence Length: 690
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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D0PX84 | MIMRMTLTLFVLVVMTAASASGDALTEAKRIPYCGQTGAECYSWCIKQDLSKDWCCDFVKDIRMNPPADKCP | Function: Neurotoxin that induces excitatory symptoms in mice following intracranial administration. No symptoms are observed after intraperitoneal and intravenous (tail vein) injections.
Sequence Mass (Da): 8040
Sequence Length: 72
Domain: The cysteine framework is XXIII (C-C-C-CC-C).
Subcellular Location: Secreted
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Q11002 | MDDLRGFLRQAGQEFLNAAGEAAMGAAKDVVGSVINEIFIKKEADTKRVLPSIKNMRVLGEKSSSLGPYSEVQDYETILNSCLASGSLFEDPLFPASNESLQFSRRPDRHIEWLRPHEIAENPQFFVEGYSRFDVQQGELGDCWLLAATANLTQESNLFFRVIPAEQSFEENYAGIFHFRFWQYGKWVDVIIDDRLPTYNGELMYMHSTEKNEFWSALLEKAYAKLHGSYEALKGGSTCEAMEDFTGGVSEWYDLKEAPGNLFTILQKAAERNSMMGCSIEPDPNVTEAETPQGLIRGHAYSITKVCLIDIVTPNRQGKIPMIRMRNPWGNEAEWNGPWSDSSPEWRYIPEEQKAEIGLTFDRDGEFWMSFQDFLNHFDRVEICNLSPDSLTEDQQNSGKRKWEMSMYEGEWTPGVTAGGCRNFLDTFWHNPQYIITLVDPDEEDEEGQCTVIVALMQKNRRSKRNMGMECLTIGFAIYSLNDRELENRPQGLNFFRYKSSVGRSPHFINTREVCARFKLPPGHYLIVPSTFDPNEEGEFIIRVFSETQNNMEENDDHVGYGGKADTITPGFPTPKPIDPQKEGLRRLFDSIAGKDMEVDWMELKRILDHSMRDDLPKPVVFNRFSNNMAFETQAAGPGDDGAGACGLLSLICGPFLKGTPFEEQLGMNDQSNKRLIGDNPADGGPVTANAIVDETHGFSKDVCRSMVAMLDADKSGKLGFEEFETLLSEIAKWKAIFKVYDVENTGRVSGFQLREALNSAGYHLNNRVLNVLGHRYGSRDGKIAFDDFIMCAVKIKTYIDIFKERDTEKNETATFTLEEWIERTIYS | Function: Calcium-regulated non-lysosomal thiol-protease. Involved in the organization of the actin-related cytoskeleton during embryogenesis.
PTM: Undergoes calcium-dependent autolytic cleavage between Lys-54 and Asn-55, which is necessary for activation of the protein.
Sequence Mass (Da): 93963
Sequence Length: 828
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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P63098 | MGNEASYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNPLVQRVIDIFDTDGNGEVDFKEFIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVGNNLKDTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDV | Function: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 19300
Sequence Length: 170
Subcellular Location: Cytoplasm
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A1RZN3 | METPRLMCTQHPDSTVKVPVQEEVEEAVRSFLVYGCDEVMSDYEGKLTPYAQPKEIVVKAGELGVPVGEGFYVTVRAPNPRLEDFDRVDLALEAAVLANYYSYKRLGVQAVRWVVLPMTDSAETVRLVQRLLARKTRVLCEEVGQPCEQAQLVPLLEDVDSLLRVREILRDLHSALAELGSDPGVLRVFLGKSDSALKAGHIASALSLLYALGESAKAGEELGLEVKPILGGGSPPFRGGVNNPRLVGVEVQRYRGYSTVTVQSAVRYDASFSEYQEVRSKLLGGAGGEPGDAGGRVAELARLAASMYRSLASKYLDFVNEYARSVPTTRDRVSWREYGRALELEDKLFSAPRAIVYTAAWYSLGVPPTFLDADFVLEAYRGDFLDEVLGYLPGLEEEWRYDAQFYLPRLAGERLGEELVKKVDEALDAMGLRPEPLEPYEKLARTAPAELRALLLGKVRGFLG | Function: Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Mass (Da): 51243
Sequence Length: 464
EC: 4.1.1.31
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Q6F6Q6 | MIQQIDAPLREDVRLLGNLLGETLKQHAGQDLFNQIEQIRALAKGARDGQAETEKKLEQLFLDLKDEEILPLTRAFSYFLNFANIAEQYHVVRSRRRSEFDEQGPPPNPLIHLFEKFKQNQISSKQLFQQVSNLSIELVLTAHPTEVSRRTLIQKYDDINEGLSKLDQQKLTPRERQQVLDDLKQLICSAWQTDEIRQNKPTPLDEAKWGFTTIEQTLWNAVPKFVRELDTLVHQHCDAHLPLDISPIRFASWMGGDRDGNPNVTHNVTQEVLWLSRWQAADLYLRDIEDLRWELSIQACSEELSQTLGRRHPEPYREYLRSTRERLKATRQWLSLRLQGLDGDDSQIIRHKQELLDPLLLCHRSLMECNLPEIANGKLLDFIYRVNCFGIELLKLDIRQESGRHRQAISAITEYLGLGNFESWTEQARQNFLIQELQSKRPLLPKYLNEPEGSLIEHPDVKEVFATMRTLAEQPPESLGAYIISMAEYASDVLAVLLLQKEAGILQPLRVVPLFETLKDLDGAAKTMETLFNMHWYKQHIQGKHEVMIGYSDSAKDAGFMSANWAQYRAQEELTAVAKSHGVQLTLFHGRGGSISRGGAPTQQALFSQPPGSISGAIRVTEQGEMIRFKFGLEGVALQNLEIYTAATLEATLLPPPVPKQEWRDLMHQMTDISVRVYRETVRENPHFVQYLRTVTPELELQMLPLGSRPAKRKVSGGIESLRAIPWVFAWTQIRLMLPAWLGTGAAINQVIDENKKAVLDEMLAEWPYFQTLIDMLEMVLSKSDANIALYYESHLTDNEDLKILGEMLRQRLNDAVQTLLSMKGESKLLSKNDVLDQAMQVRKPYLLPLHLLQAELMKRRRLYTAQSNAERTPVDHALMVSIAGIAAGLRNTG | Function: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Mass (Da): 102249
Sequence Length: 894
EC: 4.1.1.31
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A1K454 | MTPDKDAPLREDIRLLGRLLGDTVRDQQGAASFDLIERIRQTSVRFRRDEDLAARRELEDTLDALSREQTIQVVRAFSYFSHLANIAEDQHHIRRSRAHLLAGSAPREGSLAHAVGHALDEQRLDPTDLAAFFDTALISPVLTAHPTEVQRKSILNCQTVIARLLDERDRMQLTPDEAEANLDALRRAVLTLWQTRMLRPAKLSVIDEVNNGLSYFETTFLRELPRLYAALEDRLAGAQPALANHELPAFLQVGSWIGGDRDGNPYVTADVLEEALAMQARVALDYYLDELHTLGSQLSLSQGLVGASDALLALADRSPDQSPHRSDEPYRRAIAGIYARLSATYRNLLGHPPARHAVAEAEPYADVAALADDLDTLHRSLVANGTAALARGRLRHLRRAVRVFGFHLAPIDLRQNSDVHERVVAELLEVARPGAAYLAQDEAGRCALLLDELATARPLASPHVRYSDDSEGELAIFRAARRAHLRYGRGAIHNCIISKTDDLSDLLELAVLLKEAGLLRPLEKALDVNIVPLFETIGDLENAAGVMDRLFSIPVYRELLAARDQTQEVMLGYSDSNKDGGFLTSGWALYKAEGELVEVFGRHGVRLRLFHGRGGSVGRGGGPSYQAILAQPDGAVQGQIRLTEQGEVIAAKYGNPEVGRRNLEVLVAATLETSLRRDGGDATPRTFLDTMQALSDAAFTCYRGLVYETPGFEQYFWESTVISEIAGLNIGSRPASRKKGTRIDDLRAIPWVFSWSQCRLMLPGWFGFGSAVKQWLAAHPKDGLGLLQRMYREWSFFATLLSNMDMVLSKTDLAIASRYAELVKDPVLRDSIFERIRSEWKDTVDALLAITEQVELLDANPLLKRSIRNRFPYLDPLNHVQVELLRRHREGNGEDARIRNGIHISINGIAAGLRNSG | Function: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Mass (Da): 101775
Sequence Length: 917
EC: 4.1.1.31
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Q7W0D0 | MAAYNAPVSNCQFRLTHILPIPQRHGAPTDPFQMNAIRQQSDSAEPLRHDIRLLGRCLGEVIQACEGKRVYDTIETLRRTAVRFRRAGDPADDKLLQARVKQLRGNDPNSVARAFSYFLHLSNIAEDRDQNRRQRERALAGAGPERGSLRQAIESLKAQGVNNARIRRLLSEACVMPVLTAHPTEVQRKSTLDVHREISSLLVQRERELTADELSELDLALIGQVATLWQTRMLRYTRLTVADEIENALSYYRSTFLNVIPRVYGDLARLLNREPVKPFTPPPPPLEPFLRMGSWIGGDRDGNPNVDAATLERALLRQATVLFEHYLQEVHALGAELSASTLLIEADPALLALADAGGDDSPHRRDEPYRRALIGIYARLAATARHLTGQKLARRATVPAAPYDTPDALAADLAVIAASLSARHGAPIARLRLSGLQQAVTVFGFHLATVDLRQSSDVHERVLAELFARAGDGIDGQAVDYLALDEAARVAGRELAHARPLASPWIAYSEETASELAVLRAAAAGRARYGRQAVLQSIVSHTETLSDLLEVLVLQKEAGLIAPPGETIAPGDGLMVVPLFETIPDLQRGPEIMAAWLDLPEVRQRVRLAQGDTQEVMLGYSDSNKDGGFLTSNWSLYQAERALVDVFSARSVRLRMFHGRGDSVGRGGGSSYDAILAQPPGTVAGQLRLTEQGEVIQSKYKDAEVGRWHLELLVAATLESSLAPQAAATSAEDAHMQQHAPAMSFMSELAQRTYRGLVYDTPGFADYFFAATPISEIAGLNIGSRPASRKKGQHIEDLRAIPWGFSWAQCRLMLTGWYGMGSAIEAYLETGAQGAPRSRRARLAQLREMASDWPAFRTLLSNMEMVLAKSDLAIAAGYAQLVPRRGLRERVFGAITAEHGRTLAMLRLLTRRDLLADNPGLMASLRERFAYIDPLNYLQIELIKRHRAAQRRAGDDADIRVPRAIHLTINGIAAGLRNSG | Function: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Mass (Da): 107774
Sequence Length: 980
EC: 4.1.1.31
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Q14444 | MPSATSHSGSGSKSSGPPPPSGSSGSEAAAGAGAAAPASQHPATGTGAVQTEAMKQILGVIDKKLRNLEKKKGKLDDYQERMNKGERLNQDQLDAVSKYQEVTNNLEFAKELQRSFMALSQDIQKTIKKTARREQLMREEAEQKRLKTVLELQYVLDKLGDDEVRTDLKQGLNGVPILSEEELSLLDEFYKLVDPERDMSLRLNEQYEHASIHLWDLLEGKEKPVCGTTYKVLKEIVERVFQSNYFDSTHNHQNGLCEEEEAASAPAVEDQVPEAEPEPAEEYTEQSEVESTEYVNRQFMAETQFTSGEKEQVDEWTVETVEVVNSLQQQPQAASPSVPEPHSLTPVAQADPLVRRQRVQDLMAQMQGPYNFIQDSMLDFENQTLDPAIVSAQPMNPTQNMDMPQLVCPPVHSESRLAQPNQVPVQPEATQVPLVSSTSEGYTASQPLYQPSHATEQRPQKEPIDQIQATISLNTDQTTASSSLPAASQPQVFQAGTSKPLHSSGINVNAAPFQSMQTVFNMNAPVPPVNEPETLKQQNQYQASYNQSFSSQPHQVEQTELQQEQLQTVVGTYHGSPDQSHQVTGNHQQPPQQNTGFPRSNQPYYNSRGVSRGGSRGARGLMNGYRGPANGFRGGYDGYRPSFSNTPNSGYTQSQFSAPRDYSGYQRDGYQQNFKRGSGQSGPRGAPRGRGGPPRPNRGMPQMNTQQVN | Function: mRNA-binding protein that acts as a regulator of mRNAs transport, translation and/or stability, and which is involved in synaptic plasticity in neurons and cell proliferation and migration in multiple cell types . Acts as an mRNA regulator by mediating formation of some phase-separated membraneless compartment: undergoes liquid-liquid phase separation upon binding to target mRNAs, leading to assemble mRNAs into cytoplasmic ribonucleoprotein granules that concentrate mRNAs with associated regulatory factors . Undergoes liquid-liquid phase separation following phosphorylation and interaction with FMR1, promoting formation of cytoplasmic ribonucleoprotein granules that concentrate mRNAs with factors that inhibit translation and mediate deadenylation of target mRNAs . In these cytoplasmic ribonucleoprotein granules, CAPRIN1 mediates recruitment of CNOT7 deadenylase, leading to mRNA deadenylation and degradation . Binds directly and selectively to MYC and CCND2 mRNAs . In neuronal cells, directly binds to several mRNAs associated with RNA granules, including BDNF, CAMK2A, CREB1, MAP2, NTRK2 mRNAs, as well as to GRIN1 and KPNB1 mRNAs, but not to rRNAs .
PTM: Tyrosine phosphorylation by EPHA4 promotes interaction with FMR1 and liquid-liquid phase separation (LLPS) for the formation of a membraneless compartment that concentrates mRNAs with associated regulatory factors.
Sequence Mass (Da): 78366
Sequence Length: 709
Domain: The C-terminal disordered region undergoes liquid-liquid phase separation (LLPS) for the formation of a membraneless compartment that concentrates mRNAs with associated regulatory factors . CAPRIN1 molecules in the condensed phase are neutral . mRNA-binding promotes phase separation . Moderate concentrations of ATP enhance phase separation by reducing the electrostatic potential of CAPRIN1, thereby promoting intermolecular interactions . In contrast, high concentrations of ATP invert the electrostatic potential of CAPRIN1, so that CAPRIN1 molecules become negatively charged, lead to inhibition of phase separation .
Subcellular Location: Cytoplasm
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Q60865 | MPSATSHSGSGSKSSGPPPPSGSSGSEAAAGAAAPASQHPATGTGAVQTEAMKQILGVIDKKLRNLEKKKGKLDDYQERMNKGERLNQDQLDAVSKYQEVTNNLEFAKELQRSFMALSQDIQKTIKKTARREQLMREEAEQKRLKTVLELQYVLDKLGDDDVRTDLKQGLSGVPILSEEELSLLDEFYKLVDPERDMSLRLNEQYEHASIHLWDLLEGKEKPVCGTTYKALKEIVERVFQSNYFDSTHNHQNGLCEEEEAASAPTVEDQVAEAEPEPAEEYTEQSEVESTEYVNRQFMAETQFSSGEKEQVDEWTVETVEVVNSLQQQPQAASPSVPEPHSLTPVAQSDPLVRRQRVQDLMAQMQGPYNFIQDSMLDFENQTLDPAIVSAQPMNPTQNMDMPQLVCPQVHSESRLAQSNQVPVQPEATQVPLVSSTSEGYTASQPLYQPSHATEQRPQKEPMDQIQATISLNTDQTTASSSLPAASQPQVFQAGTSKPLHSSGINVNAAPFQSMQTVFNMNAPVPPANEPETLKQQSQYQATYNQSFSSQPHQVEQTELQQDQLQTVVGTYHGSQDQPHQVPGNHQQPPQQNTGFPRSSQPYYNSRGVSRGGSRGARGLMNGYRGPANGFRGGYDGYRPSFSNTPNSGYSQSQFTAPRDYSGYQRDGYQQNFKRGSGQSGPRGAPRGRGGPPRPNRGMPQMNTQQVN | Function: mRNA-binding protein that acts as a regulator of mRNAs transport, translation and/or stability, and which is involved in synaptic plasticity in neurons and cell proliferation and migration in multiple cell types . Acts as an mRNA regulator by mediating formation of some phase-separated membraneless compartment: undergoes liquid-liquid phase separation upon binding to target mRNAs, leading to assemble mRNAs into cytoplasmic ribonucleoprotein granules that concentrate mRNAs with associated regulatory factors (By similarity). Undergoes liquid-liquid phase separation following phosphorylation and interaction with FMR1, promoting formation of cytoplasmic ribonucleoprotein granules that concentrate mRNAs with factors that inhibit translation and mediate deadenylation of target mRNAs (By similarity). In these cytoplasmic ribonucleoprotein granules, CAPRIN1 mediates recruitment of CNOT7 deadenylase, leading to mRNA deadenylation and degradation (By similarity). Binds directly and selectively to MYC and CCND2 mRNAs (By similarity). In neuronal cells, directly binds to several mRNAs associated with RNA granules, including BDNF, CAMK2A, CREB1, MAP2, NTRK2 mRNAs, as well as to GRIN1 and KPNB1 mRNAs, but not to rRNAs (By similarity).
PTM: Tyrosine phosphorylation by EPHA4 promotes interaction with FMR1 and liquid-liquid phase separation (LLPS) for the formation of a membraneless compartment that concentrates mRNAs with associated regulatory factors.
Sequence Mass (Da): 78169
Sequence Length: 707
Domain: The C-terminal disordered region undergoes liquid-liquid phase separation (LLPS) for the formation of a membraneless compartment that concentrates mRNAs with associated regulatory factors. CAPRIN1 molecules in the condensed phase are neutral. mRNA-binding promotes phase separation. Moderate concentrations of ATP enhance phase separation by reducing the electrostatic potential of CAPRIN1, thereby promoting intermolecular interactions. In contrast, high concentrations of ATP invert the electrostatic potential of CAPRIN1, so that CAPRIN1 molecules become negatively charged, lead to inhibition of phase separation.
Subcellular Location: Cytoplasm
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Q5RJ80 | MRKTETMVQLSPSRTLETLTPSELTVEKDDGQGSPKPESPRMLSALQLALSSTTVYCGYEKYIEDGLICLKHKIRNIEKKKLKLERYSDKLKKGEKLNEDQLEAVGKYDEVVHNLKFAKELQKTIGSLTQDLLKAQRKAVRQEKQMKTDEEKSRLSLMLQVQYVLHSLQREDVRKNFCNTRQYSCYMSTQDMEGLMDLASLVGCKRDYSISLEDQMRRAAIVYWELLEGNEKPVAGSTYKHMKEKLLRLVDSGFFDNIPLPKSDSQEKTETIKPDSQSRPSGLTTLVKLSSNEVPSKEFLNRRYMPETDERRRGETASPRNWKEDFLAMKEREPPDSWEMEELADPPASSQSPIQKPWKGAAGLIPKTVDIVKRSTTDPKEKRQRKKAEQDSKSMPVAVEVFSSPSPLPKDPVQRRQQLETLMDQISGSFSFMQESLLDGESSPVNTQTKRCRPSPGSSTPIVQRELTKSPSDILPSSQRSTPLRILLSGEGKGCLSNGDRSINGSDLELHSEDKPRKQAEGFNSPPLYRRGSSISVSLENQSTVQAGRQMLCNGVSSSGSAQTFSTPPSRRSISAENPFHNIHSVFNVIGESSGMKADESGFSESIHRSFTSAKTSSVTTASTQTPPELNPPEEDLQIEGQYPLECAVSAGGPVFSSSHSRVGQSCYSRGAVRGGYDAYRVNVRSPGGSFMSQTHREPASALYMARENGYQQNFKRGAGTATQRSSAGWSDSSQVSSPDRDGAYPLDSGLSDTLSIPAMEVPMNPQGPHTLMPVHVYPLTQLRVAFSAARTANFAPGTLDQPIAFDLLHTNLGDMFDTGSGRFTCPATGAYVFIFHILKLAISVPLYINLMRNEEVMVSAYANDGAPDHETASNHAVLQLFQGDQVWLRLHRGAIYGSSWKYSTFSGFLLYQD | Function: Promotes phosphorylation of the Wnt coreceptor LRP6, leading to increased activity of the canonical Wnt signaling pathway. Facilitates constitutive LRP6 phosphorylation by CDK14/CCNY during G2/M stage of the cell cycle, which may potentiate cells for Wnt signaling. May regulate the transport and translation of mRNAs, modulating for instance the expression of proteins involved in synaptic plasticity in neurons. Involved in regulation of growth as erythroblasts shift from a highly proliferative state towards their terminal phase of differentiation. May be involved in apoptosis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 101570
Sequence Length: 914
Domain: The C1q domain is essential for the function in Wnt signaling.
Subcellular Location: Cytoplasm
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P12871 | MVSKAARRRRAAPRQQQRQQSNRASNQPRRRRARRTRRQQRMAATNNMLKMSAPGLDFLKCAFASPDFSTDPGKGIPDKFQGLVLPKKHCLTQSITFTPGKQTMLLVAPIPGIACLKAEANVGASFSGVPLASVEFPGFDQLFGTSATDTAANVTAFRYASMAAGVYPTSNLMQFAGSIQVYKIPLKQVLNSYSQTVATVPPTNLAQNTIAIDGLEALDALPNNNYSGSFIEGCYSQSVCNEPEFEFHPIMEGYASVPPANVTNAQASMFTNLTFSGARYTGLGDMDAIAILVTTPTGAVNTAVLKVWACVEYRPNPNSTLYEFARESPANDEYALAAYRKIARDIPIAVACKDNATFWERVRSILKSGLNFASTIPGPVGVAATGIKGIIETIGSLWV | Function: Capsid protein alpha self-assembles to form an icosahedral procapsid with a T=3 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins trimers. In addition, 240 calcium ions are incorporated per capsid during assembly. The capsid encapsulates the two genomic RNAs. Capsid maturation occurs via autoproteolytic cleavage of capsid protein alpha generating capsid protein beta and the membrane-active peptide gamma.
PTM: Capsid protein alpha autocatalytically maturates into capsid protein beta and peptide gamma.
Catalytic Activity: Hydrolysis of an asparaginyl bond involved in the maturation of the structural protein of the virus, typically -Asn-|-Ala- or -Asn-|-Phe-.
Sequence Mass (Da): 43067
Sequence Length: 399
Subcellular Location: Virion
EC: 3.4.23.44
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Q83884 | MMMASKDATSSVDGASGAGQLVPEVNASDPLAMDPVAGSSTAVATAGQVNPIDPWIINNFVQAPQGEFTISPNNTPGDVLFDLSLGPHLNPFLLHLSQMYNGWVGNMRVRIMLAGNAFTAGKIIVSCIPPGFGSHNLTIAQATLFPHVIADVRTLDPIEVPLEDVRNVLFHNNDRNQQTMRLVCMLYTPLRTGGGTGDSFVVAGRVMTCPSPDFNFLFLVPPTVEQKTRPFTLPNLPLSSLSNSRAPLPISSMGISPDNVQSVQFQNGRCTLDGRLVGTTPVSLSHVAKIRGTSNGTVINLTELDGTPFHPFEGPAPIGFPDLGGCDWHINMTQFGHSSQTQYDVDTTPDTFVPHLGSIQANGIGSGNYVGVLSWISPPSHPSGSQVDLWKIPNYGSSITEATHLAPSVYPPGFGEVLVFFMSKMPGPGAYNLPCLLPQEYISHLASEQAPTVGEAALLHYVDPDTGRNLGEFKAYPDGFLTCVPNGASSGPQQLPINGVFVFVSWVSRFYQLKPVGTASSARGRLGLRR | Function: Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding histo-blood group antigens present on gastroduodenal epithelial cells.
PTM: May be cleaved by host protease to generate soluble capsid protein. Assembled capsid cannot be cleaved.
Sequence Mass (Da): 56589
Sequence Length: 530
Domain: The shell domain (S domain) contains elements essential for the formation of the icosahedron. The Protruding domain (P domain) is divided into sub-domains P1 and P2. P domain interacts in dimeric contacts that increase the stability of the capsid and form the protrusions on the virion. An hypervariable region in P2 is thought to play an important role in receptor binding and immune reactivity.
Subcellular Location: Virion
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Q9JH65 | MAEKPQQKAVASAAKQLAKEVVKLDKITKSNGKQHPQKNVPARKWRPRQAKPNNRRVTHKIKRELHKQGLEGPASRFRVTVSATIGKVGPNKEQGPELQIATFLHPSLVKEPNDGSNFGPLQAAAAQWGLWRISDLEVRFTPLVGSSAVTGSVTRASLNLTQSPGATSWGGLGARKHLDVPTGVSKVWKLRRGDLTGPRQTWWVTDTNEEGGQSCGPMLEVHGLGKTTSTYKDSDWTGDLFIVELHGTWEFSNYNAKPALGMLERVTDQTNVELGVDTEGQITMTIPENSPMARHMGERFERASASNASSVGETIWQIVDEGAGLASSVAPAPFGWLIKGGWWFVKKILGRAANAGSQYLVYASLADAQNGKPAMSTSRGYVREVKQTILSSTQLNAPNTGPGASQPALAAYEMFPYFPHGEPAVGQPFYLMSTVSTGVYREAMPVWVKYNYPGAPSNQAPFEVTIGQTTYQAQTYFKLTEPVAYGADIPEVTSEVKPALNGWYTLDTLPAIGTFQAIFTLPGTKSKYGDVVAASHFSITPQLMLVAYLVRVTTALPNALRGSPWSDNADNSILYYTPLVNAYAAATSDANPIQFTPNRACVSECRSHCGHPTIVAADVGEYILALVWCRGNGFSAGVINSYGALADTSFNLDSLRADSNGVMTLLNRAVPYSSLCALRMTRGVPPTSDDELVARILGQLQTRLKFAAGSGSSSEDDLSDDDDFECLRSTPLQQIYEGVRGLRGHAEAVAVVKSLQSRGHAE | Function: The capsid polyprotein VP90 self-assembles and undergoes a proteolytic cleavage by host caspases to yield the VP70 virions. This immature virion is composed of 180 VP70 subunits with 90 dimeric spikes and displays a T=3 icosahedral symmetry. The mature virion is obtained by further cleavages resulting in three structural proteins VP25, VP27 and VP34. This forms contains only 30 spikes located on the icosahedral 2-fold axes. Plays a role in the attachment to target host cell. This attachment induces virion internalization through clathrin-dependent endocytosis (By similarity).
PTM: Specific enzymatic cleavages in vivo yield mature protein(s). VP90 undergoes a cascade of proteolytic cleavages presumably mediated by host caspases and extracellular proteases (By similarity).
Sequence Mass (Da): 82366
Sequence Length: 762
Subcellular Location: Virion
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P19896 | MAKINELLRESTTTNSNSIGRPNLVALTRATTKLIYSDIVATQRTNQPVAAFYGIKYLNPDNEFTFKTGATYAGEAGYVDREQITELTEESKLTLNKGDLFKYNNIVYKVLEDTPFATIEESDLELALQIAIVLLKVRLFSDAASTSKFESSDSEIADARFQINKWQTAVKSRKLKTGITVELAQDLEANGFDAPNFLEDLLATEMADEINKDILQSLITVSKRYKVTGITDSGFIDLSYASAPEAGRSLYRMVCEMVSHIQKESTYTATFCVASARAAAILAASGWLKHKPEDDKYLSQNAYGFLANGLPLYCDTNSPLDYVIVGVVENIGEKEIVGSIFYAPYTEGLDLDDPEHVGAFKVVVDPESLQPSIGLLVRYALSANPYTVAKDEKEARIIDGGDMDKMAGRSDLSVLLGVKLPKIIIDE | Function: Capsid protein that self-associates to form pentons, building the capsid in association with hexamers of the major capsid protein and one dodecamer of the portal protein. The capsid vertex protein self-associates to form 11 pentons, building the T=13 laevo capsid in association with 160 hexamers of the major capsid protein.
PTM: A proteolytic cleavage gives rise to the mature capsid vertex protein.
Sequence Mass (Da): 46993
Sequence Length: 427
Subcellular Location: Virion
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P77885 | MKRYLVLEDGTIYPGTGFGATTATVGELVFNTGMSGYQESITDQSYNGEILMFTYPLIGNYGINRDDHESIKPTCKGVVVHEVARRASNWRNAQSLDDYLKQNAIPGIMDIDTRAVTKHIRTKGAMKATIVDNVLPDTVDRLKVTELNRAVVAQSSTNNAYPNPATGPNVVVVDFGLKHSILRELAKRQCNLTVLPYNTTASEIMALNPDGVMLTNGPGDPKDVPGALEMIREVEKHVPLFGICLGHQLFALANGADTFKMKFGHRGFNHPVREIATGRIDFTSQNHGYAVDRDSLAQTDLLITHEEINDGTVEGLRHRDYAAFSVQYHPDAAPGPHDADHIFDEFIDLMAANQATQKGSQFNA | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 39983
Sequence Length: 364
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
EC: 6.3.5.5
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Q1MPN3 | MKALLALEDGFILEGQSINGHCESSGEVIFNTGMTGYQEILTDPSYYGQMVCMTWPLIGNYGINKEDMESEKIHVSALIVKECCRNPSNWRSETSLPKFLQEYNIAGIEGIDTRALTRHIRINGAMRGIISTSITDPNDLILRVKKVPSMEGQNYVTKVAPNSPWVLYGQCVVPADIKEDGSFLWKQNKIPLIVYDYGIKWNIIRLLEGAGFDPLMVPPLFSLEQVKASGAKAIFLSNGPGDPGTLIDEIQIIRELMEYYPIAGICLGHQLLGHAVGGTTRKLTFGHHGSNHPIKNLATGHIEISSQNHGFCVNFESNNDIEVTHINLNDNTLEGFIHKTKPILAVQHHPEASPGPMDSQYFFTRFKEVVLLKLGC | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 41736
Sequence Length: 376
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
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Q8F6R2 | MKAFLVLDNGTIFEGESFGYETESVGEIVFNTSMAGYQEILTDPSYCNQIITLTYPMIGNYGIHPDNMESSKIQASGLIVKEYVDLPSNFKSEKTLSQFLKEYKIPAIQGIDTRKLTRFIRTNGSPNGGIFVASEYSPSFLEKVKSFPGIINADLAKVVTTSSKYIFGTHTGKKFKLAVYDYGVKTNILRLLDANGFAVTVYPAKTPSEEIMKEGTDAFFLSNGPGDPAPLDYAIASTQKIMEKRYPLFGICLGHQIIGLSLGKKTEKMKFGHRGGNQPVKNLETGQVEITSQNHGFAVIDDQKQDEPISFLNLNDHTVEGILKSGYPLLTVQYHPESAPGPNDSRYLFQKFYDLVEKTKKG | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 40130
Sequence Length: 362
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
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Q8Y664 | MTKRILMLEDGNYFIGDAIGSEKETIGEVVFNTGMTGYQETITDPSYYGQIITFTYPLVGNYGVNRDDFESINPAVKGVVVREAAEFASNWRNQITLNEFLKEKGIPGIAGIDTRKLTKLIRKEGTLKGILAAETADKEELLHHLRSVRLPVDQVHEVSSAKAFASPGDGKRVVLVDYGVKSSILRELNKRNCYVTVVPYNTSAEEILAMHPDGVMLSNGPGDPKDVPEALEMIRGIQGKLPLFGICLGHQLFALANGADTFKLKFGHRGANHPVKELATGRVDFTAQNHGYAVEKDSLIGTDLKVTHIELNDETVEGLAHKEYPAYTVQYHPEANPGPSDVNYLFDEFMEMMNGKEEGELHA | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 40055
Sequence Length: 363
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
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Q0AMR3 | MTSTPTPTPTGALALADGSVFLGHGTGATGIALGEVCFNTAMTGHQEILADPSYAGQVVCFTFPHVGNVGANGEDEEAASPQARKAAVGMIARAKITPPASWRADTTFEEWLCTRGIVALTGIDTRALTRKIREGGMQMCAIAHDAAGNIDIEALKAAAAGAPTMEGRELAADVARTEGGDWTEGNWTLGEGYAVGPEDGPRVVVLDYGVKANILRLLTGAGARVAVLPGKASIDDIKALNPDGVVVSNGPGDPAETGKYALPTIKAVLDANIPTLGICLGHQMLALAIGAKTAKMPQGHHGANHPVKNHETGQVEIVSMNHGFAVDGTTLPANAAETHVSLFDGSNSGFKLTDKPVWAVQHHPEASPGPQDSFGVFDRFVGELKGRVEA | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 40256
Sequence Length: 390
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
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C6C0A9 | MKAILALEDGTYFEGTSFTGPGESGGEAIFNTGMTGYQEVLTDPSYTGQMVCMTYPLIGNYGITKEDIESAKVHVAAFIVKECCKHPSNWRSVMSLPEYLKEAGVMGIEGIDTRALTRHLRINGAMRGIISTEELDPEKLVAKAKQLPTMEGQNLADTVTSETCYAWQDGKPVPVDVSSGYKWSDKGPRLVLVDYGVKWNILRLLDEQGFEVLSVPSHYSEEQVRALEPDAIFLSNGPGDPAVLDQAVKNAKSYCEDLPVAGICLGHQILGQALGGKAFKLKFGHHGCNHPVMDMESKKIEISSQNHGFCVDISDCSDLKITHKNLNDETLEGFAHKTKPIIAIQFHPEAAPGPHDSCYFFARFRNLVKDATGK | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 40988
Sequence Length: 374
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
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Q8TNY3 | MKAVLGLEDGTVIRGTGFGAEGTACGELVFTTQFTGYEEALTDPSYKGQILMFTYPLIGNYGVSGERFQSDNIHAEGLVVREACKKPYHYKSTRSIHQFLEDEGKPGIEGVDTRMLTIGARERGTMRAALITGSDDGEEAVKVARNFPQITDEELIARVTCKEPHFIPGAECAWKGSGKPKHAVVVDLGIKRNIINNLHKRGIDLTLVPATTKPKEIAGFEPDLLFISNGPGDPEKATDAINAVKAFAGTIPVAGICFGHQIISLAMGARTYKLKFGHRGGNQPVKDLIENKIFISSQNHGYAVDADSLEGTGLYVKYLNANDKTVEGVSHKDLDIFSVQFHPEAQAGPMDTEETFFGKVVKVLGGDL | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 39829
Sequence Length: 368
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
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Q58425 | MEAVLILEDGTILKGKGFGAEKEVFGELVFTTVMTGYVEVLTDPSYKGQIVMMTYPLEGNYGVKKDWFESDGIKAEGFVVREVTSKALDDFLKEYDIPGIQDIDTRFLTRKIRDKGVVKSCLKVAEEISDDEISELLERVKRYSDISDIDLVPLVSTKEPKIHKTANPKARCVLIDCGVKLNIIRSLVQRNCEVIQVPYNTKYDEILEYKPDFVLISNGPGDPARLKEVIKNIKNLIGVVPITGICLGNQLLSLAFGGETYKMKFGHRGGNQPVKDLKTQKVYITSQNHGFAVRKESLPDDVEVSFINLNDMTVEGIRHKDLPIFSVQFHPEARPGPHDTMFLFDEMIKLKDRK | Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Mass (Da): 39920
Sequence Length: 354
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
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Q9Y2G2 | MEKKECPEKSSSSEEELPRRDSGSSRNIDASKLIRLQGSRKLLVDNSIRELQYTKTGIFFQAEACVTNDTVYRELPCVSETLCDISHFFQEDDETEAEPLLFRAVPECQLSGGDIPSVSEEQESSEGQDSGDICSEENQIVSSYASKVCFEIEEDYKNRQFLGPEGNVDVELIDKSTNRYSVWFPTAGWYLWSATGLGFLVRDEVTVTIAFGSWSQHLALDLQHHEQWLVGGPLFDVTAEPEEAVAEIHLPHFISLQAGEVDVSWFLVAHFKNEGMVLEHPARVEPFYAVLESPSFSLMGILLRIASGTRLSIPITSNTLIYYHPHPEDIKFHLYLVPSDALLTKAIDDEEDRFHGVRLQTSPPMEPLNFGSSYIVSNSANLKVMPKELKLSYRSPGEIQHFSKFYAGQMKEPIQLEITEKRHGTLVWDTEVKPVDLQLVAASAPPPFSGAAFVKENHRQLQARMGDLKGVLDDLQDNEVLTENEKELVEQEKTRQSKNEALLSMVEKKGDLALDVLFRSISERDPYLVSYLRQQNL | Function: Inflammasome sensor, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis of CD4(+) T-cells and macrophages . Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation . Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as HIV-1 protease activity or Val-boroPro inhibitor, and mediates CARD8 inflammasome activation . In response to pathogen-associated signals, the N-terminal part of CARD8 is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (Caspase recruitment domain-containing protein 8, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the CARD8 inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis . Ability to sense HIV-1 protease activity leads to the clearance of latent HIV-1 in patient CD4(+) T-cells after viral reactivation; in contrast, HIV-1 can evade CARD8-sensing when its protease remains inactive in infected cells prior to viral budding . Also acts as a negative regulator of the NLRP3 inflammasome . May also act as an inhibitor of NF-kappa-B activation .
PTM: Undergoes autocatalytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals.
Sequence Mass (Da): 60652
Sequence Length: 537
Domain: The disordered region is required for activation of the CARD8 inflammasome.
Subcellular Location: Cytoplasm
EC: 3.4.-.-
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Q5RAV7 | MGIPTSSVSEEQESSEGQDSGDICSEENQIVSSYASKVCFEIEQDYKNRQFLGPEGNVDVELIDKSTNTYSVRFPTAGWYLWPATGLGFLVRDVVTLTIGFGSWNQHLALDLQHHEQWLVGGPLFDITAEPEEAVAEIHLPHFISLQAGEVDVSWFLIAHFKNEGMVLEHPARVEPFYAVLEKPSFSLMGILLRIASGTRLSIPITSNTLIYYHPHPEDIKFHLYLVPSDALLTKMIDDEEDRFCGVRLQTSPPVEPLNFGARYIVSNSAHLEIIPTELKLSYRSPGEIQHFSKFYAGQMKEPIQLEITEKRHETLVWKTVVKPVDIQLGAASAPPAFSGAAFVKENHRQLQARMGDLKGVLDDLQDNEVLTENEKELVEQAKTRQSKNDTLLTMVEKKGDRALELLFRSISERDPYLVSYLRQQSL | Function: Inflammasome sensor, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis of CD4(+) T-cells and macrophages. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation. Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as Val-boroPro inhibitor, and mediates CARD8 inflammasome activation. In response to pathogen-associated signals, the N-terminal part of CARD8 is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (Caspase recruitment domain-containing protein 8, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the CARD8 inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis. Also acts as a negative regulator of the NLRP3 inflammasome. May also act as an inhibitor of NF-kappa-B activation.
PTM: Undergoes autocatalytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals.
Sequence Mass (Da): 48186
Sequence Length: 427
Domain: The disordered region is required for activation of the CARD8 inflammasome.
Subcellular Location: Cytoplasm
EC: 3.4.-.-
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Q9H257 | MSDYENDDECWSVLEGFRVTLTSVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQLYKKVTGKEPARVFSMIIDASGESGLTQLLMTEVMKLQKKVQDLTALLSSKDDFIKELRVKDSLLRKHQERVQRLKEECEAGSRELKRCKEENYDLAMRLAHQSEEKGAALMRNRDLQLEIDQLKHSLMKAEDDCKVERKHTLKLRHAMEQRPSQELLWELQQEKALLQARVQELEASVQEGKLDRSSPYIQVLEEDWRQALRDHQEQANTIFSLRKDLRQGEARRLRCMEEKEMFELQCLALRKDSKMYKDRIEAILLQMEEVAIERDQAIATREELHAQHARGLQEKDALRKQVRELGEKADELQLQVFQCEAQLLAVEGRLRRQQLETLVLSSDLEDGSPRRSQELSLPQDLEDTQLSDKGCLAGGGSPKQPFAALHQEQVLRNPHDAGLSSGEPPEKERRRLKESFENYRRKRALRKMQKGWRQGEEDRENTTGSDNTDTEGS | Function: Adapter protein that plays a key role in innate immune response against fungi by forming signaling complexes downstream of C-type lectin receptors . CARD9-mediated signals are essential for antifungal immunity against a subset of fungi from the phylum Ascomycota . Transduces signals in myeloid cells downstream of C-type lectin receptors CLEC7A (dectin-1), CLEC6A (dectin-2) and CLEC4E (Mincle), which detect pathogen-associated molecular pattern metabolites (PAMPs), such as fungal carbohydrates, and trigger CARD9 activation (By similarity). Upon activation, CARD9 homooligomerizes to form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10 and subsequent recruitment of MALT1: this leads to activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines . CARD9 signaling in antigen-presenting cells links innate sensing of fungi to the activation of adaptive immunity and provides a cytokine milieu that induces the development and subsequent of interleukin 17-producing T helper (Th17) cells . Also involved in activation of myeloid cells via classical ITAM-associated receptors and TLR: required for TLR-mediated activation of MAPK, while it is not required for TLR-induced activation of NF-kappa-B (By similarity). CARD9 can also be engaged independently of BCL10: forms a complex with RASGRF1 downstream of C-type lectin receptors, which recruits and activates HRAS, leading to ERK activation and the production of cytokines (By similarity). Acts as an important regulator of the intestinal commensal fungi (mycobiota) component of the gut microbiota . Plays an essential role in antifungal immunity against dissemination of gut fungi: acts by promoting induction of antifungal IgG antibodies response in CX3CR1(+) macrophages to confer protection against disseminated C.albicans or C.auris infection . Also mediates immunity against other pathogens, such as certain bacteria, viruses and parasites; CARD9 signaling is however redundant with other innate immune responses (By similarity). In response to L.monocytogenes infection, required for the production of inflammatory cytokines activated by intracellular peptidoglycan: acts by connecting NOD2 recognition of peptidoglycan to downstream activation of MAP kinases (MAPK) without activating NF-kappa-B (By similarity).
PTM: Phosphorylated at Thr-231 by PRKCD downstream of C-type lectin receptors activation: phosphorylation promotes interaction with BCL10, followed by activation of NF-kappa-B and MAP kinase p38 pathways (By similarity). Phosphorylated at Thr-531 and Thr-533 by CK2 following interaction with VHL, leading to inhibit the ability to activate NF-kappa-B (By similarity).
Sequence Mass (Da): 62241
Sequence Length: 536
Domain: The linker region, also named autoinhibitory interface, is required to prevent constitutive activation and maintain CARD9 in an autoinhibitory state . Disruption of this region triggers polymerization and activation, leading to formation of BCL10-nucleating filaments .
Subcellular Location: Cytoplasm
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A2AIV8 | MSDYENDDECWSTLESFRVKLISVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQLYRKVTGKEPARVFSMIIDASGESGLTQLLMTEVMKLQKKVQDLTALLSSKDDFIKELRVKDSLLRKHQERVQRLKEECELSSAELKRCKDENYELAMCLAHLSEEKGAALMRNRDLQLEVDRLRHSLMKAEDDCKVERKHTLKLRHAMEQRPSQELLWELQQEKDLLQARVQELQVSVQEGKLDRNSPYIQVLEEDWRQALQEHQKQVSTIFSLRKDLRQAETLRARCTEEKEMFELQCLALRKDAKMYKDRIEAILLQMEEVSIERDQAMASREELHAQCTQSFQDKDKLRKLVRELGEKADELQLQLFQTESRLLAAEGRLKQQQLDMLILSSDLEDSSPRNSQELSLPQDLEEDAQLSDKGVLADRESPEQPFMALNKEHLSLTHGMGPSSSEPPEKERRRLKESFENYRRKRALRKMQNSWRQGEGDRGNTTGSDNTDTEGS | Function: Adapter protein that plays a key role in innate immune response against fungi by forming signaling complexes downstream of C-type lectin receptors . CARD9-mediated signals are essential for antifungal immunity against a subset of fungi from the phylum Ascomycota . Transduces signals in myeloid cells downstream of C-type lectin receptors CLEC7A (dectin-1), CLEC6A (dectin-2) and CLEC4E (Mincle), which detect pathogen-associated molecular pattern metabolites (PAMPs), such as fungal carbohydrates, and trigger CARD9 activation . Upon activation, CARD9 homooligomerizes to form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10 and subsequent recruitment of MALT1: this leads to activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines . CARD9 signaling in antigen-presenting cells links innate sensing of fungi to the activation of adaptive immunity and provides a cytokine milieu that induces the development and subsequent of interleukin 17-producing T helper (Th17) cells . Also involved in activation of myeloid cells via classical ITAM-associated receptors and TLR: required for TLR-mediated activation of MAPK, while it is not required for TLR-induced activation of NF-kappa-B . CARD9 can also be engaged independently of BCL10: forms a complex with RASGRF1 downstream of C-type lectin receptors, which recruits and activates HRAS, leading to ERK activation and the production of cytokines . Acts as an important regulator of the intestinal commensal fungi (mycobiota) component of the gut microbiota . Plays an essential role in antifungal immunity against dissemination of gut fungi: acts by promoting induction of antifungal IgG antibodies response in CX3CR1(+) macrophages to confer protection against disseminated C.albicans or C.auris infection . Also mediates immunity against other pathogens, such as certain bacteria, viruses and parasites; CARD9 signaling is however redundant with other innate immune responses . In response to L.monocytogenes infection, required for the production of inflammatory cytokines activated by intracellular peptidoglycan: acts by connecting NOD2 recognition of peptidoglycan to downstream activation of MAP kinases (MAPK) without activating NF-kappa-B .
PTM: Phosphorylated at Thr-231 by PRKCD downstream of C-type lectin receptors activation: phosphorylation promotes interaction with BCL10, followed by activation of NF-kappa-B and MAP kinase p38 pathways . Phosphorylated at Thr-531 and Thr-531 by CK2 following interaction with VHL, leading to inhibit the ability to activate NF-kappa-B (By similarity).
Sequence Mass (Da): 62462
Sequence Length: 536
Domain: The linker region, also named autoinhibitory interface, is required to prevent constitutive activation and maintain CARD9 in an autoinhibitory state. Disruption of this region triggers polymerization and activation, leading to formation of BCL10-nucleating filaments.
Subcellular Location: Cytoplasm
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Q9EPY0 | MSDYENDDECWSALESFRVKLISVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQLYRKVTGKEPARVFSMIIDASGESGLTQLLMTEVMKLQKKVQDLTALLSSKDDFIKELRVKDSLLRKHQERVQRLKEECELSSAELKRCKDENYDLAMRLAHLSEEKGAALMRNRDLQLEVDQLRHSLMKAEDDCKVERKHTLKLRHAMEQRPSQELLWDLQQERDLLQARVQELEVSVQEGKLHRNSPYIQVLEEDWRQALQEHQEQASTIFSLRKDLRQAEALRTRCMEEKEMFELQCLALRKDAKMYKDRIEAILQQMEEVSIERDQAMTSREELHAQCAQSFQDKDKLRKQVRELDEKADELQLQLFQTESRLLAAEGRLKQQQLDMLILSSDLEDSSPRNSQELSLPQDLEEDAQLSDKGVLADRESPEQPFVVLNKKHLSQTHDTVPSSSEPPEKERRRLKESFENYRRKRALRKMQNSWRQGEGDHGNTTGSDNTDTEGS | Function: Adapter protein that plays a key role in innate immune response against fungi by forming signaling complexes downstream of C-type lectin receptors (By similarity). CARD9-mediated signals are essential for antifungal immunity against a subset of fungi from the phylum Ascomycota (By similarity). Transduces signals in myeloid cells downstream of C-type lectin receptors CLEC7A (dectin-1), CLEC6A (dectin-2) and CLEC4E (Mincle), which detect pathogen-associated molecular pattern metabolites (PAMPs), such as fungal carbohydrates, and trigger CARD9 activation . Upon activation, CARD9 homooligomerizes to form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10 and subsequent recruitment of MALT1: this leads to activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines . CARD9 signaling in antigen-presenting cells links innate sensing of fungi to the activation of adaptive immunity and provides a cytokine milieu that induces the development and subsequent of interleukin 17-producing T helper (Th17) cells (By similarity). Also involved in activation of myeloid cells via classical ITAM-associated receptors and TLR: required for TLR-mediated activation of MAPK, while it is not required for TLR-induced activation of NF-kappa-B (By similarity). CARD9 can also be engaged independently of BCL10: forms a complex with RASGRF1 downstream of C-type lectin receptors, which recruits and activates HRAS, leading to ERK activation and the production of cytokines (By similarity). Acts as an important regulator of the intestinal commensal fungi (mycobiota) component of the gut microbiota (By similarity). Plays an essential role in antifungal immunity against dissemination of gut fungi: acts by promoting induction of antifungal IgG antibodies response in CX3CR1(+) macrophages to confer protection against disseminated C.albicans or C.auris infection (By similarity). Also mediates immunity against other pathogens, such as certain bacteria, viruses and parasites; CARD9 signaling is however redundant with other innate immune responses (By similarity). In response to L.monocytogenes infection, required for the production of inflammatory cytokines activated by intracellular peptidoglycan: acts by connecting NOD2 recognition of peptidoglycan to downstream activation of MAP kinases (MAPK) without activating NF-kappa-B (By similarity).
PTM: Phosphorylated at Thr-231 by PRKCD downstream of C-type lectin receptors activation: phosphorylation promotes interaction with BCL10, followed by activation of NF-kappa-B and MAP kinase p38 pathways (By similarity). Phosphorylated at Thr-531 and Thr-533 by CK2 following interaction with VHL, leading to inhibit the ability to activate NF-kappa-B .
Sequence Mass (Da): 62632
Sequence Length: 536
Domain: The linker region, also named autoinhibitory interface, is required to prevent constitutive activation and maintain CARD9 in an autoinhibitory state. Disruption of this region triggers polymerization and activation, leading to formation of BCL10-nucleating filaments.
Subcellular Location: Cytoplasm
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Q9XFX3 | MGTSIKANVLALFLFYLLSPTVFSVSDDGLIRIGLKKRKVDRIDQLRGRRALMEGNARKDFGFRGTVRDSGSAVVALTNDRDTSYFGEIGIGTPPQKFTVIFDTGSSVLWVPSSKCINSKACRAHSMYESSDSSTYKENGTFGAIIYGTGSITGFFSQDSVTIGDLVVKEQDFIEATDEADNVFLHRLFDGILGLSFQTISVPVWYNMLNQGLVKERRFSFWLNRNVDEEEGGELVFGGLDPNHFRGDHTYVPVTYQYYWQFGIGDVLIGDKSTGFCAPGCQAFADSGTSLLSGPTAIVTQINHAIGANGVMNQQCKTVVSRYGRDIIEMLRSKIQPDKICSHMKLCTFDGARDVSSIIESVVDKNNDKSSGGIHDEMCTFCEMAVVWMQNEIKQSETEDNIINYANELCEHLSTSSEELQVDCNTLSSMPNVSFTIGGKKFGLTPEQYILKVGKGEATQCISGFTAMDATLLGPLWILGDVFMRPYHTVFDYGNLLVGFAEAA | Function: Aspartic proteinase with a high preference for bonds between hydrophobic residues. Cleaves alpha-lactalbumin but not beta-lactoglobulin.
PTM: N-glycosylated. Glycans found at Asn-139 include approximately 6% oligomannose, 82% oligosaccharides of the plant modified type with proximal fucose but without xylose and 6% oligosaccharides of the plant modified type with proximal fucose and xylose. Glycans found at Asn-432 include 14% oligosaccharides of the plant modified type with proximal fucose but without xylose and 86% oligosaccharides of the plant modified type with proximal fucose and xylose.
Sequence Mass (Da): 55504
Sequence Length: 504
Subcellular Location: Microsome membrane
EC: 3.4.23.-
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Q9XFX4 | MGTPIKASLLALFLFFLLSPTAFSVSNGGLLRVGLKKRKVDRLDQLRAHGVHMLGNARKDFGFRRTLSDSGSGIVALTNDRDTAYYGEIGIGTPPQNFAVIFDTGSSDLWVPSTKCDTSLACVIHPRYDSGDSSTYKGNGTTASIQYGTGAIVGFYSQDSVEVGDLVVEHQDFIETTEEDDTVFLKSEFDGILGLGFQEISAGKAVPVWYNMVNQGLVEEAVFSFWLNRNVDEEEGGELVFGGVDPNHFRGNHTYVPVTRKGYWQFEMGDVLIGDKSSGFCAGGCAAIADSGTSFFAGPTAIITQINQAIGAKGVLNQQCKTLVGQYGKNMIQMLTSEVQPDKICSHMKLCTFDGAHDVRSMIESVVDKNNDKSSGGEICTFCEMALVRMQNEIKRNETEDNIINHVNEVCDQLPTSSAESIVDCNGISSMPNIAFTIGSKLFEVTPEQYIYKVGEGEAATCISGFTALDIMSPQGPIWILGDMFMGPYHTVFDYGKLRVGFAEAV | Function: Aspartic protease. Cleaves alpha-lactalbumin but not beta-lactoglobulin.
Sequence Mass (Da): 54951
Sequence Length: 506
Subcellular Location: Microsome membrane
EC: 3.4.23.-
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P85136 | DSGSAIVALTNDRDTSYFGEIGIGTPPQKYTVIYDTGSSVLWVPSSKEQDFIEATDETDNVFLHRRFSFWLNRNVDEEEGGELVFGGLDPNHFRGDHTYVPVTYQYYWQFGIGDVLIGDKSTGFCAPGCQAFADSGTSLLSGPTAIVTQINHAIGANSEELNVKFGLTPEQYILKGEATQCISGFTAMDATLLGPLWILGDVFMRPYHTVFDYGNLLVGFAEAA | Function: Aspartic protease with a high preference for bonds between hydrophobic residues.
PTM: N-glycosylated.
Sequence Mass (Da): 24507
Sequence Length: 224
Subcellular Location: Microsome membrane
EC: 3.4.23.-
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P85137 | ADSGSAVVALTNDRDTSYYGEIGIGTPPQKFTVIFDTGSSVLWVPSSKAHSMYESSGSSTYKSQDSVTIGDLVVKEQDFIEATEEADNVFLNRLFDGILGLSFQTISVPVWYNMLNQGLVKRFSFWLNRNVDEEEGGELVFGGLDPNHFRGDHTYVPVTYQYYWQFGIGDVLIGDKSTGFCAPGCQAFADSGTSLLSGPTAIVTQINHAIGANGSEELNVKFGLTPEQYILKGEATQCISGFTAMDATLLGPLWILGDVFMRPYHTVFDYGNLLVGFAEAA | Function: Aspartic protease with a high preference for bonds between hydrophobic residues.
PTM: N-glycosylated.
Sequence Mass (Da): 30561
Sequence Length: 281
Subcellular Location: Microsome membrane
EC: 3.4.23.-
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A4XES9 | MVTKGVVVVSSFRRSRQDANRPHAFLTGIHAPVKEERTIEDLAVTGTIPAELSGRYVRIGPNPFRADPRGHHWFVGDGMVHGVCMKGGKALWYRNRYVRSRNLQDAGGPAAAPGPRRSTFDTVNTNVIQHAGRTFALVEAGSFPVELTHDLESFAYSDLGGTLKGPFSAHPHLDPLTGELHAVTYDGQTLDTVWHVVVDREGRVRREEPVPVAHGPSIHDCAITAKYVLILDLPVTFSMAALVGGARFPYRWNPAHRARVGLLPREGTAADVIWCDVDAAYVFHVANAFDNPDGTVTVDLAAYETMFAHGPDGPNGKSLGMERWTVDPAARKVARKTLDAAPQEFHRPDERFFGQPYRFAWSMGLPAENAEDFLGHAPIYGYDLATGQRSAHDFGPGKIPGEFVFIPRRADAEEGDGWLMGYVIDLASETTDLAILDARNLAAPPLALIHIPCRIPPGFHGNWLPDAAD | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the conversion of 8'-apo-beta-carotenal to 13-apo-beta-carotenone and C12-dialdehyde. Has also weak activity with 4'-apo-beta-carotenal and gamma-carotene.
Catalytic Activity: all-trans-8'-apo-beta-carotenal + O2 = 13-apo-beta-carotenone + 2,6-dimethyldeca-2,4,6,8-tetraenedial
Sequence Mass (Da): 51308
Sequence Length: 469
EC: 1.13.11.82
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P75409 | MPNPVRFVYRVDLRSPEEIFEHGFSTLGDVRNFFEHILSTNFGRSYFISTSETPTAAIRFFGSWLREYVPEHPRRAYLYEIRADQHFYNARATGENLLDLMRQRQVVFDSGDREMAQMGIRALRTSFAYQREWFTDGPIAAANVRSAWLVDAVPVEPGHAHHPAGRVVETTRINEPEMHNPHYQELQTQANDQPWLPTPGIATPVHLSIPQAASVADVSEGTSASLSFACPDWSPPSSNGENPLDKCIAEKIDNYNLQSLPQYASSVKELEDTPVYLRGIKTQKTFMLQADPQNNNVFLVEVNPKQKSSFPQTIFFWDVYQRICLKDLTGAQISLSLTAFTTQYAGQLKVHLSVSAVNAVNQKWKMTPQDIAITQFRVSSELLGQTENGLFWNTKSGGSQHDLYVCPLKNPPSDLEELQIIVDECTTHAQFVTMRAASTFFVDVQLGWYWRGYYYTPQLSGWSYQMKTPDGQIFYDLKTSKIFFVQDNQNVFFLHNKLNKQTGYSWDWVEWLKHDMNEDKDENFKWYFSRDDLTIPSVEGLNFRHIRCYADNQQLKVIISGSRWGGWYSTYDKVESNVEDKILVKDGFDRF | Function: The main virulence factor for this bacteria, a mono-ADP-ribosylating toxin (mART), that transfers the ADP-ribosyl group from NAD(+) to multiple target proteins in vitro . Also elicits cytopathic effects in mammalian cells, such as disorganization and disruption of respiratory epithelial integrity in tracheal epithelium and vacuolization in the cytoplasm of CHO and HeLa cells as well as in mice and baboons . Treatment of mice or baboons with CARDS elicits a response that is consistent with human M.pneumoniae infections and mouse models of both infection and intoxication, suggesting that CARDS toxin is sufficient to cause prolonged inflammatory responses and airway dysfunction. Treatment of baboons with CARDS induces a number of cytokines; G-CSF (40 fold), IL-1Ra (10 fold), IL-6 and IL-8 (333 and 100 fold, respectively), MIP-1a (5 fold), and RANTES (9 fold). Treatment of mice gives a similar response . Binds phosphatidyl choline, dipalmitoylphosphatidylcholine (DPPC) and sphingomyelin via domains D2 plus D3 .
PTM: 8 hours after treatment of HeLa cells with purified protein, a substantial amount is processed to 2 nearly equal-sized fragments . The disulfide bond between Cys-230 and Cys-247 is required to for the toxin to exert its mART and vacuolating activities within target cells, and for protein processing . Acidic pH in the endosome and retrograde transport are required for toxin cleavage, which is required for both toxin activities . Trypsin treatment under mild conditions leads to cleavage at Lys-305 and Lys-307; the 2 proteins fragments remain associated and can be internalized and vacuolate HeLa cells .
Sequence Mass (Da): 68057
Sequence Length: 591
Domain: The N-terminus (up to about residue 249) has mART activity, as well as NADase activity. The C-terminal 41 residues are required for internalization by HeLa cells and for vacuolization . The C-terminus (residues 266-591) is required for interaction with annexin A2 . Has 3 structural domains, the N-terminal mART domain (mono-ADP ribosyltransferase, residues 1-205), D2 (residues 273-439) and D3 (residues 440-591). mART is joined to D2 by a linker (residues 257-272) which has a disulfide bond. The 3 domains assemble into an isosceles triangle, where the probable active site and NAD(+)-binding site are occulded. Enzyme activity will require either a conformation change or proteolytic processing. Domain D2 and D3 together bind lipids, domain D3 is at least partially responsible for binding to and internalization by host cells . A C-terminal fragment (residues 273-591) is capable of inducing vacuolization upon incubation with HeLa cells .
Subcellular Location: Cell membrane
EC: 2.4.2.-
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H6LGM7 | MRILVCAKQVPDTNEVKIDPKTGTMIREGVPSILNPDDANALEAALVIKDENPGTEVIVMTMGPPQASEMLRECLAMGADEAYLLSDRAFGGADTWATSATLAAGIKKVKKVDLVLAGRQAIDGDTAQVGSQIAQRLKMPVVTYVEDIKIEDKKAIVHRQMEDGYEVIEVQLPCLLTCVKELNDPRYMSVGGIMDAYEQPITIWNHEDIGLSPEACGLNASPTQVFRSFSPPAKGGGEMITGTTVNEVAGSLVSKLKEKHII | Cofactor: Binds 1 FAD per subunit.
Function: Caffeyl-CoA reductase-Etf complex catalyzes the reduction of caffeyl-CoA to yield hydrocaffeyl-CoA. It couples the endergonic ferredoxin reduction with NADH as reductant to the exergonic reduction of caffeoyl-CoA with the same reductant. It uses the mechanism of electron bifurcation to overcome the steep energy barrier in ferredoxin reduction. The electron transfer flavoprotein (Etf) mediates the electron transfer between the different donors and acceptors. The complex can also reduce 4-coumaroyl-CoA and feruloyl-CoA.
Catalytic Activity: hydrocaffeoyl-CoA + 2 NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = (E)-caffeoyl-CoA + 2 NADH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 28237
Sequence Length: 262
Subcellular Location: Cytoplasm
EC: 1.3.1.108
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F6IBC7 | MAANNLSYTIAPLEHTPLDEIAAKVDLVRKTFRSGRTKDMEFRMKQIRKLYWAIVDNTELMQDALIKDLRKCKYEAVLAEIDWCKQECIDMVNNMEKWLRDEPVPNVPLQFRAMKHRTRFEPLGVVLNIGSFNFPFQLNLPVVIGAIACGNCVVLKASESSPNCAMVLKKIFDESLDPECFTYVNGALPETQLLLEQKFDKICFTGGKAVGKIIAQKAAETLTPVLLELGGLNPAFVTKHANLKLAARRLLWQKSLNAGQVCMSHNYILVERSVLSQFLGELNNQMRTFFPQGAKNSPDLCRIVNAGHFNRLKKMLDGTNGKIVLGGSMDESTLFMEPTAVLVDDINDSMMTQEAFGPIFAMMAVDSLDQAIDIANTVDPTPLSLSAFGSKAENNKILDNVTSGGATCNDAFFHSQIPQSPLGGVGQSGMGNYHGIYSIRTFSHQRTIAEVPYWADFLFRVRYMPYQWPVMNRMKAVADSKPNFDRNGNKTKGITYFLALVLGLGSKKSKGALLRWAVLVVAAAILEAKKGVLSQLLTR | Function: Beta-apo-4'-carotenal oxygenase involved in the last step of synthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigments and leading to orange pigmentation . Converts the aldehyde beta-apo-4'-carotenal into neurosporaxanthin . Is also able to use shorter apocarotenals as substrates (such as beta-apo-8'-carotenal (C30), beta-apo-10'-carotenal (C27), or the acyclic apocarotenal apo-8'-lycopenal (C30)), indicating wide substrate specificity . Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme carAR first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase carB then introduces 4 desaturations to lead to lycopene which is substrate of the carotene cyclase activity of carAR that leads to the production of gamma-carotene. CarB then performs a 5th desaturation reaction to yield torulene. Torulene is the substrate of the dioxidase carT that breaks the molecule, removing five carbon atoms to yield beta-apo-4'-carotenal, whereas the aldehyde dehydrogenase carD mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable).
Catalytic Activity: 4'-apo-beta-carotenal + H2O + NAD(+) = 2 H(+) + NADH + neurosporaxanthin
Sequence Mass (Da): 59891
Sequence Length: 539
EC: 1.2.1.82
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Q1K615 | MAASKVEIAPFEVTPLDAIPAVCSTARATFASHKTKNLQWRLVQLRKLYWALDDFKASLMAALQQDLRKGGYESDFTEVDWVKNDCLHMINNLETFAKTEKLKDLPVTYSMMNFRVKKEPLGTVLIIGPYNFPIQLVLAPLVGAIGAGCTAVIKPSELTPACAMAMKEMIESRLDRDAFAVVNGGVPETNALMEEKWDKIMFTGSAQVGSIIARKAAETLTPVCLELGGRNPAFVTKKANLALAARRLMWGKVLNAGQVCMSHNYVLVDKDVADTFIEFLKIAYKDMFPNGAKASPDLSRIVNARHFNRIKKMLDETKGKIVMGGEMDESELYIEPTAVLVDSLDDPMMQEESFGPIFSIYPVDTLDQALSIANNVHRTPLALMAFGDKSETNRILDEMTSGGACINDSYFHGAVHTVPFGGVGDSGWGAYRGKASFDNFTHFRTVSETPTWMDRFLRVRYMPYDWSELRLLQRWTNKKPNFDRQGTVAKGSEYWMWYFLGLGTKGGVKGALMRWLVVVAGYYLSAYMKARRA | Function: Beta-apo-4'-carotenal oxygenase involved in the last step of synthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigment and leading to orange pigmentation . Converts the aldehyde beta-apo-4'-carotenal into neurosporaxanthin . Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme al-2 first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase al-1 then introduces 5 desaturations to lead to 3,4-didehydrolycopene via the intermediates phytofluene, zeta-carotene, neurosporene and lycopene. Al-2 cyclase activity then converts 3,4-didehydrolycopene into torulene. Al-2 can also convet lycopene into gamma-carotene which in turn is converted to beta-carotene by an additional al-2 cyclization reaction. Torulene is the substrate of the dioxidase cao-2 that breaks the molecule, removing five carbon atoms to yield beta-apo-4'-carotenal, whereas the aldehyde dehydrogenase ylo-1 mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable).
Catalytic Activity: 4'-apo-beta-carotenal + H2O + NAD(+) = 2 H(+) + NADH + neurosporaxanthin
Sequence Mass (Da): 59504
Sequence Length: 533
EC: 1.2.1.82
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O15234 | MADRRRQRASQDTEDEESGASGSDSGGSPLRGGGSCSGSAGGGGSGSLPSQRGGRTGALHLRRVESGGAKSAEESECESEDGIEGDAVLSDYESAEDSEGEEGEYSEEENSKVELKSEANDAVNSSTKEEKGEEKPDTKSTVTGERQSGDGQESTEPVENKVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYDIRSAHNPDDIKPRRIRKPRYGSPPQRDPNWNGERLNKSHRHQGLGGTLPPRTFINRNAAGTGRMSAPRNYSRSGGFKEGRAGFRPVEAGGQHGGRSGETVKHEISYRSRRLEQTSVRDPSPEADAPVLGSPEKEEAASEPPAAAPDAAPPPPDRPIEKKSYSRARRTRTKVGDAVKLAEEVPPPPEGLIPAPPVPETTPTPPTKTGTWEAPVDSSTSGLEQDVAQLNIAEQNWSPGQPSFLQPRELRGMPNHIHMGAGPPPQFNRMEEMGVQGGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTHGDSPAPLPPQGMLVQPGMNLPHPGLHPHQTPAPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPSYPYAPGALPPPPPPHLYPNTQAPSQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVTIKPPPPEVVSRGSS | Function: Required for pre-mRNA splicing as component of the spliceosome . Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Binds poly(G) and poly(U) RNA homomer.
PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination.
Sequence Mass (Da): 76278
Sequence Length: 703
Domain: The coiled coil domain may be involved in oligomerization.
Subcellular Location: Cytoplasm
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Q96PB1 | MAALAYNLGKREINHYFSVRSAKVLALVAVLLLAACHLASRRYRGNDSCEYLLSSGRFLGEKVWQPHSCMMHKYKISEAKNCLVDKHIAFIGDSRIRQLFYSFVKIINPQFKEEGNKHENIPFEDKTASVKVDFLWHPEVNGSMKQCIKVWTEDSIAKPHVIVAGAATWSIKIHNGSSEALSQYKMNITSIAPLLEKLAKTSDVYWVLQDPVYEDLLSENRKMITNEKIDAYNEAAVSILNSSTRNSKSNVKMFSVSKLIAQETIMESLDGLHLPESSRETTAMILMNVYCNKILKPVDGSCCQPRPPVTLIQKLAACFFTLSIIGYLIFYIIHRNAHRKNKPCTDLESGEEKKNIINTPVSSLEILLQSFCKLGLIMAYFYMCDRANLFMKENKFYTHSSFFIPIIYILVLGVFYNENTKETKVLNREQTDEWKGWMQLVILIYHISGASTFLPVYMHIRVLVAAYLFQTGYGHFSYFWIKGDFGIYRVCQVLFRLNFLVVVLCIVMDRPYQFYYFVPLVTVWFMVIYVTLALWPQIIQKKANGNCFWHFGLLLKLGFLLLFICFLAYSQGAFEKIFSLWPLSKCFELKGNVYEWWFRWRLDRYVVFHGMLFAFIYLALQKRQILSEGKGEPLFSNKISNFLLFISVVSFLTYSIWASSCKNKAECNELHPSVSVVQILAFILIRNIPGYARSVYSSFFAWFGKISLELFICQYHIWLAADTRGILVLIPGNPMLNIIVSTFIFVCVAHEISQITNDLAQIIIPKDNSSLLKRLACIAAFFCGLLILSSIQDKSKH | Function: O-acetyltransferase that catalyzes 9-O-acetylation of sialic acids . Sialic acids are sugars at the reducing end of glycoproteins and glycolipids, and are involved in various processes such as cell-cell interactions, host-pathogen recognition .
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-9-O-acetylneuraminate
Sequence Mass (Da): 91680
Sequence Length: 797
Subcellular Location: Golgi apparatus membrane
EC: 2.3.1.45
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Q0S4D9 | MTAPTDPQLHLDQVMSRLTGPGGRFELVEEPVLGTRMPVMKNRGRSVGELLTTSLRWGDRDYLVTADRRMSYTEHAAAVAALATALREDYGVRKGDRVAILAANTPEWVVAFWATQVLGAISVGLNGWWVPREVEYGLTHSRPTVVVADAKRAETLAAVGTDLPVLTMEEDLPALFARYAGSPMPHTDVDEDDPAAILYTSGTSGRPKGALHSQRNILAVVDYHRFSDAVVGEFSGRPVDPAVPSPLRYLLTSPLFHIASLHNLVIPRLATGGAVVMHQGGFDVDAVLRLVERERVTNWGAVPTMASRLVEHDDLDKYDLSSLTSFSLASAPSSVAFKERLREKVPFARNALVDSYGLTECSTAIAVATAPELEQFPGTLGRPIITVSMEIRDPYGEWLPDGVEGEVCVRSPFVMLGYWEDEAATAAAIAPGRWLRTGDYGLVENGRLRLTGRRSDLILRGGENVYPTEIEQCLDEHPEVLECAVIGTPHEDLGQEVAAVVVLRPGAAATEAELREYAADRLSYFKVPTRWRITTDLLPRNATGKMVRRDITV | Function: Involved in cholate catabolism . Catalyzes the transformation of cholate to cholyl-CoA, thus initiating degradation of the C5 cholate side chain . Can also catalyze the ATP-dependent formation of CoA thioesters of deoxycholate and chenodeoxycholate .
Catalytic Activity: ATP + cholate + CoA = AMP + choloyl-CoA + diphosphate
Sequence Mass (Da): 60484
Sequence Length: 553
Pathway: Steroid metabolism.
EC: 6.2.1.-
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Q0S4D7 | MELERTTIARMLFDRLGDDRLGVRTREQDWTWDEVVRESAARGAVASSLRRDGPFHVGVLLENTPEFLFWLGGAALAGAAVVGVNPTRRGAELEAEIRYVDCQLIVTDTAGKAQLAGLDLGLSEDRFLLVDDPAYTELVAAHAVESPAEDPGIDASTLFLLLFTSGTTGTSKAVRCSQGRLARLAYANTAKYGHVREDVDYCCMPLFHGNALMALWAPALANGATVCLPRKFSASGFLPDVRFFGATFFTYVGKALAYLMATPEQPDDRDNTLVRGFGTEASPEDKTEFVRRFGAELYEGYGSSEGAGSVTLDPDAPEGALGRPANENIVIVDPDTRVEKARARLDEHGRVLNPDEAIGEMVDKAGASRFEGYYKNEDAIADRIRHGWYWTGDLGYVDEAGFIYFAGRKGDWIRVDGENTSALMVERILRRHPKVVATGVFAVPDPRSGDQVMAAVEVADPTDFDPAEFAAFLGNQDDLGTKAAPRFVRVSRDLPVTGSNKVLKRTLQEQRWRCDDPVFRWVGRGVPEYHEMTDSEKAVLEQEFHTHGRQRFLHV | Function: Involved in cholate catabolism . Catalyzes the ATP-dependent formation of CoA thioesters of steroids with isopropanoyl side chains, likely occurring as degradation intermediates . Can use 4-BNC, HSBNC and HIDP as substrate .
Catalytic Activity: 3-oxochol-4-en-22-oate + ATP + CoA = 3-oxochol-4-en-22-oyl-CoA + AMP + diphosphate
Sequence Mass (Da): 61164
Sequence Length: 555
Pathway: Steroid metabolism.
EC: 6.2.1.-
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O33950 | MNKQAIDALLQKINDSAINEGNPRTKQIVNRIVRDLFYTIEDLDVQPDEFWTALNYLGDAGRSGELGLLAAGLGFEHFLDLRMDEAEAKAGVEGGTPRTIEGPLYVAGAPVSDGHARLDDGTDPGQTLVMRGRVFGEDGKPLANALVEVWHANHLGNYSYFDKSQPAFNLRRSIRTDAEGKYSFRSVVPVGYSVPPQGQTQLLLDQLGRHGHRPAHIHFFVSAPGFRKLTTQINIDGDPYLWDDFAFATRDGLVPAVRQAEVRKANRTAWTVSSR | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Can cleave 4-methyl-, 4-chloro-, and 3-methoxycatechol at lower rates than catechol, but has no activity with 4-nitrocatechol or protocatechuic acid.
Catalytic Activity: catechol + O2 = cis,cis-muconate + 2 H(+)
Sequence Mass (Da): 30399
Sequence Length: 275
Pathway: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydro-2-furylacetate from catechol: step 1/3.
EC: 1.13.11.1
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P25819 | MDPYKYRPASSYNSPFFTTNSGAPVWNNNSSMTVGPRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDLVGNNFPVFFIRDGMKFPDMVHALKPNPKSHIQENWRILDFFSHHPESLNMFTFLFDDIGIPQDYRHMDGSGVNTYMLINKAGKAHYVKFHWKPTCGVKSLLEEDAIRVGGTNHSHATQDLYDSIAAGNYPEWKLFIQIIDPADEDKFDFDPLDVTKTWPEDILPLQPVGRMVLNKNIDNFFAENEQLAFCPAIIVPGIHYSDDKLLQTRVFSYADTQRHRLGPNYLQLPVNAPKCAHHNNHHEGFMNFMHRDEEVNYFPSRYDQVRHAEKYPTPPAVCSGKRERCIIEKENNFKEPGERYRTFTPERQERFIQRWIDALSDPRITHEIRSIWISYWSQADKSLGQKLASRLNVRPSI | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 56931
Sequence Length: 492
Subcellular Location: Cytoplasm
EC: 1.11.1.6
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P30567 | MDPYKFRPSSSFDSPFWTTNSGAPVWNNNSSLTVGARGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISQLTCADFLRAPGVQTPLIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDLVGNNFPVFFIRDGMKFPDMVHALKPNPKSHIQENWRILDFFSHHPESLHMFTFLFDDIGVPQDYRHMDGSGVHTYTLINKAGKSHYVKFHWKPTCGVKSLLEDEAIRVGGANHSHATQDLYDSIAAGNYPEWKLFIQIMDPLHEDRFDFDPLDVTKTWPEDIFPLQPMGRMVLNKNIDNFFAENEQLAFCPSLIVPGIYYSDDKLLQTRIFSYSDTQRHRLGPNYLQLPANAPKCAHHNNHHEGFMNFMHRDEEVNYFPSRYDPVRHAEKHPIPSTVLSGKREKCIIGKENNFKQPGERYRSFSADRQERFINRWIDALSDPRVTHEIRSIWISYWSQADKSLGQKIASRLNVRPSI | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 56935
Sequence Length: 492
Subcellular Location: Peroxisome
EC: 1.11.1.6
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Q0D9C4 | MDPYKHRPSSGSNSTFWTTNSGAPVWNNNSALTVGERGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPVIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPSPKTNMQENWRIVDFFSHHPESLHMFSFLFDDVGIPLNYRHMEGFGVNTYTLINKDGKPHLVKFHWKPTCGVKCLLDDEAVTVGGTCHSHATKDLTDSIAAGNYPEWKLYIQTIDPDHEDRFDFDPLDVTKTWPEDIIPLQPVGRMVLNKNIDNFFAENEQLAFCPAIIVPGIHYSDDKLLQTRIFSYADTQRHRLGPNYLMLPVNAPKCAYHNNHHDGSMNFMHRDEEVNYFPSRFDAARHAEKVPIPPRVLTGCREKCVIDKENNFQQAGERYRSFDPARQDRFLQRWVDALSDPRITHELRGIWISYWSQCDASLGQKLASRLNLKPNM | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide (By similarity). May prevent the excessive accumulation of H(2)O(2) during water stress in response to the accumulation of abscisic acid (ABA) . Involved in the modulation of ROS levels related to root growth regulation (Ref.11). Required for pollen viability and floret fertility upon heat stress (HS) by detoxifying reactive oxygen species (ROS) and malondialdehyde (MDA) accumulation in developing anthers exposed to HS .
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 56587
Sequence Length: 492
Subcellular Location: Peroxisome
EC: 1.11.1.6
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P15202 | MSKLGQEKNEVNYSDVREDRVVTNSTGNPINEPFVTQRIGEHGPLLLQDYNLIDSLAHFNRENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRTKCLTRFSTVGGDKGSADTVRDPRGFATKFYTEEGNLDWVYNNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMFWDFLTTPENQVAIHQVMILFSDRGTPANYRSMHGYSGHTYKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQDLFEAIQNGNYPSWTVYIQTMTERDAKKLPFSVFDLTKVWPQGQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTTVPYQEASADPVLQARLFSYADAHRYRLGPNFHQIPVNCPYASKFFNPAIRDGPMNVNGNFGSEPTYLANDKSYTYIQQDRPIQQHQEVWNGPAIPYHWATSPGDVDFVQARNLYRVLGKQPGQQKNLAYNIGIHVEGACPQIQQRVYDMFARVDKGLSEAIKKVAEAKHASELSSNSKF | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 58555
Sequence Length: 515
Subcellular Location: Peroxisome
EC: 1.11.1.6
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P92131 | MALSLLLAVVCAKPLVSRAELRRIQALNPPWKAGMPKRFENVTEDEFRSMLIRPDRLRARSGSLPPISITEVQELVDPIPPQFDFRDEYPQCVKPALDQGSCGSCWAFSAIGVFGDRRCAMGIDKEAVSYSQQHLISCSLENFGCDGGDFQPTWSFLTFTGATTAECVKYVDYGHTVASPCPAVCDDGSPIQLYKAHGYGQVSKSVPAIMGMLVAGGPLQTMIVVYADLSYYESGVYKHTYGTINLGFHALEIVGYGTTDDGTDYWIIKNSWGPDWGENGYFRIVRGVNECRIEDEIYAVYLD | Function: Thiol protease which is required for parasite excystation and invasion of the proximal small intestine of the human host.
Sequence Mass (Da): 33508
Sequence Length: 303
Subcellular Location: Vacuole
EC: 3.4.22.-
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O33949 | MIATPVKIESVETILVDVPTIRPHRLSVATMNCQTLVLVRIRCADGVVGVGEGTTIGGLAYGEESPESIKVNIDTYFAPLLKGLDATRPGAAMATLRGLFQGNRFARSAVETALFDAQAQRLGVPLSELFGGRIRDSVDVAWTLASGDTTRDIDEAERVFEAKRHRVFKLKIGSRALADDVAHVVAIQKALQGRGEVRVDVNQAWTESEAIWAGKRFADASVALIEQPIAAENRAGLKRLTDLAQVPIMADEALHGPADAFALASARAADVFAVKIAQSGGLSGAANVAAIALAANIDLYGGTMLEGAVGTIASAQLFSTFGELKWGTELFGPLLLTEEILTEPLRYENFVLHLPQGPGLGITLDWDKIDRLRRDTRKGASITMN | Function: Catalyzes a syn cycloisomerization.
Catalytic Activity: (S)-muconolactone = cis,cis-muconate + H(+)
Sequence Mass (Da): 41138
Sequence Length: 385
Pathway: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydro-2-furylacetate from catechol: step 2/3.
EC: 5.5.1.1
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Q93VC9 | MADNCIRLLHSASVFFCLGLLISSFNLLQGIAAENLSKQKLTSWILQNEIVKEVNENPNAGWKASFNDRFANATVAEFKRLLGVKPTPKTEFLGVPIVSHDISLKLPKEFDARTAWSQCTSIGRILDQGHCGSCWAFGAVESLSDRFCIKYNMNVSLSVNDLLACCGFLCGQGCNGGYPIAAWRYFKHHGVVTEECDPYFDNTGCSHPGCEPAYPTPKCARKCVSGNQLWRESKHYGVSAYKVRSHPDDIMAEVYKNGPVEVAFTVYEDFAHYKSGVYKHITGTNIGGHAVKLIGWGTSDDGEDYWLLANQWNRSWGDDGYFKIRRGTNECGIEHGVVAGLPSDRNVVKGITTSDDLLVSSF | Function: Thiol protease that plays a central role in plant programmed cell death (PCD). In addition to its role in protein degradation, may cleave and/or degrade a number of target proteins, activating signaling towards PCD. Contributes to the increase of caspase-3-like activity after UV-C-induced PCD and is required for abiotic stress-induced PCD . Functions redundantly with CATHB1 and CATHB3 in basal defense and distinct forms of plant programmed cell death (PCD). Participates in the establishment of basal resistance against the bacterial pathogen Pseudomonase syringae pv. tomato DC3000. Required for full levels of PCD during resistance (R) gene-mediated hypersensitive response (HR). Involved in the regulation of senescence, a developmental form of PCD in plants .
Sequence Mass (Da): 40033
Sequence Length: 362
Subcellular Location: Vacuole
EC: 3.4.22.-
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P92132 | MKLFLLAAAAFSAPALTVSELNHIKSLNPRWKAGIPKRFEGLTKDEISSLLMPVSFLKNAKGAAPRGTFTDKDDVPESFDFREEYPHCIPEVVDQGGCGSCWAFSSVATFGDRRCVAGLDKKPVKYSPQYVVSCDHGDMACNGGWLPNVWKFLTKTGTTTDECVPYKSGSTTLRGTCPTKCADGSSKVHLATATSYKDYGLDIPAMMKALSTSGPLQVAFLVHSDFMYYESGVYQHTYGYMEGGHAVEMVGYGTDDDGVDYWIIKNSWGPDWGEDGYFRMIRGINDCSIEEQAYAGFFDE | Function: Thiol protease which is required for parasite excystation and invasion of the proximal small intestine of the human host.
Sequence Mass (Da): 33002
Sequence Length: 300
Subcellular Location: Vacuole
EC: 3.4.22.-
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Q94K85 | MAVYNTKLCLASVFLLLGLLLAFDLKGIEAESLTKQKLDSKILQDEIVKKVNENPNAGWKAAINDRFSNATVAEFKRLLGVKPTPKKHFLGVPIVSHDPSLKLPKAFDARTAWPQCTSIGNILDQGHCGSCWAFGAVESLSDRFCIQFGMNISLSVNDLLACCGFRCGDGCDGGYPIAAWQYFSYSGVVTEECDPYFDNTGCSHPGCEPAYPTPKCSRKCVSDNKLWSESKHYSVSTYTVKSNPQDIMAEVYKNGPVEVSFTVYEDFAHYKSGVYKHITGSNIGGHAVKLIGWGTSSEGEDYWLMANQWNRGWGDDGYFMIRRGTNECGIEDEPVAGLPSSKNVFRVDTGSNDLPVASV | Function: Thiol protease that possesses high activity toward the cathepsin synthetic substrate Arg-Arg-7-amino-4-methylcoumarin (RR-AMC) and the papain substrate Gly-Arg-Arg-AMC (GRR-AMC). Can cleave the papain substrate Phe-Arg-AMC (FR-AMC) and the caspase-3 substrate Asp-Glu-Val-Asp-rhodamine 110 (DEVD-R110). Has no activity towards the caspase-6 substrate VEID-AMC, caspase-8 substrate IETD-AMC and caspase-1 substrate YVAD-AMC . Plays a central role in plant programmed cell death (PCD). In addition to its role in protein degradation, may cleave and/or degrade a number of target proteins, activating signaling towards PCD. Contributes to the increase of caspase-3-like activity after UV-C-induced PCD and is required for abiotic stress-induced PCD . Functions redundantly with CATHB1 and CATHB2 in basal defense and distinct forms of plant programmed cell death (PCD). Participates in the establishment of basal resistance against the bacterial pathogen Pseudomonase syringae pv. tomato DC3000. Required for full levels of PCD during resistance (R) gene-mediated hypersensitive response (HR). Involved in the regulation of senescence, a developmental form of PCD in plants . May be involved in the degradation of seed storage proteins during seed germination .
Sequence Mass (Da): 39418
Sequence Length: 359
Subcellular Location: Vacuole
EC: 3.4.22.-
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Q43931 | MYKSVETILVDIPTIRPHKLSVTTMQTQTLVLIKIITEDGIVGWGEATTIGGLNYGEESPESVKANIDTYFKPLLLSIKAPLNVAQTLKLIRKSINGNRFAKCAIQTALLEIQAKRLNVPVSELLGGRIRDRLPVLWTLASGDTDKDIAEAKKMIELKRHNTFKLKIGSNPLQHDVDHVIAIKKALGPEISVRVDVNRAWSELECVKGIQQLQDGGIDLIEQPCAIENTDALARLTARFDVAIMADEVLTGPDSAYRIAKKSGADVFAVKVEQSGGLIEACEVAKIARLAGISLYGGTMLEGPVGSIASAHAFSTFETLEFGTELFGPLLLTQSILKTPLQYENFELVVPNTPGLGIEVDEDKLEQLRRH | Function: Catalyzes a syn cycloisomerization.
Catalytic Activity: (S)-muconolactone = cis,cis-muconate + H(+)
Sequence Mass (Da): 40415
Sequence Length: 370
Pathway: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydro-2-furylacetate from catechol: step 2/3.
EC: 5.5.1.1
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Q92405 | MRLTFIPSLIGVANAVCPYMTGELNRRDEISDGDAAAATEEFLSQYYLNDNDAFMTSDVGGPIEDQNSLSAGERGPTLLEDFIFRQKIQRFDHERVPERAVHARGAGAHGVFTSYGDFSNITAASFLAKEGKQTPVFVRFSTVAGSRGSSDLARDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQAATAHDSAWDFFSQQPSTMHTLLWAMSGHGIPRSFRHVDGFGVHTFRFVTDDGASKLVKFHWKSLQGKASMVWEEAQQTSGKNPDFMRQDLHDAIEAGRYPEWELGVQIMDEEDQLRFGFDLLDPTKIVPEEFVPITKLGKMQLNRNPRNYFAETEQVMFQPGHIVRGVDFTEDPLLQGRLFSYLDTQLNRHGGPNFEQLPINQPRVPVHNNNRDGAGQMFIPLNPHAYSPKTSVNGSPKQANQTVGDGFFTAPGRTTSGKLVRAVSSSFEDVWSQPRLFYNSLVPAEKQFVIDAIRFENANVKSPVVKNNVIIQLNRIDNDLARRVARAIGVAEPEPDPTFYHNNKTADVGTFGTKLKKLDGLKVGVLGSVQHPGSVEGASTLRDRLKDDGVDVVLVAERLADGVDQTYSTSDAIQFDAVVVAAGAESLFAASSFTGGSANSASGASSLYPTGRPLQILIDGFRFGKTVGALGSGTAALRNAGIATSRDGVYVAQSVTDDFANDLKEGLRTFKFLDRFPVDH | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
PTM: N-glycosylated.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 79910
Sequence Length: 728
Subcellular Location: Secreted
EC: 1.11.1.6
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Q877A8 | MRALSLASLIGIASAACPYMTGELERRDTGTDDATAATEEFLSQYYMADNDTFLTSDVGGPIEDQNSLQVGDRGPTLLEDFIFRQKIQRFDHERVPERAVHARGVGAHGVFTSYGDYSNITAASFLGAEGKETPVFVRFSTVAGSRGSSDLARDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQAATAHDSAWDFFSQQPSSLHTLLWAMSGHGIPRSLRHVDGFGIHTFRFVTDNGDSKLVKFHWKSLQGKASMVWEEAQQVSGKNPDFMRQDLFEAIEAGRYPEWELGVQIMDEEDQLKFGFDLFDPTKIVPEEYVPITKLGKMTLNRNPRNYFAETEQVMFQPGHIVRGVDFTEDPLLQGRLFSYLDTQLNRHGGPNFEQLPINQPRVPVHNNNRDGAGQMFIPLNPNAYSPNTLNKGSPKQANQTVGKGFFTAPGRESTGRFTRAVSPSFEDVWSQPRLFYNSLTPAEQQFVVDAIRFENSNVKSSVVRNNVIIQLNRVSNDLARRVARAIGVEEPEADPTYYHNNKTTDVGTFGQKLKKLDGLKVGFLASVETPASIEAASELSKQLSEDGVDVVVVAERLSDGVDQTYSGSDAIQFDAVIVAPGAEGLFSTFSFTAPSNATSSSTLFPAGRPLQIVIDGFRFGKPVGAVGSAATALKNAGIQTSRDGVYVDKSVTSGFVDGIKDGLRTFKFLDRFKLDH | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide through its degradation into water and oxygen.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 79868
Sequence Length: 725
Subcellular Location: Secreted
EC: 1.11.1.6
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Subsets and Splits