entry
stringlengths 6
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stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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B0JJ82
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GLMU_MICAN
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Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157)]
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MVAVAILAAGKGTRMKSSLPKVLHPLGSRSLVERVLNVSESLHPQRKLVIIGYQGQQVRNTLQHLDDIEFVEQKEQLGTGHAIQQLIPHLEDFQGDLLVLNGDVPLLRPETLQNLLQIHQDHGNAATLLTANLPNPKGYGRVFCDGNNLVKQIVEERDCTDAQRQNHRINGGIYCFNWSKLAAILPNLTPNNDQGEYYLTDVVNFLDPVMAVDVEDFLEITGINDRKQLAAAYDILQTRVKDDWMAAGVTIIDPDSVTIEDTVTLSADVIIEPQTHLRGETIIASGCRIGPGSLIENSRIGSDVTVLFSVISDSQVDSGCRIGPYAHLRGEAKIGANCRVGNFVEIKKSSIGNKTNIAHLSYLGDATLGEKVNVGAGTITANYDGVKKHQTMIGSGTKTGANSVLVAPLKLGKNVTVAAGSTITKNVPDNALVIARESQRVIENWADQFQ
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Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}.
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B0JZV4
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CBPC5_XENTR
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Cytosolic carboxypeptidase-like protein 5 (EC 3.4.17.-) (EC 3.4.17.24) (ATP/GTP-binding protein-like 5) (Protein deglutamylase CCP5)
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MEVRCGGLLFSSKFDSGNLARVEKVEKPGAEGDAFSGSVSGGSVPTPDYEFNIWTKPDCAETEYENGNRSWFYFSVRFGAPGKLIKINIMNMNKQSKLYSQGMAPFVRTVPIRSRWERIRDRPTFEMVENQFILSFVHRFLDCRGSTTYFAFCFPFSYEESQELMAGLDDRFSDCKNITPGSFPDSIYYHRELLCHSLDGLRVDLLTISSCHGMTEEREPRLDKLFPDRSTPRPYRFTGKRVYFLSSRVHPGETPSSFVFNGFLEFILRQDDPRAQMLRRMFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLNPDFELHPSVYAAKTVLLYHHVYNSVGPNDPDWRTSVSLQTSNISLCPKTSNHSLKDLPLEDSLSELEKANNLLNSMEKEECYITCPQAVTQGAPPENDPNFLSDSRDFIRQRDVFILESDTEPKDIYSHSGSSQPTIFTKSIPPQESGIAFYVDLHGHASKRGCFMYGNYFTEENDQVENMLYPKLISLNSANFDFLACNFSEKNMYAKDKRDGQSKEGSGRVAIHKATGIIHSYTLECNYNTGRCVNSIPAACHDCGRASPPPPPAFPPKYTTQVFEQIGRAVATAALDMAECNPWPRLIMSEYNNLTNLRAWMLKHLRNTKGVLPGTLKKKSTKSPVKASSLTSGSLSENSLIRTRSYSNSTASTNSQQNSPQIKPSINFTFLCSSSNHSPPKVSQRVLGPVRETKAQEKRRQQSLLRSSVRSPTACQQRLSTQAPSLSSGYPKTSSHAKTSCPLSLSLSMSGSGFSGLSQAAKVKNGTKKNNLEGDSTRQHIHQGHGIALLQNMQKRGSSHNNAEYSKSLESLGVRPSRIPVRRNGLLTNEKESPILRVWKYTTDTSLKHCSLADLAAVTSSLTVCSVPLLKSKAEEPVFICEATKETADQHFPAVSQDAAHLSAYQSVLSFCSEA
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Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Cleaves alpha- and gamma-linked polyglutamate tubulin side-chain, as well as the branching point glutamate. Also catalyzes the removal of alpha-linked glutamate residues from the carboxy-terminus of alpha-tubulin.
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B0K011
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OSR1_RAT
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Protein odd-skipped-related 1
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MGSKTLPAPVPIHPSLQLTNYSFLQAVNGLPTVPSDHLPNLYGFSALHAVHLHQWTLGYPAMHLPRSSFSKVPGAVSSLMDARFQLPAFPWFPHVIHPKPEITAGGSGAALKTKPRFDFANLALAATQEDPTKLGRGEGPGSPAGGLGALLDVTKLSPEKKPTRGRLPSKTKKEFVCKFCGRHFTKSYNLLIHERTHTDERPYTCDICHKAFRRQDHLRDHRYIHSKEKPFKCQECGKGFCQSRTLAVHKTLHSQVKELKTSKIKC
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Transcription factor that plays a role in the regulation of embryonic heart and urogenital development.
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B0K019
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BAG1_RAT
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BAG family molecular chaperone regulator 1 (BAG-1) (Bcl-2-associated athanogene 1)
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MADRGGARRPRGDQEPLGPRLRAPRSARETRQSESRAERGLPPSQRSSVRSAASGHDRSTRGAASGACKPRVKKKVRPRSSQSEKVAHSKELTRSKKLTRSKKVTGTQEATQVEEVTTIEEATQTEEITVAEEVTQTENMAQTEEMVQTEEMEPPTLSVVVTHSNERYDLLVTPQQGNSEPIVQDLAQLVEEATGVPLPFQKLIFKGKSLKEMETPLSALGMQNGCRVMLIGEKSNPEEEAELKKLKDLEVSVEKTANHLEELNKELSDIQQGFLAKELQAEALCRLDRKIKATIEQFMKILEEIDTMVLPENFKDSRLKRKNLVKKVQVFLAECDTVEQYICQETERLQSTNLALPE
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Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli.
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B0K020
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CISD1_RAT
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CDGSH iron-sulfur domain-containing protein 1 (Cysteine transaminase CISD1) (EC 2.6.1.3) (MitoNEET)
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MGLSSDSPVRVEWIAAVTFAAGTAALGYLAYKKFYAKESRTKAMVNLQIQKDNPKVVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHIKHNEETGDNVGPLIIKKKET
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L-cysteine transaminase that catalyzes the reversible transfer of the amino group from L-cysteine to the alpha-keto acid 2-oxoglutarate to respectively form 2-oxo-3-sulfanylpropanoate and L-glutamate (By similarity). The catalytic cycle occurs in the presence of pyridoxal 5'-phosphate (PLP) cofactor that facilitates transamination by initially forming an internal aldimine with the epsilon-amino group of active site Lys-55 residue on the enzyme (PLP-enzyme aldimine), subsequently displaced by formation of an external aldimine with the substrate amino group (PLP-L-cysteine aldimine). The external aldimine is further deprotonated to form a carbanion intermediate, which in the presence of 2-oxoglutarate regenerates PLP yielding final products 2-oxo-3-sulfanylpropanoate and L-glutamate. The proton transfer in carbanion intermediate is suggested to be controlled by the active site lysine residue, whereas PLP stabilizes carbanion structure through electron delocalization, also known as the electron sink effect (By similarity). Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation (By similarity). May be involved in iron-sulfur cluster shuttling and/or in redox reactions. Can transfer the [2Fe-2S] cluster to an apo-acceptor protein only when in the oxidation state, likely serving as a redox sensor that regulates mitochondrial iron-sulfur cluster assembly and iron trafficking upon oxidative stress (By similarity).
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B0KH74
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FADB_PSEPG
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MIYEGKAITVKALESGIVELKFDLKGESVNKFNRLTLNELRQAVEAIQADASVKGVIVSSGKDVFIVGADITEFVDNFKLPEAELVAGNLEANRIFNAFEDLEVPTVAAINGIALGGGLEMCLAADYRVMSNSAKIGLPEVKLGIYPGFGGTVRLPRLIGSDNAIEWIAAGKENRAEDALKVGAVDAVVAPELLLAGALDLIKRAISGELDYKAKRQPKLEKLKLNAIEQMMAFETAKGFVAGQAGPNYPAPVEAIKSIQKAANFGRDKALEVEAAGFAKLAKTSVAESLIGLFLNDQELKRKAKAHDEIAHDVKQAAVLGAGIMGGGIAYQSAVKGTPILMKDIREEAIQLGLNEASKLLGNRVEKGRLTPAKMAEALNAIRPTLSYGDFANVDIVVEAVVENPKVKQAVLAEVEGQVKDDAILASNTSTISINLLAKALKRPENFVGMHFFNPVHMMPLVEVIRGEKSSEVAVATTVAYAKKMGKNPIVVNDCPGFLVNRVLFPYFGGFAKLVSAGVDFVRIDKVMEKFGWPMGPAYLMDVVGIDTGHHGRDVMAEGFPDRMKDERRSAVDALYEANRLGQKNGKGFYAYETDKRGKPKKVFDATVLDVLKPIVFEQREVTDEDIINWMMVPLCLETVRCLEDGIVETAAEADMGLVYGIGFPPFRGGALRYIDSIGVAEFVALADQYADLGPLYHPTAKLREMAKNGQRFFN
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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B0KW95
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CADH2_CALJA
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Cadherin-2 (Neural cadherin) (N-cadherin) (CD antigen CD325)
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MCRIAGAPRTLLPLLAALLQASVEASGEIALCKTGFPEDVYSAVLSKDVHEGQPLLNVKFSNCNGKRKVQYESSEPADFKVDEDGMVYAVRSFPLSSEHAKFLIYAQDKETQEKWQVAVKLSLKPTLPEESVKESTEVEEIVFPRQLGKHSGHLQRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDREQIARFHLRAHAVDINGNQVENPIDIVINVIDMNDNRPEFLHQVWNGTVPEGSKPGTYVMTVTAIDADDPNALNGMLRYRILSQAPSTPSPNMFTINNETGDIITVAAGLDREKVQQYTLIIQATDMEGNPTYGLSNTATAIITVTDVNDNPPEFTAMTFYGEVPENRVDVIVANLTVTDKDQPHTPAWNAVYRISGGDPTGRFAIQTDPNSNDGLVTVVKPIDFETNRMFVLTVAAENQVPLAKGIQHPPQSTATVSVTVIDVNENPYFAPNPKIIRQEEGLHAGTMLTTFTAQDPDRYMQQNIRYTKLSDPANWLKIDPVNGQITTIAILDRESPNVKNNIYNATFLASDNGIPPMSGTGTLQIYLLDINDNAPQVLPQEAETCETPDPNSINITALDYDIDPNAGPFAFDLPLSPVNIKRNWTITRLNGDFAQLNLKIKFLEAGIYEVPIIITDSGNPPKSNISILRVKVCQCDSNGDCTDVDRIVGAGLGTGAIIAILLCIIILLILVLMFVVWMKRRDKERQAKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPDTVEPDAIKPVGIRRMDERPIHAEPQYPVRSAAPHPGDIGDFINEGLKAADNDPTAPPYDSLLVFDYEGSGSTAGSLSSLNSSSSGGEQDYDYLNDWGPRFKKLADMYGGGDD
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Calcium-dependent cell adhesion protein preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell. Cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence. Plays a role in cell-to-cell junction formation between pancreatic beta cells and neural crest stem (NCS) cells, promoting the formation of processes by NCS cells (By similarity). Required for proper neurite branching. Required for pre- and postsynaptic organization (By similarity). CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density.
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B0KWU8
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BRCC3_CALJA
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Lys-63-specific deubiquitinase BRCC36 (EC 3.4.19.-) (BRCA1-A complex subunit BRCC36) (BRCA1/BRCA2-containing complex subunit 3) (BRCA1/BRCA2-containing complex subunit 36) (BRISC complex subunit BRCC36)
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MAVQVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDTRSDSKFAYTGTEMRTVAEKVDAVRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSIQAQKSSESLHGPRDFWSSSKHISIEGQKEEERYERIEIPIHIVPHVTIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHLRELQQEKEELMQELSSLE
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Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1 deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (By similarity). Acts as a regulator of the NLRP3 inflammasome by mediating deubiquitination of NLRP3, leading to NLRP3 inflammasome assembly (By similarity). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (By similarity). Deubiquitinates HDAC1 and PWWP2B leading to their stabilization (By similarity).
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B0KYV5
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LIMA1_PIG
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LIM domain and actin-binding protein 1 (Epithelial protein lost in neoplasm)
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MESTPFNRQQWTSLSLRVTAKELSLVNKNKSSAIVEIFSKYQKAAEEANMEKRRSNTENLPQHFRRGNLTVLKKKWENPAPGVESLPESTRNSSAEVRHRGDPPPAEVASSSASGVEADQGVCPRPRFSSPPEVPYPNPRIKDTEHLKDHSAESKKMENCLAESRHEVGKPETSENAEASNKIEKYNVPLNRLKMMFERGEPAQTKILRAQSRSTGGRKISENSYSLDDLEIGPGQLSSSAFNTEKSESRRNLEFPRLSDTSIKDRMAKYQAAVSKQSSSTNYTNELKANGGEIKTHKLEQKENVPPGPEVCISHQDGEKVSASENSLAACSTPPEDDSCKSQVKSDVQQPVHPKPLSPVARASSLSESSPPKAVKKFQAPARETCVECQKTVYPMERLLANQQVFHISCFRCSYCNNKLSLGTYASLHGRIYCKPHFNQLFKSKGNYDEGFGHRPHKDLWASKLENEETLERPAQLPNAAEIPQSPGVEDAPIAKVGVLTASMEAKASSQLEKEDKPAETKKLRIAWPPPTELSSSGSALEEGIKVSKPKWPPEDEVSKPEAPEDVDLDLKKLRRSSSLKERSRPFTVAASFRTASVKSPKPLSPPMRKGWSLSEQSEEFGGGVAAERKQMEKASASEKNGSVGKTTWPSKESRGGEAAGRSKEVQDFEIGSENLIENGASLDEGDRDLLQQQSPLEPKSKNWSSFADNTSAKEFTTQKQKSQDVEFWEGEVVEELSVEEQIKRNRYYDEEEDEE
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Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (By similarity). Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (By similarity).
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B0L3A2
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DESPR_HUMAN
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Dual endothelin-1/VEGF signal peptide receptor (DEspR protein) (Dual endothelin-1/VEGFsp receptor) (FBXW7 antisense RNA 1)
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MTMFKGSNEMKSRWNWGSITCIICFTCVGSQLSMSSSKASNFSGPLQLYQRELEIFIVLTDVPNYRLIKENSHLHTTIVDQGRTV
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Dual receptor for both endothelin-1 and the signal sequence of vascular endothelial growth factor A. Does not act as a receptor for angiotensin-2. Does not bind the VEGFA mature protein (By similarity). May play a role in angiogenesis with a significant role in cardiovascular and neural development (By similarity).
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B0LDU5
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PKS4_RUBID
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Polyketide synthase 4 (RiPKS4) (EC 2.3.1.212) (EC 2.3.1.74) (Benzalacetone synthase PKS4) (RiBAS) (Naringenin-chalcone synthase PKS4)
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MVTVEEVRKAQRAEGPATVLAIGTATPPNCVGQSTYPDYYFRITNSEHKIELKQKFQRMCDKSMIKKRYMYLTEEILKENPSMCEYMAPSLDARQDMVIVEIPKLGKEAATKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLIKLFGLRPSVKRLMMYQQGCFAGGTVLRLAKDLAENNRGARVLVVCSEITVVTFRGPSDTHLDCLVGQALFGDGVASIIVGADPLPEIEKPLFELVSAAQTILPDSEGAIEGHLREVGLTFHLLENVPALISKNIEKSLNETFKPLDIMDWNSLFWIAHPGGPAILDQVEAKLGLKPEKLEATGHILSEYGNMSSACVLFILDVVRRKSAANGVTTRILSIGQISKSLLILAWFLFSLV
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Bifunctional polyketide synthase producing both 4-hydroxybenzalacetone and naringenin chalcone. Can use p-coumaryl-CoA and ferulyl-CoA as substrates. Catalyzes the initial key reaction step in the biosynthesis of phenylbutanoids.
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B0LL23
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PLR_SINHE
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Bifunctional pinoresinol-lariciresinol reductase (PhPLR) ((+)-lariciresinol reductase) (EC 1.23.1.2) ((+)-pinoresinol reductase) (EC 1.23.1.1)
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MAKSRVLIVGGTGYLGRRMVKACLDQGHTTYVLHRQEVGVDIDKIQMLLSFKEQGAHLVEGSFNDHRSLVEAVKLVDVVICTISGVHIRSHQILLQLKLVEAIEEAGNVKRFLPSEFGMDPARMAHAMEPGRATFDEKMVVRKAIEDAKIPHTYASANCFAGYFLGGLCQFGKIIPSKESVILSGDGNVKGIYVDEYDIATYTIKTMDDPRTLNKTIYIRPPANILSQREVVEIWEKLIGKVLDKSSLSEEDFLALMKGLSHGHQAGLTHYYHVSYEGCLTNFEVEDGVDASKLYPQVNYTTVSEYLKRYL
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Reductase involved in lignan biosynthesis. Also involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family. Catalyzes the enantioselective sequential conversion of (+)-pinoresinol into (+)-lariciresinol and of (+)-lariciresinol into (-)-secoisolariciresinol. Abstracts the 4R-hydride from the NADPH cofactor during catalysis.
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B0LPN4
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RYR2_RAT
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Ryanodine receptor 2 (RYR-2) (RyR2) (Cardiac muscle ryanodine receptor) (Cardiac muscle ryanodine receptor-calcium release channel) (Type 2 ryanodine receptor)
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MADAGEGEDEIQFLRTDDEVVLQCTATIHKEQQKLCLAAEGFGNRLCFLESTSNSKNVPPDLSICTFVLEQSLSVRALQEMLANTVEKSEGKFMMKTAQGGGHRTLLYGHAILLRHSYSGMYLCCLSTSRSSTDKLAFDVGLQEDTTGEACWWTIHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSYGNSSWRVDAAFQQTLWSVAPISSGSEAAQGYLIGGDVLRLLHGHMDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLMEDKNLLLMDKEKADVKSTAFAFRSSKEKLDAGVRKEVDGMGTSEIKYGDSICYIQHVDTGLWLTYQAVDVKSARMGSIQRKAIMHHEGHMDDGLNLSRSQHEESRTARVIRSTVFLFNRFIRGLDALSKRAKLPTVDLPIESVSLSLQDLIGYFHPPDEHLEHEDKQNRLRALKNRQNLFQEEGMINLVLECIDRLHVYSSAAHFADVAGREAGESWKSILNSLYELLAALIRGNRKNCAQFSGSLDWLISRLERLEASSGILEVLHCVLVESPEALNIIKEGHIKSIISLLDKHGRNHKVLDVLCSLCVCHGVAVRSNQHLICDNLLPGRDLLLQTRLVNHVSSMRPNIFLGVSEGSAQYKKWYYELMVDHTEPFVTAEATHLRVGWASTEGYSPYPGGGEEWGGNGVGDDLFSYGFDGLHLWSGCIARTVSSPNQHLLRTDDVISCCLDLSAPSISFRINGQPVQGMFENFNIDGLFFPVVSFSAGIKVRFLLGGRHGEFKFLPPPGYAACYEAVLPKEKLKVEHSREYKQERTYTRDLLGPTVSLTQAAFTPVPVDTSQIVLPPHLERIRERLAENIHELWVMNKIELGWQYGPVRDDNKRQHPCLVEFCKLPEQERNYNLQMSLETLKTLLALGCHVGIADEHAEEKVKKMKLPKNYQLTSGYKPAPMDLSFIKLTPSQEAMVDKLAENAHNVWARDRIRQGWTYGIQQDVKNRRNPRLVPYTLLDDRTKKSNKDSLREAVRTLLGYGYHLEAPDQDHASRAEVCSGTGERFRIFRAEKTYAVKAGRWYFEFEAVTAGDMRVGWSRPGCQPDLELGSDERAFAFDGFKAQRWHQGNEHYGRSWQAGDVVGCMVDMNEHTMMFTLNGEILLDDSGSELAFKDFDVGDGFIPVCSLGVAQVGRMNFGKDVSTLKYFTICGLQEGYEPFAVNTNRDITMWLSKRLPQFLQVPSNHEHIEVTRIDGTIDSSPCLKVTQKSFGSQNSNTDIMFYRLSMPIECAEVFSKSVAGGIPGAGFYGPKNDLEDFDVDSDFEVLMKTAHGHLVPDRMDKDKETPKPEFNNHKDYAQEKPSRLKQRFLLRRTKPDYSTSHSARLTEDVLADDRDDYEYLMQTSTYYYSVRIFPGQEPANVWVGWITSDFHQYDTGFDLDRVRTVTVTLGDEKGKVHESIKRSNCYMVCAGESMSPGQGRNNSNGLEIGCVVDAASGLLTFIANGKELSTYYQVEPSTKLFPAVFAQATSPNVFQFELGRIKNVMPLSAGLFKSEHKNPVPQCPPRLHVQFLSHVLWSRMPNQFLKVDVSRISERQGWLVQCLDPLQFMSLHIPEENRSVDILELTEQEELLQFHYHTLRLYSAVCALGNHRVAHALCSHVDEPQLLYAIENKYMPGLLRAGYYDLLIDIHLSSYATARLMMNNEFIVPMTEETKSITLFPDENKKHGLPGIGLSTSLRPRMCFSSPSFVSISNECYQYSPEFPLDILKAKTIQMLTEAVKEGSLHARDPVGGTTEFLFVPLIKLFYTLLIMGIFHNEDLKHILQLIEPSVFKEAATPEEEGGAPEKEISIDDSKLEVKEEAKAGKRPKEGLLQMKLPEPVKLQMCLLLQYLCDCQVRHRIEAIVAFSDDFVAKLQDNQRFRYNEVMQALNMSAALTARKEFRSPPQEQINMLLNFKDDKSECPCPEEIRDQLLDFHEDLMTHCGIELDEDGSLDGSNDLTIRGRLLSLVEKVTYLKKKQAEKPVASDSRKSSSLQQLISETMVRWAQESVIEDPELVRAMFVLLHRQYDGIGGLVRALPKTYTINGVSVEDTINLLASLGQIRSLLSVRMGKEEEKLMIRGLGDIMNNKVFYQHPNLMRALGMHETVMEVMVNVLGGGESKEITFPKMVANCCRFLCYFCRISRQNQKAMFDHLSYLLENSSVGLASPAMRGSTPLDVAAASVMDNNELALALREPDLEKVVRYLAGCGLQSCQMLVSKGYPDIGWNPVEGERYLDFLRFAVFCNGESVEENANVVVRLLIRRPECFGPALRGEGGNGLLAAMEEAIKIAEDPSRDGPSPTSGSSKTLDAEEEEDDTIHMGNAIMTFYAALIDLLGRCAPEMHLIHAGKGEAIRIRSILRSLIPLGDLVGVISIAFQMPTIAKDGKVVEPDMSAGFCPDHKAAMVLFLDRVYGIEVQDFLLHLLEVGFLPDLRAAASLDTAALSATDMALALNRYLCTAVLPLLTRCAPLFAGTEHHASLIDSLLHTVYRLSKGCSLTKAQRDSIEVCLLSICGQLRPSMMQHLLRRLVFDVPLLNEHAKMPLKLLTNHYERCWKYYCLPGGWSNFGAASEEELHLSRKLFWGIFDALSQKKYEQELFKLALPCLSAVAGALPPDYMESNYVSMMEKQSSMDSEGNFNPQPVDTSNITIPEKLEYFINKYAEHSHDKWSMDKLANGWIYGEIYSDSSKIQPLMKPYKLLSEKEKEIYRWPIKESLKTMLAWGWRIERTREGDSMALYNRTRRISQTSQVSIDAAHGYSPRAIDMSNVTLSRDLHAMAEMMAENYHNIWAKKKKMELESKGGGNHPLLVPYDTLTAKEKAKDREKAQDIFKFLQISGYAVSRGFKDLDLDTPSIEKRFAYSFLQQLIRYVDEAHQYILEFDGGSRSKGEHFPYEQEIKFFAKVVLPLIDQYFKNHRLYFLSAASRPLCTGGHASNKEKEMVTSLFCKLGVLVRHRISLFGNDATSIVNCLHILGQTLDARTVMKTGLDSVKSALRAFLDNAAEDLEKTMENLKQGQFTHTRSQPKGVTQIINYTTVALLPMLSSLFEHIGQHQFGEDLILEDVQVSCYRILTSLYALGTSKSIYVERQRSALGECLAAFAGAFPIAFLETHLDKHNVYSIYNTRSSRERAALSLPANVEDVCPNIPSLEKLMTEIIELAESGIRYTQMPHMMEVVLPMLCSYMSRWWEHGPENHPERAEMCCTALNSEHMNTLLGNILKIIYNNLGIDEGAWMKRLAVFSQPIINKVKPQLLKTHFLPLMEKLKKKAAMVVSEEDHLKAEARGDMSEAELLILDEFTTLARDLYAFYPLLIRFVDYNRAKWLKEPNPEAEELFRMVAEVFIYWSKSHNFKREEQNFVVQNEINNMSFLITDTKSKMSKAAISDQERKKMKRKGDRYSMQTSLIVAALKRLLPIGLNICAPGDQELIALAKNRFSLKDTEEEVRDVIRSNIHLQGKLEDPAIRWQMALYKDLPNRAEDTSDPERTVERVLDIANVLFHLEQVEHPQRSKKAVWHKLLSKQRKRAVVACFRMAPLYNLPRHRAVNLFLQGYEKSWIETEEHYFEDKLIEDLAKPGSELPEEDEAMKRVDPLHQLILLFSRTALTEKCKLEEDFLYMAYADIMAKSCHDEEDDDGEEEVKSFEVTGSQRSKEKEMEKQKLLYQQARLHDRGAAEMVLQTFSASKGETGPMVAATLKLGIAILNGGNSTVQQKMLDYLKEKKDVGFFQSLAGLMQSCSVLDLNAFERQNKAEGLGMVTEEGSGEKVLQDDEFTCDLFRFLQLLCEGHNSDFQNYLRTQTGNNTTVNIIISTVDYLLRVQESISDFYWYYSGKDIIDEQGQRNFSKAIQVAKQVFNTLTEYIQGPCTGNQQSLAHSRLWDAVVGFLHVFAHMQMKLSQDSSQIELLKELMDLQKDMVVMLLSMLEGNVVNGTIGKQMVDMLVESSNNVEMILKFFDMFLKLKDLTSSDTFKEYDPDGKGVISKRDFHKAMESHKHYTQSETEFLLSCAETDENETLDYEEFVKRFHEPAKDIGFNVAVLLTNLSEHMPNDTRLQTFLELAESVLNYFQPFLGRIEIMGSAKRIERVYFEISESSRTQWEKPQVKESKRQFIFDVVNEGGEKEKMELFVNFCEDTIFEMQLAAQISESDLNERSANKEESEKERPEEQAPRMGFFSLLTVQSALFALRYNVLTLVRMLSLKSLKKQMKRMKKMTVKDMVSAFFSSYWSVFVTLLHFVASVCRGFFRIVSSLLLGGSLVEGAKKIKVAELLANMPDPTQDEVRGDEEEGERKPLESALPSEDLTDLKELTEESDLLSDIFGLDLKREGGQYKLIPHNPNAGLSDLMTNPIPVPEVQEKFQEQKVKEEKEGKEETKSEPEKAEGEDGEKEEKAKDDKGKQKLRQLHTHRYGEPEVPESAFWKKIIAYQQKLLNYFARNFYNMRMLALFVAFAINFILLFYKVSTSSVVEGKELPTRTSSDAAKVTTSLDSSPHRIIAVHYVLEESSGYMEPTLRILAILHTIISFFCIIGYYCLKVPLVIFKREKEVARKLEFDGLYITEQPSEDDIKGQWDRLVINTQSFPNNYWDKFVKRKVMDKYGEFYGRDRISELLGMDKAALDFSDAREKKKPKKDSSLSAVLNSIDVKYQMWKLGVVFTDNSFLYLAWYMTMSVLGHYNNFFFAAHLLDIAMGFKTLRTILSSVTHNGKQLVLTVGLLAVVVYLYTVVAFNFFRKFYNKSEDGDTPDMKCDDMLTCYMFHMYVGVRAGGGIGDEIEDPAGDEYEIYRIIFDITFFFFVIVILLAIIQGLIIDAFGELRDQQEQVKEDMETKCFICGIGNDYFDTVPHGFETHTLQEHNLANYLFFLMYLINKDETEHTGQESYVWKMYQERCWEFFPAGDCFRKQYEDQLN
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Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca(2+) levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity is modulated by formation of heterotetramers with RYR3. Required for cellular calcium ion homeostasis. Required for embryonic heart development (By similarity).
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B0LSW3
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LIS1_FELCA
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Platelet-activating factor acetylhydrolase IB subunit beta (Lissencephaly-1 protein) (LIS-1) (PAF acetylhydrolase 45 kDa subunit) (PAF-AH 45 kDa subunit) (PAF-AH alpha) (PAFAH alpha)
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MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR
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Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition-dependent manner (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos. May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By similarity).
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B0LT89
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STK24_RAT
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Serine/threonine-protein kinase 24 (EC 2.7.11.1) (Mammalian STE20-like protein kinase 3) (MST-3) (MST3b) (STE20-like kinase MST3) [Cleaved into: Serine/threonine-protein kinase 24 35 kDa subunit (Mammalian STE20-like protein kinase 3 N-terminal) (MST3/N); Serine/threonine-protein kinase 24 12 kDa subunit (Mammalian STE20-like protein kinase 3 C-terminal) (MST3/C)]
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MAHSPVQSGLPGMQTLKADPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGPLDEIQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELAKGEPPHSELHPMKVLFLIPKNNPPTLEGSYSRPLKEFVEACLNKEPSFRPTAKELLKHKFIIRNAKKTSYLTELIDRYKRWKAEQSHEDSSSEDSDVETDSQASGGSDSGDWIFTIREKDPKNLENGTLQPSDLERNKMKDFPKRPFSQCLSTIISPLFAELKEKSQACGGNLGSIEELRGAIYLAEEACPGISDTMVAQLVQRLQRYSLSGGGASAH
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Serine/threonine-protein kinase that acts on both serine and threonine residues and promotes apoptosis in response to stress stimuli and caspase activation. Mediates oxidative-stress-induced cell death by modulating phosphorylation of JNK1-JNK2 (MAPK8 and MAPK9), p38 (MAPK11, MAPK12, MAPK13 and MAPK14) during oxidative stress. Plays a role in a staurosporine-induced caspase-independent apoptotic pathway by regulating the nuclear translocation of AIFM1 and ENDOG and the DNase activity associated with ENDOG. Phosphorylates STK38L on 'Thr-442' and stimulates its kinase activity. In association with STK26 negatively regulates Golgi reorientation in polarized cell migration upon RHO activation. Regulates also cellular migration with alteration of PTPN12 activity and PXN phosphorylation: phosphorylates PTPN12 and inhibits its activity and may regulate PXN phosphorylation through PTPN12 (By similarity). Acts as a key regulator of axon regeneration in the adult optic nerve and radial nerve.
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B0M3E8
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UGE1_PEA
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Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 1 (EC 5.1.3.2) (EC 5.1.3.5) (UDP-D-xylose 4-epimerase) (UDP-L-arabinose 4-epimerase) (UDP-galactose 4-epimerase 1) (UDP-glucose 4-epimerase 1) (PsUGE1)
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MVASSQKILVTGGAGFIGTHTVVQLLNNGFNVSIIDNFDNSVMEAVERVREVVGSNLSQNLEFTLGDLRNKDDLEKLFSKSKFDAVIHFAGLKAVGESVENPRRYFDNNLVGTINLYEVMAKHNCKKMVFSSSATVYGQPEKIPCVEDFKLQAMNPYGRTKLFLEEIARDIQKAEPEWRIVLLRYFNPVGAHESGKLGEDPRGIPNNLMPYIQQVAVGRLPELNVYGHDYPTRDGSAIRDYIHVMDLADGHIAALRKLFTSENIGCTAYNLGTGRGSSVLEMVAAFEKASGKKIALKLCPRRPGDATEVYASTAKAEKELGWKAKYGVEEMCRDQWNWAKNNPWGYSGKP
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Catalyzes the interconversion between UDP-glucose and UDP-galactose and the interconversion between UDP-arabinose and UDP-xylose.
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B0R0I6
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CHD8_DANRE
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Chromodomain-helicase-DNA-binding protein 8 (CHD-8) (EC 3.6.4.12) (ATP-dependent helicase CHD8)
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MADPIMDLFDDTPLFNLDSLPEDAFSQGSSDPVEEALKLALGQVDPPTDPIPDPGVPILSDVVTDPALIPTPVSVPLQNLQTQQLSQIPHEVSVASAPISIQPSLSVASNSSGAATVLLSSSLGVPVSGAQVTPQQQTQQITAVTQQAAGQHAPKIVILKGPQGQTQVLQGVTGATGSPGKVTLARVLTGTPLRPGMAVVSGGTVLNATSPAQGQVKVGTGVQRLVQTANGPMKQVLLTSVPQTQSQVQTQPVQVQIPVQTQLQSPSQPQQLQAQIQAQTQVALQTQAQTQTPTSPAAAGIRPQSVTLSAVPQQVRFVLGSLPGKLVLQGDQLAALAQAKAGQTGAQAKVLTIQLQVQQQPNQQGAKFQLVSGAANAGGSPQVVQISQGQGGQRLAVPLKLLLQPQSNTVSSAGGAVSVVKVINTSAAGSTSGTTTTAASSGVRLAKIQEPVRRVETLCKQEKANRIVAEAIARAKARGERNIPRVLNQDELPAGQTSADLEGAGGATGAKKKGGGGVGGGGGGSKKKSPSAGGAKMVVGGDKKSKAKTPVIPGGGSKSKSKTKLNTITLVGKKRKRNPSSDHSDVDLSPPVSPRTLEEEMSQKRRSNRQVKRKKYTEDLDIKITDDEDELDADVDVTTTPMPAVGHVQPLGAELPPELDGDGLPSMQFFVENPSEEDAAIVDKILSMRVTKKEARQYTNVEEFFVKYKNYSYMHCEWASLEQLERDKRIHQKLKRFKTKQAQMRNLFQEDEEPFNPDYVEVDRILDESHSVDKDNGEPVVYYLVKWCSLPYEDATWELKEDVDEGKVEEFRKIESRQPRLKRTPRPAASAWKKLDESTEYKNGNQLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIALLSEMFSAGVQSPFMIIAPLSTITNWEREFSNWTDMNAIVYHGSLASRQMIQQYEMYCKDDKGHLIPGAYKFDALITTFEMILSDCPELREISWRCVVIDEAHRLKNRNCKLLDSLKMLEIEHKVLLTGTPLQNTVEELFSLLHFLEPAQFPSEIEFLREFGDLKTEEQVQKLQSILKPMMLRRLKEDVEKNLAPKQETIIEVELTDVQKKYYRAILERNFSFLSMGATQNSNVPNLLNTMMELRKCCNHPYLITGAEEKIVSELREVYDPLAPDFHLQALVRSAGKLVLLDKLLPRLKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDRFVFLLCTRAGGLGINLTAADTCVIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMLDKASLKLGLDRAVLQSMSGNKESSIQQFSKKEIEDLLRKGAYAAIMDENDEGSRFCEEDIDQILQRRATTITIESEGKGSTFSKASFVASENRTDIALDDPEFWQKWAKKADIDMDSLNRKNTLVIDTPRVRKQTRQFSSLRGEGGDLSDLDSDDDYPPHNSRQSRASRRSDRHSGGGYGRTDCFRVEKHLLVYGWGRWRDILSHARCKRRLSERDVETICRVILVFCLIHYRGDENIKSFIWELITPPENGREPQALLNHSGLSIPVPRGRKGKRVKAQSSFDVQKVEWIRKYNPDSLLLDDSYRKHLKHQCNKVLLRVRMLYYLKQEVIGEHADSVLSGADARDIDIWLPEMEQQDVPSGWWDAEADRCLLIGVYKHGYEMYTTMRADPCLCFVERCGRPNEQDINAEQQAADPELGEGGDYDKYSEDPEFKPATRHAKEMYEEGDSVNADGEICVEDRSAPMQVEGPSSGSSDLCYWPTSSSLTARLRRLITAYQRSYRREQLKIEAAEKGDRRRRRCEQATKLKEIARQERQQRWTRREECDFYRVVSTFGVERIKKETDAPEGDEHHMDWNRFRSFARLDKKTDESLTRYFKCFMSMCRKVCHIRPGRGDESQDMSQSLAPITEERASRTLYRVTLLCRLRERVLPHPSLEERLSLAPQTSDLPSWWSIPKHDHELLLAAARHGVSRTELSIFSDPLYSFSQSRLDYLQNQQAQAAAQIHAFSQSQDPAGIKEEGLEDESRLLGVEALCPSDSPAMLLSHSDSKVGIQAGWVWKKSKNNGPSERKLGGGGGGASDSDSDSDSGSSSSSRHSGSSDDSGDSDVEREQAALKMCDGDEENSILSLTPSQEGAPPESLTDPLRVDWPKDRILINRIENLCSLVITGHWPSGRRYISDIQLNTVSDEHELGDDLGYSRVARKINSTLSAEALEGQESEFTVKLLKEEGLKLTFSKQALMPNGEGSARKKRKDHELEDAEGVLHAPRRRDLPNWLKENPDYEVEGDMLELLVNRTKRKRRRKRVEKGAALTGSERVKVIDIRTGKKFAGVFGPALQDLREHLEENPDHAVAPEWSETVRHSGFLPEILFHRLLSPHASIPKKSRHYLHTPSLQTDDPLLGGGEGEMLVSDGAYMMDDEDLEDGGHLTSSHHFLTPAYDVKMEPSALDMDGGDSLSQGGYDSSDREAILDDVIMAPKHSDTSSSSED
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DNA helicase that acts as a chromatin remodeling factor and regulates transcription. Acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. Suppresses p53/tp53-mediated apoptosis by recruiting histone H1 and preventing p53/tp53 transactivation activity. Acts as a negative regulator of Wnt signaling pathway by regulating beta-catenin (ctnnb1) activity. Negatively regulates ctnnb1-targeted gene expression by being recruited specifically to the promoter regions of several ctnnb1 responsive genes. May also act as a transcription activator by participating in efficient U6 RNA polymerase III transcription. {ECO:0000255|HAMAP-Rule:MF_03071}.
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B0R6I4
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BAST_HALS3
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Transducer protein BasT (Branched chain and sulfur-containing amino acids transducer protein)
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MSDIDRGLFERVLPARIRGSYAAKFNVLLLVVVIIVAAAGGYIHLQTQSTVGENTERRVSGIAEQQAATLHDWLTQKESTTTFLASNIGGDAVRTSDVKPQLERQLATLQQDVRAIHVVSTSQDTVVASTDDARSGTTLQAGDAPWLSTIEDGTTDVSVSDPYEVDDSPVVAMTAPTDKPGWVLVMTMSLAQHSQSFNSPIATGDVKVVNGDGVITLDNRNRALLEQYTDTAGNVPAAVATARSGQTVYNTEPERTGMDDGRYATAYTPVAGTDWVLTYHVPRGQAYALQSEVTQNLAGLVVVALVGLLLVGLTVGRRTSSALDELAGVAAAIADGDLDTTIPDTDRTDELGQLVGAFGEMQTYLTTAASQADALADQNFDADVLDEDLPGAFGASLSQMHTRLEALITDLDEAREDAEQTRKDAEEARAASERLNERLERRAAEYSDEMAAAAAGDLTRRLDEDVDSEPMQDIAEAFNDMMGDVEATLAQVRSIADAVDAASTDVSTSAAEIRSASDQVSESVQDISADADQQRDRLGTVGDEVTSLSATVEEIAASADDVAETVNQAATESERGQELGEDAVAELERIEATADSAVERVTALEEAVDAIGDVTGVITDIAEQTNMLALNANIEAARADKSGDGFAVVADEVKDLADEVKESATEIETLVDDVQADVADTVADMSELGDRVDAGSETIEAALAALDDIGDQVEAANGSVQSISDATDEQAASTEEVVTMIDEVTDLSDRTATESQQVSAAAEEQAASVSEVAGRADDLDDQVSTLNDLLDQFDARAASADTDEN
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Mediates chemotaxis towards five attractant amino acids (leucine, isoleucine, valine, methionine and cysteine). Probably transduces the signal from the substrate-binding protein BasB to the histidine kinase CheA.
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B0R8E4
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CSG_HALS3
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Cell surface glycoprotein (S-layer glycoprotein)
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MTDTTGKLRAVLLTALMVGSVIGAGVAFTGGAAAANASDLNDYQRFNENTNYTYSTASEDGKTEGSVASGATIFQGEEDVTFRKLDNEKEVSPATLSRTGGSDEGVPLQMPIPEDQSTGSYDSNGPDNDEADFGVTVQSPSVTMLEVRNNADNDVTGGVLNTQQDESSIAVDYNYYAAEDLELTVEDEDGLDVTDEILAADQSGGAYEDGTGNNGPNTLRFDIDPNNVDAGDYTVSVEGVEDLDFGDATESASVTISSSNKASLNLAEDEVVQGANLKYTIENSPEGNYHAVTIDSSDFRDSSSGADAAKVMRSVGDTVDTGLVVDNDSTTEIVDDYENTSISDVDYAYAIVEIDDGNGVGSIETQYLDDSSADIDLYPASDTEDAPDYVNSNEELTNGSALDGVSTDDDTDFDVTQGDITLDNPTGAYVVGSEVDINGTANEGTDDVVLYARDNNDFELVTVDGEKSIEVDSDDTFEEEDITLSDGDKGGDDILGLPGTYRLGIIAKSDAVNSSGGVKDNIDTSDFNQGVSSTSSIRVTDTELTASFETYNGQVADDDNQIDVEGTAPGKDNVAAIIIGSRGKVKFQSISVDSDDTFDEEDIDISELRQGSASAHILSSGRDGKFGEDTANSISDLEDEVGNYTSGSPTGDQIRDRILSNTVDDTASDDLIVTQQFRLVDGLTTIEATEGGEAGGSLTVMGTTNRKADDNTITVELLQGDASIEINSTDEWNSDGQWSVDVPLSNVEPGNYTVEADDGDNTDRQNVEIVEELEEPDQTTVDQPENNQTMTTTMTETTTETTTEMTTTQENTTENGSEGTSDGESGGSIPGFGVGVALVAVLGAALLALRQN
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S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.
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B0RP51
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PFP_XANCB
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Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (EC 2.7.1.90) (6-phosphofructokinase, pyrophosphate dependent) (PPi-dependent phosphofructokinase) (PPi-PFK) (Pyrophosphate-dependent 6-phosphofructose-1-kinase)
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MTNGNLLYAQSGGVTAVINATAAGVIGEARARKIKVLAARNGILGALREELIDTSKESAAAIAALAQTPGGAFGSCRYKLKSLEQDRAKYERLLEVLRAHDVRWFLYNGGNDSADTALKVSQLAKAFGYPLHCIGVPKTIDNDLAVTDTCPGFGSAAKYTAVSVREAALDVAAMADTSTKVFIYEAMGRHAGWLAAAAGLAGQGPDDAPQIILLPERAFDQAAFLAKVRQMVERVGWCVVVASEGIQDAQGKFVADAGGATDSFGHAQLGGVASFLAAQVKQELGYKVHWTLPDYLQRSARHLASKTDWEQAQAVGKAAVQYALKGMNAVIPVIERVSDAPYRWKIVPAPLHKVANHEKKMPPSFLRKDGFGITERARRYFAPLIKGEAPLAYGSDGLPKYVSLKNVAVAKKLPAWEG
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Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. {ECO:0000255|HAMAP-Rule:MF_01978, ECO:0000269|PubMed:24508689}.
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B0S5G3
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CSTN2_DANRE
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calsyntenin-2
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MKMRAITAMLLLVLSGQCGILAGKVNKHKPWIETSYHGVITENMDTVMLDPPLVALDKDAPVPYAGEICAFKIHGQEAPFEAEVLNRTSGEGVLRARGPIDCEQQKEYTFIIQAYDCGASPNGADWKKSHKAVVHIQVDDVNEFSPVFREPLYRATVTEGKIYDSILQVEAWDQDCSPQYSQICNYEIVTQDTPFAIDRNGNIRNTERLSFDKQQHYKIMVTAYDCGQKRAMESVPVHIDVKPVCKPGWQGWNKRVDYEPGTGSKQLFPKMHLETCDGPLSSVRAMVELQTSHIGKGCDRETYSEKSLQKLCGAASGSTDLLPAPSTSTNWTASLLTDSGRDSDLIFRFDGRQAANIPDWVVPQNLTDQFTIATWMKHGPSPGLRAEKETLLCNSDKTEMNRHHYSLYVHNCRLVFLLRRDFIQLDSFRPAEFHWRLEQICDKEWHYYVINVEFPSVTLFVDGVTYEPYLVTDDWPIHPSEIDVQLTVGACWQGGEVTTPRFTQYFRGSLSGLTIRPGKIATQKVISCLQACKEGLDISSLESLGKGIKFHFNPAQSVLVMEADDLESINTAMTKVSYINSRQFPTPGLRKLHITTTVQCFGEDTCISIPEIKAMVMVLPPSEPRITIAGVERLVWPSAQLRAPVGVALFKDIHIISTVTKTDATLSIARRPGVLELMHNLDYCDVLVIGEELDPERESLEIHHSSLLGKHLDATNSTSGISIYGVDSMAHYEQAIRQVRYRNWKPGSLSERRFRLSCSELNGRYTSNEFNLEIGVVHSSEAVEHVNHMAVQSQFMRPVHHPLVVHTVNSDHISGTPPAATVVIVMCIAALVVIVVLGIYRIHTTHQDSSKEDEEERKDPEMDWDNSNLNSIEGTQIAEEVREEEPEEDEDEDEEDDDLAGDLSSAESEDSDEDEETNIQKGKVKGKLEWDPSTLPY
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Postsynaptic adhesion molecule. Promotes synapse development by acting as a cell adhesion molecule at the postsynaptic membrane, which associates with presynaptic neurexins (By similarity).
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B0S5N4
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PLXA3_DANRE
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Plexin A3
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MRSLWLLVFSFSVLTGTNMAFPMILSERPEVTGSFKVKDTSLTHLTVHRKTGEVFVGAINRVYKLSANLTETRSHQTGPVEDNAKCYPPPSVRACTQKLESTDNVNKLLLVDYAGNRLVACGSIWQGVCQFLRLEDLFKLGEPHHRKEHYLSGAKESDGMAGVVVGDDDGDLKKKKKGGSRLFIGAAIDGKSEYFPTLSSRKLVADEESVNMFSLVYQDEFVSSQIKIPSDTLSQYPAFDIYYVYGFSSRTYIYFLTLQLDTQLTQVDVTGEKFFTSKIVRMCSNDTEFYSYVEFPLGCTKDGVEYRLVQAAYKHRPGKILAQALGLSEDEDVLFVIFSQGQKNRANPPRETVLCLFTLHQINLAMRERIKSCYRGEGKLSLPWLLNKELPCINTPKQIGDDFCGLVLNQPLGGLMVIEGIPLFDDRTDGMASVAAYTYGDHSVVFVGTRSGHLKKIRVNGVPPPSENALLYETVTVVEGSPILRDMVFSPDYQYIYLLSDKQVSRLPVESCSQYSSCKTCLGSGDPHCGWCVLHNKCSRKEACEKWAEPLHFSTELKQCVDITVTPDNMSVTSVSTQLSVKVANVPNLSAGVTCVFEELTESPGEVLAEGQILCMSPSLRDVPSVTQGYGDKRVVKLSLKSKETGLKFITTDFVFYNCSVLQSCSSCVSSPFPCNWCKYRHICTNNVAECSFQEGRVSSAEGCPQILPSSDILVPAGIVRPITLRARNLPQPQSGQKNYECVFNIQGKVQRIPAVRFNSSCIQCQNTSYWYEGNEMGDLPVDFSIVWDGDFPIDKPSSMRALLYKCEAQRDSCGLCLKADSTFECGWCLADKKCLLKQHCPSAEHNWMHQGRRNIRCSHPRITKIRPLTGPKEGGTRVTIEGENLGLQVREITHVRVAGVRCNPAAAEYISAERIVCDMEESLMSSPPGGPVELCIGDCSAEYRTQSTQTYSFVMPSFSRVRPEKGPVSGGTRLTISGRHLDAGSAVTVFLAQEECLFVRRTVREIVCVTPPSASGSGPSSVKLFIDKAEITSDTRYIYTEDPNISTIEPNWSIINGSTSLTVTGTNLLTIQEPKVRAKYGGVETTNICSLVNDSVMTCLAPGIIYTKREAPESGVHPDEFGFILDHVSALLILNGTPFTYYPNPTFEPLGNAGILEVKPGSPIILKGKNLIPPAPGNIRLNYSVTIGETPCLLTVSESQLLCDSPDLTGEQRVMILVGGLEYSPGMLHIYSDSTLTLPAIIGIGAGGGVLLIAIIAVLIAYKRKTRDADRTLKRLQLQMDNLESRVALECKEAFAELQTDIQELTNDMDGVKIPFLEYRTYTMRVMFPGIEEHPVLKELDSPANVEKALRLFSQLLHNKMFLLTFIHTLEAQRSFSMRDRGNVASLLMAALQGRMEYATVVLKQLLADLIEKNLENRNHPKLLLRRTESVAEKMLTNWFTFLLHRFLKECAGEPLFMLYCAIKQQMEKGPIDAITGEARYSLSEDKLIRQQIDYKQLTLMCIPPEGEAGTEIPVKVLNCDTITQVKDKLLDAVYKGIPYSQRPQADDMDLEWRQGRLTRIILQDEDVTTKIESDWKRLNTLAHYQVTDGSLVALVQKQVSAYNIANSFTFTRSLSRYESLLRTSSSPDSLRSRAPMITPDQETGTKLWHLVKNHEHADQREGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETVFSTAHRGSALPLAIKYMFDFLDEQADKRQITDPDVRHTWKSNCLPLRFWVNVIKNPQFVFDIHKNSITDACLSVVAQTFMDSCSTSEHRLGKDSPSNKLLYAKDIPNYKSWVERYYRDISKMPSISDQDMDAYLVEQSRLHGNEFNTLSALSELYFYINKYKEEILTALDRDGYCRKHKLRHKLEQAINLMSGSS
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Coreceptor for class 3 semaphorins. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance in the developing nervous system. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm.
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B0S6J3
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SRGP2_DANRE
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SLIT-ROBO Rho GTPase-activating protein 2 (srGAP2)
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MTSPAKFRKDKEIIAEYETQVKEIRAQLVEQLKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRYTKDPQFKKEQNILSPVNCWNLLLAQVKRESRDHATLSDLYLNNIIPRFAQISEDSGRLFKKSKEVGLQLQEDLMKVLNELYTVMKTYHMYNMDSINAESKLKEAEKQEEKQMSRSVRHEEKQTPRSPDSLTNIKIEDKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNSCVFKYYIHDLSDLIDCCDLGYHASLNRALRTYLSAEFNVETSKHGGLETIENAAENLEANSDKQRLMETYNNVFCPPMRFDFQSHMGDMVGHLCAQQPVQGELIQRCQQLQSRLSTLNIENEEVKKTMEATLQTIQDMVTIEDFDVTDCFHHSNSMESVKSTVSESFMSKPSLAKRRANQQETEQFYFTKLKEFLEGRNLITKLQAKHDLIQKTLGESQKTDYCLASGRRDSTVRKQEAIQIIPLMVESCIRFISRHGLHHEGIFRVSGSQVEVNDIKNAFERGEDPLAGDQNDHDMDSIAGVLKLYFRGLENALFPKEVFHDLMSCVSIESLQERAVHIRKVLLSLPSNILVIMRYLFAFLNHLSQYSDDNMMDPYNLAICFGPTLMSVPEGHDQVSCQAHVNELIKTIIIHHESIFPGPRELEGPVYDRGGAPEEYCDSPHIEPPLVDEPAPDTVSVIHNSDDVKSGPLTVSESDPIEAIARFDYSGRTNRELSFKKGASLLLYSRASDDWWEGRHNGTEGLVPHQYIVVQDMPDGYAGRGSPKADLEGSHDSVEEKVSTRASASSPTGGHVADIYLANLNKLRKRPEATSIRRTIRPVEEGSSGAAGGLKTSSMPAGGLAKDSSDKRPVSAHSVLNSITRHSSLKTKVEGPQVRKSTPTGRSKSFSNHRPLDPEVIAQVEHSSQDIEATMNTALSELRELERQSNVKHAPDVVLDTLEQLKSGGTSEPSSPLHSRLLREAESSQHPLQRSASSASDMPSTFRPSKTTGPKSPLSSMTTASGSTFRDNKPPATRPKPVVFPKSSSAGGSPAMGSPTTTIPPTPPPPPPPTDKSCPV
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Postsynaptic RAC1 GTPase activating protein (GAP) that plays a key role in neuronal morphogenesis and migration mainly during development of the cerebral cortex. Regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons. Mechanistically, acts by binding and deforming membranes, thereby regulating actin dynamics to regulate cell migration and differentiation.
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B0S6T2
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S15A2_DANRE
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Solute carrier family 15 member 2 (Peptide transporter 2) (PEPT2)
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MGKMKDKDVDAEKYEKAQRSPKLCGTNYPVSIAFIVVNEFCERFSYYGMKAVLTLYFMNYLHWDKNLSTAIYHAFSGLCYFTPLLGALIADSWLGKFKTIIYLSIVYVIGHVVKSVGAIPDVGDSTVHIALSMVGLGLIALGTGGIKPCVAAFGGDQFDEDNIDERRKFFSIFYMSINAGSVLSTIITPILRGDVQCFGGDCYALAFGVPAALMVIALVVFISGSGLYKKSPPEGNVLVRVCKCIGFAISNRWTNSKKSPKRSHWLDWAEEKYSKRLIQEIKMVCRVLVLYIPLPMFWALFDQQGSRWTLQATRMNMDFGGGFIIKPDQMQMLNALLILVFIPIFDMGIYPLVGLCRIKLTPLKKMATGMILAALAFCAATAVEVYVIKTVVEPPPAKESLVQVYNLMDSDVTVQFPAHNVFSEPLKPYEEPSGYSSLPLTGESQLQNVVVSHNGMNYQCRLTFTERMAYSLLLHPTAQHNGSVCNLVKDHITKSETGAAYIRFINTHTENINVTVGTEEVHASANYGISRNISVPRGEYNKAVCVTDTKEYEINLGLLDFGAFYTVILSEAGNNLAVKKMEDIQANNIHIGWQIPQYVFLTAGEVMFSITGLEFSYSQAPASMKSVLQAGWLMTVAFGNVIVLIVAEGAGMEQWVEFLLFAALLVAVSIIFSIMAYFYTYVDPDQLDKLFKEDGDGGKVESSKKDELSLGDMPKQTKM
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Proton-coupled amino-acid transporter that transports oligopeptides of 2 to 4 amino acids with a preference for dipeptides. Transports neutral and anionic dipeptides with a proton to peptide stoichiometry of 2:1 or 3:1 (By similarity).
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B0TLB9
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FADB_SHEHH
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MIYQSPTIEVELLEDNIAHLCFKAQGSVNKFDRETIDSLNAALDSIKQDTSIKALMLSSAKDAFIVGADITEFLGLFAEEDAVLQSWLEQANVVFNKLEDLPFPTLSAINGFALGAGCETILATDFRIADTTARIGLPETKLGIIPGFGGTVRLPRVIGADNALEWITSGKDQRPDAALKVGAIDAVVAPEQLRPAALRMLKDAMAEKLDWQTRRAKKLAPLTLPKLEAMMSFATAKGMVFKIAGKHYPAPMAVISVIEQAAQCGRAEALQIEHQAFIKLAKTEVAQALIGIFLNDQLVKGKAKKAGKLAKKVNSAAVLGAGIMGGGIAYQSASKGTPIVMKDIAQPALDLGLGEAAKLLTAQVKRGRSTPAKMATVLNNITPALDYAPVKDTDIIVEAVVEHPKVKSMVLAEVEEHVSEDAIITSNTSTISINLLAKSLKKPERFCGMHFFNPVHKMPLVEVIRGENSSDETVASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSGLLADGADFAAIDKVMEKQFGWPMGPAYLLDVVGLDTGHHAQAVMAEGFPDRMGKSGKDAIDVMFEAERFGQKNNKGFYQYSVDHRGKPKKDLDPTSYELLQAEFGEQKAFESDEIIARTMIPMIIETVRCLEEGIIASPAEADMGLVYGLGFPPFRGGVFRYLDTIGVANFVALADKYAHLGGLYQVTDTMRELAANNGSYYQQA
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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B0V1P1
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MC4R_DANRE
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Melanocortin receptor 4 (MC4-R)
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MNTSHHHGLHHSFRNHSQGALPVGKPSHGDRGSASGCYEQLLISTEIFLTLGLVSLLENILVIAAIVKNKNLHSPMYFFICSLAVADLLVSVSNASETVVMALITGGNLTNRESIIKNMDNVFDSMICSSLLASIWSLLAIAVDRYITIFYALRYHNIMTQRRAGTIITCIWTFCTVSGVLFIVYSESTTVLICLISMFFTMLALMASLYVHMFLLARLHMKRIAALPGNGPIWQAANMKGAITITILLGVFVVCWAPFFLHLILMISCPRNPYCVCFMSHFNMYLILIMCNSVIDPLIYAFRSQEMRKTFKEICCCWYGLASLCV
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Receptor specific to the heptapeptide core common to adrenocorticotropic hormone and alpha-, beta-, and gamma-MSH. Plays a central role in energy homeostasis and somatic growth. This receptor is mediated by G proteins that stimulate adenylate cyclase (cAMP).
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B0V2N1
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PTPRS_MOUSE
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Receptor-type tyrosine-protein phosphatase S (R-PTP-S) (EC 3.1.3.48) (PTPNU-3) (Receptor-type tyrosine-protein phosphatase sigma) (R-PTP-sigma)
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MAPTWSPSVVSVVGPVGLFLVLLARGCLAEEPPRFIREPKDQIGVSGGVASFVCQATGDPKPRVTWNKKGKKVNSQRFETIDFDESSGAVLRIQPLRTPRDENVYECVAQNSVGEITIHAKLTVLREDQLPPGFPNIDMGPQLKVVERTRTATMLCAASGNPDPEITWFKDFLPVDPSASNGRIKQLRSGALQIESSEETDQGKYECVATNSAGVRYSSPANLYVRVRRVAPRFSILPMSHEIMPGGNVNITCVAVGSPMPYVKWMQGAEDLTPEDDMPVGRNVLELTDVKDSANYTCVAMSSLGVIEAVAQITVKSLPKAPGTPVVTENTATSITVTWDSGNPDPVSYYVIEYKSKSQDGPYQIKEDITTTRYSIGGLSPNSEYEIWVSAVNSIGQGPPSESVVTRTGEQAPASAPRNVQARMLSATTMIVQWEEPVEPNGLIRGYRVYYTMEPEHPVGNWQKHNVDDSLLTTVGSLLEDETYTVRVLAFTSVGDGPLSDPIQVKTQQGVPGQPMNLRAEAKSETSIGLSWSAPRQESVIKYELLFREGDRGREVGRTFDPTTAFVVEDLKPNTEYAFRLAARSPQGLGAFTAVVRQRTLQAKPSAPPQDVKCTSLRSTAILVSWRPPPPETHNGALVGYSVRYRPLGSEDPDPKEVNNIPPTTTQILLEALEKWTEYRVTAVAYTEVGPGPESSPVVVRTDEDVPSAPPRKVEAEALNATAIRVLWRSPTPGRQHGQIRGYQVHYVRMEGAEARGPPRIKDIMLADAQEMVITNLQPETAYSITVAAYTMKGDGARSKPKVVVTKGAVLGRPTLSVQQTPEGSLLARWEPPADAAEDPVLGYRLQFGREDAAPATLELAAWERRFAAPAHKGATYVFRLAARGRAGLGEEAAAALSIPEDAPRGFPQILGAAGNVSAGSVLLRWLPPVPAERNGAIIKYTVSVREAGAPGPATETELAAAAQPGAETALTLRGLRPETAYELRVRAHTRRGPGPFSPPLRYRLARDPVSPKNFKVKMIMKTSVLLSWEFPDNYNSPTPYKIQYNGLTLDVDGRTTKKLITHLKPHTFYNFVLTNRGSSLGGLQQTVTARTAFNMLSGKPSVAPKPDNDGFIVVYLPDGQSPVTVQNYFIVMVPLRKSRGGQFPVLLGSPEDMDLEELIQDISRLQRRSLRHSRQLEVPRPYIAARFSILPAVFHPGNQKQYGGFDNRGLEPGHRYVLFVLAVLQKNEPTFAASPFSDPFQLDNPDPQPIVDGEEGLIWVIGPVLAVVFIICIVIAILLYKNKPDSKRKDSEPRTKCLLNNADLAPHHPKDPVEMRRINFQTPGMLSHPPIPITDMAEHMERLKANDSLKLSQEYESIDPGQQFTWEHSNLEANKPKNRYANVIAYDHSRVILQPLEGIMGSDYINANYVDGYRRQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTRLEEKSRIKCDQYWPNRGTETYGFIQVTLLDTMELATFCVRTFSLHKNGSSEKREVRHFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKTEKTVDVYGHVTLMRSQRNYMVQTEDQYGFIHEALLEAVGCGNTEVPARSLYTYIQKLAQVEPGEHVTGMELEFKRLASSKAHTSRFITASLPCNKFKNRLVNILPYESSRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRALWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGAPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKVLRTQRPAMVQTEDEYQFCFQAALEYLGSFDHYAT
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Cell surface receptor that binds to glycosaminoglycans, including chondroitin sulfate proteoglycans and heparan sulfate proteoglycans. Binding to chondroitin sulfate and heparan sulfate proteoglycans has opposite effects on PTPRS oligomerization and regulation of neurite outgrowth. Contributes to the inhibition of neurite and axonal outgrowth by chondroitin sulfate proteoglycans, also after nerve transection. Plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. Required for normal brain development, especially for normal development of the pituitary gland and the olfactory bulb. Functions as tyrosine phosphatase. Mediates dephosphorylation of NTRK1, NTRK2 and NTRK3 (By similarity). Plays a role in down-regulation of signaling cascades that lead to the activation of Akt and MAP kinases. Down-regulates TLR9-mediated activation of NF-kappa-B, as well as production of TNF, interferon alpha and interferon beta.
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B0XMC1
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ER10A_ASPFC
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Acetyl-CoA acetyltransferase erg10A, mitochondrial (EC 2.3.1.9) (Acetoacetyl-CoA thiolase erg10A) (Ergosterol biosynthesis protein 10A)
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MAIQTTTGLAARLVAKRATFPASRRNFSASRSALKEIQEAYILSGARTPTAKFNGSFVSVSAPELGAVAIKSAVSKSGVPVEKITDVYMGNVLQGAVGQAPARQASMFAGLSPTVESMTVNKVCASGLKAVALAAQNIQLGLAEAQVAGGMENMSRVPYYLPRSTQLPPFGEIKLQDGLIQDGLWDVYNQFHMGICAEKTAKKYEISREEQDQYAIQSYQRAQAAWKENKFAEEIAPVTVKGKKGETVVERDEGYENLRIDKMATLKPAFLRDGTGTVTAGNASTMNDGASALVLGSKAIAREFAQGNRALARIVSTADAAIDPVDFPVAPAKAVPIALERAGITKDQVAVWEFNEAFAAVIKANEKILGLQNARVNPLGGAISLGHALGSSGSRILVTLLHQLQPGEYGVAAICNGGGAATAMVVQKLDRVD
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Mitochondrial acetyl-CoA acetyltransferase that catalyzes both the formation and degradation of acetoacetyl-CoA. Has no overlapping function with erg10B and seems not to be involved in ergosterol biosynthesis. Plays an important role in growth, morphogenesis and maintaining mitochondrial function including the response to oxidative stresses.
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B0XRM8
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ARO1_ASPFC
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Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
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MTGPTKISILGQESIVADFGLWRNYVAKDLISGCPSTTYVLITDTNIGSIYTPGFQKSFEEAAASVSPSPRLLIYNAPPGEVSKSRQTKADIEDWMLSQSPPCGRDTVVIALGGGVIGDLTGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPSRIYIDLEFLETLPVREFINGMAEVIKTAAISSEEEFTALEDNAETILSAVRREVKPGQRRFEGIEEILKARILASARHKAFVVSADEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELARHLGILKGVAVARIVKCIAAYGLPTSLKDSRIRKLTAGKHCSVDQILFNMALDKKNDGPKKKIVLLSAIGRTYEPRASVVPNEDIGVVLAPSIEVHPGVSTTSEVVCAPPGSKSISNRALVLAALGSGTVRIKNLLHSDDTEVMLNALERLGAATFSWEEEGEVLVVNGKGGALQAHPSPLYLGNAGTASRFLTTVATLATASSVDSSVLTGNNRMKQRPIGDLVDALTANGAQIEYVENKGSLPLKIAASGGFTGGQINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGKPISQPYIDMTTAMMRSFGIDVKKSTTEEHTYHIPQGRYINPAEYVVESDASSATYPLAIAAVTGTTCTIPNIGSKSLQGDARFAVDVLRPMGCTVEQTDTSTTVTGPADGVLRPLPNVDMEPMTDAFLGASVLAAIARGKDSNHTTRIYGIANQRVKECNRIKAMHDELAKFGVVCREHDDGLEIDGIDRSTLRQPAGGVFCYDDHRVAFSFSVLSLIAPKPTLILEKECVGKTWPGWWDTLRQKFAVKLEGKELKEAESPVLTRAEKASASVFIIGMRGAGKTTSGHWVASTLKRPFIDLDDELERIEGMTIPDIIKQRGWQGFRDAELNLLQRTMKERPTGHVFACGGGVVEIPEARKLLIDWHKTKGNVLLIMRDIKQVMAFLNIDKTRPAYVEDMLGVWLRRKPWFQECSNIQYYSQHASAGLPRASEDFARFIKFVTGLEDSLGTIKKKQHSFFVSLTLPDVRGADQILEQACVGSDAVELRVDLLEDPDSSNGIPTVDFVADQISYLRSRITLPVIFTIRTKGQGGRFPDDAHAEAMQLYRLAVRSGCEFVDLEIAFPDEMLRAVTEMKGYSKIIASHHDPNGELSWANMSWMKYYNRALEYGDVIKLVGVARNLDDNTALRKFKNWAEEAHDVPLIAINMGGNGQLSRILNGFMTPVSHPALPFRAAPGQLSATDIRKGLSLMGEIKKKRFALFGSPISESRSPALHNTLFAEMGLPHEYTRLETANVEDVKDFIRAPDFGGASVTIPLKLDIMPLLDEITAEAEIIGAVNTVVPVSDGEGKPQRLVGHNTDWQGMVQCLRNAGAYGADGSASALVVGGGGTSRAAIYALHQMGFSPIYIVGRNPAKLESMVSTFPTSYNIQIVEGNEKLEHVPHVAIGTIPADRPIDPGMREILCHMFERAQEADADASRTIEGSPRVLLEMAYKPRVTALMQLAVDAGWTTIPGLEALIGQGVHQVGLIDLLQMDITDGVQFQHWTGIRPLYERARVCCDILLSGRTMLTCS
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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B0XT72
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GEL1_ASPFC
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1,3-beta-glucanosyltransferase gel1 (EC 2.4.1.-) (Glucan elongating glucanosyltransferase 1)
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MKASAVTAALAVGASTVLAAPSIKARDDVTPITVKGNAFFKGDERFYIRGVDYQPGGSSDLADPIADADGCKRDIAKFKELGLNTIRVYSVDNSKNHDECMNALADAGIYLVLDVNTPKYSINRAKPKESYNDVYLQYIFATVDAFAGYKNTLAFFSGNEVINDGPSSSAAPYVKAVTRDLRQYIRSRKYREIPVGYSAADIDTNRLQMAQYMNCGSDDERSDFFAFNDYSWCDPSSFKTSGWDQKVKNFTGYGLPLFLSEYGCNTNKRQFQEVSSLYSTDMTGVYSGGLVYEYSQEASNYGLVEISGNNVKELPDFDALKTAFEKTSNPSGDGNYNKTGGANPCPAKDAPNWDVDNDALPAIPEPAKKYMTEGAGKGPGFAGPGSQDRGTQSTATAEPGSGSATGSSSSGTSTSSKGAAAGLTVPSLTMAPVVVGAVTLLSTVFGAGLVLL
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Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall morphogenesis.
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B0Y0P7
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UBA4_ASPFC
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Adenylyltransferase and sulfurtransferase uba4 (Common component for nitrate reductase and xanthine dehydrogenase protein F) (Ubiquitin-like protein activator 4) [Includes: Molybdopterin-synthase adenylyltransferase (EC 2.7.7.80) (Adenylyltransferase uba4) (Sulfur carrier protein MOCS2A adenylyltransferase); Molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) (Sulfur carrier protein MOCS2A sulfurtransferase) (Sulfurtransferase uba4)]
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MENLEQTCASLRAQIAATEAQLAGLKRELEIAEQAAEVKAQSTTRTITAEDGKTNETREWPLLSEEYKRYGRQMIVPQLGLQGQLKLRAARVLIVGAGGLGCPAALYLAGAGVGTLGLVDGDTVENSNLHRQVLHSSKNVGTFKVDSAIEYLRELNPHPTYVPYRAHLTPQEAPGIFKDYDIVLDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLMVLNYPPRPVGDKSGGPCYRCVFPKPPPANSVVSCADGGILGPVVGTMGVLQALEAIKVITSPAVNPSASPPSLLIFSAYSTPLFRTIRLRARRANCAVCSADASVTLETLKNGSTDYVFFCGVAGLEATLSPEERISPLEFKKRHPKEVPQDGGRINKEPTIIDVREKVQFDICSLENSINIPISTILSSASSPTNVDANAQPSLPFWLPRELASADSTDPIYVVCRHGNDSQIAVRRLKELGLDRGGQRYVGDIQGGLRAWREQIDPDWPEY
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Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards urm1 and mocs2a. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor nfs1 probably acting as a sulfur donor for thiocarboxylation reactions (By similarity).
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B0Y3B5
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SKP1_ASPFC
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E3 ubiquitin ligase complex SCF subunit sconC (Sulfur controller C) (Sulfur metabolite repression control protein C)
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MTTVTLTSSDGVDITVDRDVAERSILIKNMLEDLGESDEAIPIPNVNEVVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKALLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEE
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Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor (By similarity).
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B0Y4X4
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MPKA_ASPFC
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Mitogen-activated protein kinase mpkA (MAPK mpkA) (EC 2.7.11.24)
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MSDLQGRKVFKVFNQDFIVDERYNVTKELGQGAYGIVCAATNVHTGEGVAIKKVTNVFSKKILAKRALREIKLLQHFRGHRNITCLYDMDIPRPDNFNETYLYEELMECDLAAIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSIDPEENAGYMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGGRPFFKGRDYVDQLNQILHYLGTPNEETLSRIGSPRAQEYVRNLPFMPKIPFQRLFPNANPDALDLLDRMLAFDPASRISVEEALEHPYLHIWHDASDEPTCPTTFDFHFEVVDDVQEMRKMIYDEVVRFRNLVRQQSQAQAAAAAQQQQQQIAQQTNVPIPDHQQGGWKQEEPKPQEVHAAGGHVNDLESSLQRGMDVQ
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Mitogen-activated kinase (MAPK), part of the cell wall integrity (CWI) signaling pathway composed by three protein kinases bck1, mkk2 and mpkA and responsible for the maintaining of cell-wall integrity balance. The CWI pathway regulates also the oxidative stress response, as well as the production of some secondary metabolites including gliotoxin, pyomelanin, pseurotin A, fumiquinazoline C or dihydroxynaphthalene (DHN)-melanin. MpkA directly phosphorylates the fumiquinazoline C biosynthesis cluster nonribosomal peptide synthetase fmqC during conidiation. Mpka is also required for adaptation to iron starvation and regulates the expression of genes involved in siderophore biosynthesis in a hapX/sreA-independent manner.
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B0YA65
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ER10B_ASPFC
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Acetyl-CoA acetyltransferase erg10B, cytosolic (EC 2.3.1.9) (Acetoacetyl-CoA thiolase erg10B) (ACAT) (Cytosolic thiolase erg10B) (CT) (Ergosterol biosynthesis protein 10B)
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MSSLPAVYIVSSARTPVGSFLGSLSSLTAPQLGAHAIKAALAKVDGLKPSDVQEVFFGNVISANVGQNPARQCALGAGLEESTICTTVNKVCASGLKAIILGAQTIMTGNADVVVAGGTESMSNAPHYLPNLRTGAKYGHQSLVDGIMKDGLTDAGKQELMGLQAEECAQDHGFSREQQDEYAIRTYEKAQAAQKAGLFDEEIAPIQLPGFRGKPDVTVTQDEEPKNLNPEKLRAIKPAFIPGSGTVTAPNSSPLNDGAAAVVLVSEAKLKELNLKPVAKILGWGDAAQQPSKFTTAPALAIPKALKHAGVGQDAIDAFEINEAFSVVALANMKLLGIPEEKVNLHGGAVAIGHPIGASGARILTTLLGVLKAKKGKLGCAGICNGGGGASALVVELL
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Acetyl-CoA acetyltransferase part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (Probable). In this module, the cytosolic acetyl-CoA acetyltransferase erg10B catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases AFUA_8G07210 and AFUA_3G10660 then condense acetyl-CoA with acetoacetyl-CoA to form HMG-CoA (Probable). The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hmg1 and hmg2. Mevalonate is also a precursor for the extracellular siderophore triacetylfusarinine C (TAFC).
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B0YJ81
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HACD1_HUMAN
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Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 1 (EC 4.2.1.134) (3-hydroxyacyl-CoA dehydratase 1) (HACD1) (Cementum-attachment protein) (CAP) (Protein-tyrosine phosphatase-like member A)
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MGRLTEAAAAGSGSRAAGWAGSPPTLLPLSPTSPRCAATMASSDEDGTNGGASEAGEDREAPGERRRLGVLATAWLTFYDIAMTAGWLVLAIAMVRFYMEKGTHRGLYKSIQKTLKFFQTFALLEIVHCLIGIVPTSVIVTGVQVSSRIFMVWLITHSIKPIQNEESVVLFLVAWTVTEITRYSFYTFSLLDHLPYFIKWARYNFFIILYPVGVAGELLTIYAALPHVKKTGMFSIRLPNKYNVSFDYYYFLLITMASYIPLFPQLYFHMLRQRRKVLHGEVIVEKDD
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[Isoform 1]: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. [Isoform 2]: In tooth development, may play a role in the recruitment and the differentiation of cells that contribute to cementum formation. May also bind hydroxyapatite and regulate its crystal nucleation to form cementum.
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B0ZB55
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OMT1_HUMLU
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Desmethylxanthohumol 6'-O-methyltransferase (EC 2.1.1.338) (O-methyltransferase 1) (HlOMT1)
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MESLRGQEQIWQLMFSFVDSMALKCAIELRIADIIHSHGKPITLSQIASGIRSNSNSSISPNIPYLSRIMRFLVRKNIFTEHQEDNDEVISLYGLSDSSRWLLRDFKSSLAPMVLMQTHPLSMAVWHFLEDYVRNSSNTFEKAHGCNIWEFSSANPDFNKIFNNAMASIVPIYMGAVLSSYKDGLGCIKGTVVDVGGGTGGSISELMKYYPNIKGINFDLPHVIATAPALDGVTHISGDIFESIPSADAVLMKGVLHCFSDEKCVKVLRNCRKAITDKKNGKIIILEIVLDPTSNQIFDETRMVYDLLIPLFSGGKERTELEWKRLLNEAGFTSIKITKIPIIPAIIEAFLV
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Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the biosynthesis of xanthohumol. Methylates desmethylxanthohumol and xanthogalenol, but not caffeic acid, prenylflavanones, simple phenols or phenylpropanoids.
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B0ZB56
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OMT2_HUMLU
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Xanthohumol 4-O-methyltransferase (EC 2.1.1.339) (Desmethylxanthohumol 6'-O-methyltransferase) (EC 2.1.1.338) (Isoliquiritigenin 2'-O-methyltransferase) (EC 2.1.1.154) (O-methyltransferase 2) (HlOMT2)
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MELARNDQTEAALRGEANVWKSINGIADFMVMKCALELRIPDIVHSHSAPITLAQIASSVPDSPSLNLSYLSRIMRLLVRRKIFSQHKSLDGEEVLYGPTHSSRLLLSKTTLPDQVTLAPFVAFMTHPYLSAPWSCLARCVKEGGNGFEMVHGGRQLWDLSPGNPEFNKVFNDGMASTARITTMAILSEYRDVFCGICSLVDVGGEFGGSISAIVKSHPHIKGINYDLPHVVATAPTYTGLVSHVGGNMFEWIPTAVAVFMKWILHDWADEDCVKILKNCRRAMPEKGGKIIIVDIVLEPEGNGLFDDAAVMLDIALMALTRGKERTEKEWKRVLEEGGFPRYQILKIPALTSVIEAYPQ
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Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). O-methyltransferase with a low substrate selectivity. Methylates chalconaringenin, desmethylxanthohumol, xanthohumol, isoliquiritigenin, butein, 2',4-dihydroxychalcone, resveratrol, genistein and guaiacol. Catalyzes the biosynthesis of 2',4'-dihydroxy-4,6'-dimethoxy-3'-prenylchalcone (4-O-methylxanthohumol).
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B1A612
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MENC_GEOKU
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o-succinylbenzoate synthase (OSB synthase) (OSBS) (EC 4.2.1.113) (4-(2'-carboxyphenyl)-4-oxybutyric acid synthase) (N-acylamino acid racemase) (NAAAR) (N-succinylamino acid racemase) (NSAAR) (NSAR) (EC 5.1.1.-) (o-succinylbenzoic acid synthase)
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MAINIEYVILRHLQMELKAPFTTSFGTFQTKEFILVEVVDCDGVSGWGESVAFSVPWYSEETVKTNWHMLEEFLVPLLFSKPLRHPAELPERFAAIRQNNMAKAALEGAVWDLYAKRLGVPLCQALGGTKKEIEVGVSIGIQPTVDDLLQVIERYVAQGYRRIKVKIKPGWDVDVIRDVRRAFPDVPLMADANSAYTLADAKRLQALDEFGLMMIEQPLAADDLVDHARLQPLLKTPICLDESIRSYDDARKALDLGSCRIINIKIGRVGGLWEAKRIHDLCAERGVPVWCGGMLEAGVGRAHNIAITTLENFALPGDTAASSHYWERDIITPEVEVHNGLIRVPNAPGIGYDVDRRQVERYTQFAKLFHRTATA
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Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (By similarity). Also acts as a N-succinylamino acid racemase (NSAR) that catalyzes the racemization of various N-succinylamino acids, including N-succinyl-alanine and N-succinyl-phenylalanine (Ref.1). Can catalyze the racemization of a broad range of N-acylamino acids, including N-acetyl-methionine, N-acetyl-phenylalanine, N-carbamoyl-methionine, N-formyl-D-methionine, N-formyl-D-norleucine and N-carbamoyl-D-norleucine (Ref.1, PubMed:25875730). May be a bifunctional enzyme involved in menaquinone biosynthesis and in an irreversible pathway for the conversion of D- to L-amino acids, thereby facilitating the survival and/or growth of the organism (By similarity).
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B1A8Z2
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CIB1_SHEEP
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Calcium and integrin-binding protein 1 (Calmyrin)
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MGGSGSRLSKELLAEYQDLTFLTKQEILLAHRRFCELLPQEHRSVEESLQARVSLEQILSLPELKANPFKERICKVFSTSPSRDSLSFEDFLDLLSVFSDTATPDIKSHYAFRIFDFDDDGTLNREDLSQLVNCLTGESEDTRLSASEMKQLIDNILEESDIDRDGTINLSEFQHVISRSPDFASSFKIVL
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Calcium-binding protein that plays a role in the regulation of numerous cellular processes, such as cell differentiation, cell division, cell proliferation, cell migration, thrombosis, angiogenesis, cardiac hypertrophy and apoptosis. Involved in bone marrow megakaryocyte differentiation by negatively regulating thrombopoietin-mediated signaling pathway. Participates in the endomitotic cell cycle of megakaryocyte, a form of mitosis in which both karyokinesis and cytokinesis are interrupted. Plays a role in integrin signaling by negatively regulating alpha-IIb/beta3 activation in thrombin-stimulated megakaryocytes preventing platelet aggregation. Up-regulates PTK2/FAK1 activity, and is also needed for the recruitment of PTK2/FAK1 to focal adhesions it thus appears to play an important role in focal adhesion formation. Positively regulates cell migration on fibronectin in a CDC42-dependent manner, the effect being negatively regulated by PAK1. Functions as a negative regulator of stress activated MAP kinase (MAPK) signaling pathways. Down-regulates inositol 1,4,5-trisphosphate receptor-dependent calcium signaling. Involved in sphingosine kinase SPHK1 translocation to the plasma membrane in a N-myristoylation-dependent manner preventing TNF-alpha-induced apoptosis. Regulates serine/threonine-protein kinase PLK3 activity for proper completion of cell division progression. Plays a role in microtubule (MT) dynamics during neuronal development disrupts the MT depolymerization activity of STMN2 attenuating NGF-induced neurite outgrowth and the MT reorganization at the edge of lamellipodia. Promotes cardiomyocyte hypertrophy via activation of the calcineurin/NFAT signaling pathway. Stimulates calcineurin PPP3R1 activity by mediating its anchoring to the sarcolemma. In ischemia-induced (pathological or adaptive) angiogenesis, stimulates endothelial cell proliferation, migration and microvessel formation by activating the PAK1 and ERK1/ERK2 signaling pathway. Promotes also cancer cell survival and proliferation. May regulate cell cycle and differentiation of spermatogenic germ cells, and/or differentiation of supporting Sertoli cells (By similarity).
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B1AK53
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ESPN_HUMAN
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Espin (Autosomal recessive deafness type 36 protein) (Ectoplasmic specialization protein)
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MALEQALQAARQGELDVLRSLHAAGLLGPSLRDPLDALPVHHAARAGKLHCLRFLVEEAALPAAARARNGATPAHDASATGHLACLQWLLSQGGCRVQDKDNSGATVLHLAARFGHPEVVNWLLHHGGGDPTAATDMGALPIHYAAAKGDFPSLRLLVEHYPEGVNAQTKNGATPLYLACQEGHLEVTQYLVQECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVSCTDVSLSEQDKDGATAMHFAASRGHTKVLSWLLLHGGEISADLWGGTPLHDAAENGELECCQILVVNGAELDVRDRDGYTAADLSDFNGHSHCTRYLRTVENLSVEHRVLSRDPSAELEAKQPDSGMSSPNTTVSVQPLNFDLSSPTSTLSNYDSCSSSHSSIKGQHPPCGLSSARAADIQSYMDMLNPELGLPRGTIGKPTPPPPPPSFPPPPPPPGTQLPPPPPGYPAPKPPVGPQAADIYMQTKNKLRHVETEALKKELSSCDGHDGLRRQDSSRKPRAFSKQPSTGDYYRQLGRCPGETLAARPGMAHSEEVRARQPARAGCPRLGPAARGSLEGPSAPPQAALLPGNHVPNGCAADPKASRELPPPPPPPPPPLPEAASSPPPAPPLPLESAGPGCGQRRSSSSTGSTKSFNMMSPTGDNSELLAEIKAGKSLKPTPQSKGLTTVFSGIGQPAFQPDSPLPSVSPALSPVRSPTPPAAGFQPLLNGSLVPVPPTTPAPGVQLDVEALIPTHDEQGRPIPEWKRQVMVRKMQLKMQEEEEQRRKEEEEEARLASMPAWRRDLLRKKLEEEREQKRKEEERQKQEELRREKEQSEKLRTLGYDESKLAPWQRQVILKKGDIAKY
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Multifunctional actin-bundling protein. Plays a major role in regulating the organization, dimension, dynamics and signaling capacities of the actin filament-rich microvilli in the mechanosensory and chemosensory cells. Required for the assembly and stabilization of the stereociliary parallel actin bundles. Plays a crucial role in the formation and maintenance of inner ear hair cell stereocilia (By similarity). Involved in the elongation of actin in stereocilia. In extrastriolar hair cells, required for targeting MYO3B to stereocilia tips, and for regulation of stereocilia diameter and staircase formation.
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B1AQJ2
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UBP36_MOUSE
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Ubiquitin carboxyl-terminal hydrolase 36 (EC 3.4.19.12) (Deubiquitinating enzyme 36) (Ubiquitin thioesterase 36) (Ubiquitin-specific-processing protease 36)
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MPIVDKLKEALKPGRKDSAEDGDLGRLLAASAKKVLLQRIEFEPASKSFSYQLESLKSKYVLLSARAEGASRHRSGDELQARKPGTERVSGSGGDGVPAPQKVLFPVERLSLRWERVFRVGAGLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSCHQGGFCMLCLMQNHMVQAFANSGNAIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKACLNGYAKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIALEIRQAANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQSSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYLRIPGSKKSPEGPVSRVGATLPSRPKVVPEHSKKSPGNGVVPSPLMAKRQDSVMMRKLPAPEEVGVPVSRNGSLPGLKLQNGCAPAKTPAGSPSPRLTPTPTHMPTILDEPGKKVKKSAPLQSLTTSPTTSQGSPGTGESRSQRPGSWASRDTIFSTSPKLLARAITNGHRLKGEGSGVDLEKGDSSSSSPEHSASSDPAKAPQTAESRAAHACDSQGTNCPTAGHPKALLNGVDAKMVKLKSPALSSTTTEPTSLMSPPPAKKLALSAKKASTLRRATGNDIGSPSPSAFCDLTSPMKATHPVVASTGPVSKTRTAAPAPRPSTHPHSASLSSSSAKPLGTSEPQSCRPSAWTPLPQVNGHFTSHLHQLPEASEALHSPSKKRKKTPNGDPQRLGIDTLLPQCLRGAPAAARRKRKKRCSEGEGATAPKQEGQFQDQSWSSGSQKEEGTQPQVNGHQVSHILDSYHVSSRKRRKRKRSEGLSQEATPSQDLIQHSCSPVDHSEPEARTELQKKKKKKRRKRKPEPQQDEESKHPGDQRSPRPSVTPVPALSVNGHLPSDCLGLGQAPLVTWNRDQEPDVVQALLQDSSDKAYGKKVLTWDGEPSAISQDAIKDSRLARTQTVVDDWDEEFDRGKEKKIKKFKREKKRNFNAFQKLQSRRNFWSVTHPAKVASLSYRR
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Deubiquitinase essential for the regulation of nucleolar structure and function. Required for cell and organism viability. Plays an important role in ribosomal RNA processing and protein synthesis, which is mediated, at least in part, through deubiquitination of DHX33, NPM1 and FBL, regulating their protein stability. Functions as a transcriptional repressor by deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, such as CDKN1A, thereby preventing histone H3 'Lys-4' trimethylation (H3K4) (By similarity). Specifically deubiquitinates MYC in the nucleolus, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with isoform 3 of FBXW7 (FBW7gamma) in the nucleolus and counteracting ubiquitination of MYC by the SCF(FBW7) complex (By similarity). In contrast, it does not interact with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm (By similarity). Interacts to and regulates the actions of E3 ubiquitin-protein ligase NEDD4L over substrates such as NTRK1, KCNQ2 and KCNQ3, affecting their expression an functions (By similarity). Deubiquitinates SOD2, regulates SOD2 protein stability (By similarity). Deubiquitinase activity is required to control selective autophagy activation by ubiquitinated proteins (By similarity). Promotes CEP63 stabilization through 'Lys-48'-linked deubiquitination leading to increased stability (By similarity).
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B1ARD8
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SLFN8_MOUSE
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Schlafen family member 8 (EC 3.1.-.-) (Schlafen-8) (mSLFN8)
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METHPSLAVKWSCPDLTIYAGEVTIGEEDRNKMDSKKRKLEKTRITEAACALLNSGGGLIAMQMTNKSEHPVEMGQDLEKSLRELIMSPNMQAFFETKQQEDQFYIFVKSWSCRPEDGSTKPRICSLGSSLYCRSITSKVAMDSREAFEFLKDKKACIKYRPTDDGAPPAKIPRAMCQNSLESNPAFEIFQSKKLEYGQCLLFSESTSIEFKQFSTKHVQAYMKNIIPEYISAFANTQGGYLFIGVDDKRIILGCPKDNVDRDSLKTVANETISKVPVFHFCSSKDKDKVSYETRVIDVFQEGNLYGYLCVIKVEPFCCAVFSEAPISWMVDKEKGVYRLNTEEWVRMMVDFGPEASSKDLSKDFECQLSLCNSPPHCRPVYSKKGLQHKVDLQQRLFQVSPDCLKYTPESLWKELCSQHKRLKGLVKQQIRSFSCGLLILYRSWAVDLNLKEKQEVICDALLIAQNSPPILYTILGEQDEQGQDYCNHTAFTLKQKLVNTGGYTGRVCVMTKVLCLSSQNNIETNGGSVSPINYPSSYNLANIQEMQDLLQALVIVLLNFRSFLSDQLGCEILNLLTAQQYEILSKSLRKTRELFVHGLPGSGKTIIAMKIMEKIRNTFHCETDSILYICENQPLRDFIRAKRICQAVTRKTFMNYRFKTNSFQHIIVDEAQNFRTEDGNWYGKAKAISRRVKSCPGMFWIFLDYFQTSHLKESGLPDFSRQYPREELTQVVRNGDKIAEFLQKELQKIRDNPPCSIPRQSLNIVHEFKWSQSVSGNIKTEQFTLEDMVIYVADKCYDFLRKGYSLQDIAVLFSTDKEKKTYESMFLGEMRKRRRASEMNHAYLCDSNMFDSIRRFSGLERSIVFGINPIATEQPISHNLLLCLASRAMKHLYILYFSTPEGHSSTEAC
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Endoribonuclease that cleaves tRNAs and rRNAs. Cleaves tRNAs 11 nucleotides from the 3'-terminus at the acceptor stem. May be involved in immune system via regulation of inflammation.
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B1AS29
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GRIK3_MOUSE
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Glutamate receptor ionotropic, kainate 3 (GluK3) (Glutamate receptor 7) (GluR-7) (GluR7)
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MTAPWRRLRSLVWEYWAGFLVCAFWIPDSRGMPHVIRIGGIFEYADGPNAQVMNAEEHAFRFSANIINRNRTLLPNTTLTYDIQRIHFHDSFEATKKACDQLALGVVAIFGPSQGSCTNAVQSICNALEVPHIQLRWKHHPLDNKDTFYVNLYPDYASLSHAILDLVQSLKWRSATVVYDDSTGLIRLQELIMAPSRYNIRLKIRQLPIDSDDSRPLLKEMKRGREFRIIFDCSHTMAAQILKQAMAMGMMTEYYHFIFTTLDLYALDLEPYRYSGVNLTGFRILNVDNPHVSAIVEKWAMERLQAAPRAESGLLDGVMMTDAALLYDAVHIVSVCYQRAPQMTVNSLQCHRHKAWRFGGRFMNFIKEAQWEGLTGRIVFNKTSGLRTDFDLDIISLKEDGLEKVGVWSPADGLNITEVAKGRGPNVTDSLTNRSLIVTTVLEEPFVMFRKSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDDKGQWNGMVKELIDHKADLAVAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIARFSPYEWYDAHPCNPGSEVVENNFTLLNSFWFGMGSLMQQGSELMPKALSTRIIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVKDGATMTFFKKSKISTFEKMWAFMSSKPSALVKNNEEGIQRTLTADYALLMESTTIEYITQRNCNLTQIGGLIDSKGYGIGTPMGSPYRDKITIAILQLQEEDKLHIMKEKWWRGSGCPEEENKEASALGIQKIGGIFIVLAAGLVLSVLVAVGEFIYKLRKTAEREQRSFCSTVADEIRFSLTCQRRLKHKPQPPMMVKTDAVINMHTFNDRRLPGKDSMSCSTSLAPVFP
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Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds domoate > kainate >> L-glutamate = quisqualate >> AMPA = NMDA (By similarity).
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B1ASB6
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SPOC1_MOUSE
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SPOC domain-containing protein 1
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MPVDKFLARAGGQRTLSRFQDSLCDFLATGSSRSLCGTSLDFPDRVLVCTEGPAGMEEASSPSFRQATTVEGMVSPEDPTLSKEGLSAKGPPPSPVLPPFRRKCRKCGICPQEEEKSGFSLRFGQRPDGDPPECASPEAFAGPPRLLSSKDTEPGEPGGSWVECAVETEVENMLFSKDGVAPDSLDHLFEFPGLFGGEPLSLVTQEPLQSPALYPEVLTEDSTDQQEVQPAFVVGSPGTPPDPVGPEDKAQSGSRMELEQGLSAPANSCASSPEPLGGLDGAPLEQRRPTHVKKRPWTSPDDSSQDHAEGASKKDFPRLEARVPRGVKTVYYVYTGSGIRLVGAASSSQPGQIEPLEELDTNSARRKRRPTTAHPTPCQSDPSETENAEPHQQRAEDPGEQGMTPLDAGVRSTVVRAMQEVLWTRAQELPDLALREDEVEAIAEGIEEALFHLTQDTNLRYKNKYRSLLFNLRDPRNVDLFLKVAHCDVTPNNLVQMSSIQLAPKELSRWRDQEERKGLDIIEQQQKELYRLPASKLTHKGEVEIPRDLDQMLTLEDLMEPIVPRECSLQPLSTPLEDTTNWHQHHQCDSNCQICTGGEEGRKADDGSQPELQVDISYNVDRKSSTKLPAFSGVIMNREENAIQKAPGPAPASSPEVLKVGETPPKEPQDRLQMPAGLKNAPPSPPPWEGSLDMFSIKHFRAKAQLISGHSCQLVQALPDVIRSAGRLPPSHVWDLLDSMGPSKAKDICVIRLCPHGSRDIQNYRLLYSYLNNKQCHCLATVQQVKMVLLPLPAFEPLPARLRPLGGPGLEITHTSLLLAVLFPKDALPDTATSIPVSNKVPKTVSFSKRVERILYSPEDRRSEATSSPLEEDPKQSLARGSLAPRSVCAPQSFPRGRGRQGPGWGQWSPEAAWCYSQHPSSAGPVFPGIGQGQHLHRASCFHHDLLQHLKVLVTMSHQFQASLWPQSQDSLPPSTVVSAVPDPPGPSLGPMDGGGSNCPPPEGSDPLEPPEHEC
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Essential excecutor of PIWIL4-piRNA pathway directed transposon DNA methylation and silencing in the male embryonic germ cells. Associates with the de novo DNA methylation machinery and repressive chromatin remodeling complexes. Tethering of PIWIL4 to a nascent transposable element transcript recruits repressive chromatin remodeling activities and the de novo methylation apparatus through SPOCD1. Not required for piRNA biosynthesis.
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B1ATG9
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TIKI2_MOUSE
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Metalloprotease TIKI2 (EC 3.4.-.-) (Heart, kidney and adipose-enriched transmembrane protein) (TRAB domain-containing protein 2B)
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MHAALAGPLLAALLATARARPQPPDGGQCRPPGSQRDLNSFLWTIRRHPPAYLFGTIHVPYTRVWDFIPDNSKAAFQASTHVYFELDLTDPYTISALASCQLLPHGENLQDVLPRELYWRLKRHLDYVKLMIPSWMTPAQRGKGLYADYLFNAIAGNWERKRPVWVMLMVNSLTETDVRSRGVPVLDLYLAQQAEKMKKSTGAVERVEEQCHPLNGLNFSQVLFALNQTLLQHESVRAGSLQAPYTTEDLIKHYNCGDLNAVIFNHDTSQLPNFINTTLPPHEQVTAQEIDSYFRQELIYKRNERMGKRVMALLQENQDKICFFAFGAGHFLGNNTVIDVLRQAGLEVDHTPAGQAIHGPAAVGSPAPPPEITSPASPAPATPAAAVPEATSATPTTPPEEEDPVLSPHLLLPDSLSQLEEFGRQKWRKRLNKHQRPRQFNDLWVRIEDSTTISPPPLPLQPTPSSETTKPFVKSSHQLQQQDAVGPTSSSAPTLGLLHAITASIVAPFLLHSLGPS
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Metalloprotease that acts as a negative regulator of the Wnt signaling pathway by mediating the cleavage of the 8 N-terminal residues of a subset of Wnt proteins. Following cleavage, Wnt proteins become oxidized and form large disulfide-bond oligomers, leading to their inactivation. Able to cleave WNT3A, WNT5, but not WNT11. Required for head formation (By similarity).
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B1AUH1
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PTPRU_MOUSE
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Receptor-type tyrosine-protein phosphatase U (R-PTP-U) (EC 3.1.3.48) (Ftp-1) (Pancreatic carcinoma phosphatase 2) (PCP-2) (Protein-tyrosine phosphatase-lamda) (PTP-lambda) (PTPlambda) (Receptor-type protein-tyrosine phosphatase psi) (R-PTP-psi)
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MARAQALVLALTFQFCAPETETPAAGCTFEEASDPVVPCEFSQAQYDDFQWEQVRIHPGTRTPEDLPHGAYLMVNASQHAPGQRAHIIFQTLSENDTHCVQFSYFLYSRDGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWPNEYQVLFEALISPDHKGYIGLDDILLFSYPCAKAPHFSRLGDVEVNAGQNASFQCMAAGRAAEAEHFFLQRQSGVLVPAAGVRHISHRRFLATFPLASVGRSEQDLYRCVSQAPRGAGVSNFAELIVKEPPTPIAPPQLLRAGPTYLIIQLNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVNLQTYKLWHLDPDTEYEISVLLTRPGDGGTGRPGPPLISRTKCAEPTRAPKGLAFAEIQARQLTLQWEPLGYNVTRCHTYAVSLCYRYTLGGSHNQTIRECVKMERGASRYTIKNLLPFRNIHVRLILTNPEGRKEGKEVTFQTDEDVPGGIAAESLTFTPLEDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTSKGFGQAALTEITTNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISVYQVVVEEERPRRLRREPGAQDCFSVPLTFETALARGLVHYFGAELAASSLLEAMPFTVGDNQTYRGFWNPPLEPRKAYLIYFQAASHLKGETRLNCIRIARKAACKESKRPLEVSQRSEEMGLILGICAGGLAVLILLLGAIIVIIRKGRDRYAYSYYPKPVNMTKATVNYRQEKTHMMSAVDRSFTDQSTLQEDERLGLSFMDAPGYSPRGDQRSGGVTEASSLLGGSPRRPCGRKGSPYHTGQLHPAVRVADLLQHINQMKTAEGYGFKQEYESFFEGWDATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIDGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLCGETTIPVNEFKATYREMIRIDPQSNSSQLREEFQTLNSVTPPLDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLEALELR
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Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis (By similarity).
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B1AVY7
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KI16B_MOUSE
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Kinesin-like protein KIF16B
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MASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTKTFTYDFSFYSADTKSPDYVSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTRWDEASFRTEVSYLEIYNERVRDLLRRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAANPLVKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINEDANVKLIRELRAEIARLKTLLAQGNQIALLDSPTALSMEEKLHQNEARVQELTKEWTNKWNETQNILKEQTLALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLREKRKSGLLSSFSLSMTDLSKSCENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLLQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEMDPARLEHEIHQLKQKICEVDGVQRPHHGILEGQAVLSSLPPSGGNSHLAPLMDARISAYIEEEVQRRLHDLHRAIGDANHTPADVMKSNEELHNGTTQRKLKYERMYSRSLGTNRDDLKDPIKISIPRYVLCGQGKDEHFEFEVKISVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVVAERRTHLEKYLREFFSVMLQSETSPLHINKVGLTLSKHTICEFSPFFKKGVFDYSSHGTG
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Plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. Regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development.
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B1AWL2
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ZN462_MOUSE
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Zinc finger protein 462 (Zinc finger PBX1-interacting protein) (ZFPIP)
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MEVLQCDGCDFRAPSYEDLKAHIQDVHTAFLQPTDVAEDNDDEPLSGSMNASNQTEVEFSSIKDEFVIAEDLPGQSATALGSGGYYGHSPGYYGQHITPNPKPTNKFFQCKFCVRYFRSKNLLIEHTRKVHGAQAEESPTGPPVPGSLNYNIMMHEGFGKVFSCQFCTYKSPRRARIIKHQKMYHKNSLKESTAPPPAPAPLPDPLVPPVSLQDPCKELPAEVVERSILESMVKPLTKSRGNFCCEWCSYQTPRRERWCDHMMKKHRSMVKILSSIRQQEGPNVSEAQNDNEPSPTSNSTYLSMNAASREMPNANVSNFRGSMGNSIMRPNSSSTSKFSSSMSYPQMKPKSPHNSGLVNLTERSRYGMSDMTNSSADLDTNSMLNDSSSDEDLNEVDSENGLSVLDHQASGLSAEQLMGSDGNKLLETKGIPFRRFMNRFQCPFCPFLTMHRRSISRHIENIHLSGKTAVYKCDECPFTCKSSLKLGAHKQCHTGTSDWDTVNSQSESLSSSLNEGMVSYESSSINGRKSGVMLDPLQQQQPPQPPPPLPPPPPPPSQPLPQPPPPPLQSPHQVPPPTQQPQPPTQAPPLHPYKCTMCSYSTMTLKGLRVHQQHKHSFCDNLPKFEGQPSSLPLENETDSHPSSSNTVKKSQTSILGLSSKNNFVAKANRKLASDFPLDLSPVKKRTRIDEIASNLQSKINQTKLQEDAIINVEDDEEEEDDNEVEIEVELDREEEATDPIMEVPTAFSAQQIWARDASEAQKEPNYRSITHDYTATNGAEIELTLSEDEEDYYGSSASMKDQVSNAALLNTQPAIYGTEPSNENTDFGDSGRLYYCKHCDFNNKSARSVSTHYQRMHPYIKFSFRYILDPNDHSAVYRCLECYIDYTNFEDLQQHYGEHHPEAMNVLNFDHSDLIYRCRFCSYTSPNVRSLMPHYQRMHPTVKINNAMIFSSYVVEQQEGLNAESQTLREILNSAPKSMATSTPVARGGGLPATFNKNTPPKTFTPECESQKDPSVNTVVVYDCDVCSFASPNMHSVLVHYQKKHPEEKASYFRIQKTMRMVSVDRGSALSQLSFEVGAPMSPKMSNMGSPPPPQPPPPDLSIELYYCKHCSYSNRSVVGVLVHYQKRHPEIKVTAKYIRQAPPTAAMMRGAEGLQDSPRPPAPLQLNSSERDCPPVETEMFFCQHCDYGNRTVKGVLIHYQKKHRDFKANADVIRQHTATIRSLCDRNQKPASCVLLPASGMERDKTKLRALKCRQCSYTSPYFYALRKHIKKDHPALKATVTSIMRWAFLDGLIEAGYHCEWCIYSHMEPSGLLLHYQRRHPEHYVDYTYMATKLWAGPDPSSPTLTMSAEAKTYRCRDCVFEAVSIWDITNHYQAFHPWAMNGDESVLLDIIKEKDGVDKALLAPEELIGPVNCENSIPNPLPEQEAECPEDARLSPEKSIHLASANPAISSTPYQCTVCQSEYNNLHGLLTHYGKKHPGMKVKAADFAQDIDINPGAVYKCRHCPYINTRIHGVLTHYQKRHPAIKVTAEDFVHDVEQSADISQNDVEETSRIFKQGYGAYRCKLCPYTHGTLEKLKIHYEKYHNQPEFDVFSPPPPKLPVSLEPEITTEVSPSQVSVTEEEVGEDPMSTAHFSTSHLVSHTVFRCQLCKYFCSTRKGIARHYRIKHNNVRAQPEGKNNLFKCALCAYTNPIRKGLAAHYQKRHDIDAYYTHCLAASRTISDKPNKVIIPSPPKDDSPQLSEELRRAVEKKKCSLCSFQSFSKKGIVSHYMKRHPGVFPKKQHASKLGGYFTAVYADEHEKPPLMEEEERSSFERAEVEGEAQDIEWLPFRCIKCFKLSFSTAELLCMHYTDHHSRDLKRDFVILGSGPRFQNSTFQCKHCDSKLQSIAELTSHLNIHNEEFQKRAKRQERRKQLLSKQKYADGAFADFKQERPFGHLEEVPKIKERKVVGYKCKFCVEVHPTLRAICNHLRKHVQYGSVPAVSAAVKGLRSHERSHLALAMFTREDKYSCQYCSFVSAFRHNLDRHMQTHHGHHKPFRCKLCSFKSSYNSRLKTHILKAHAGEHAYKCSWCSFSTMTISQLKEHSLKVHGKALTLPRPRIVSLLSSHAHPSSQKATPAEEVEDSNDSSYSEPPDVQQQLNHYQSAALARNKSRVSPVPPSGTAAGTEQKAEAVLHCEFCEFSSGYIQSIRRHYRDKHGGKKLFKCKDCSFYTGFKSAFTMHVEAGHSAVPEEGPKDLRCPLCLYHTKYKRNMIDHIVLHREERVVPIEVCRSKLSKYLQGVVFRCDKCTFTCSSDESLQQHIEKHNELKPYKCQLCYYETKHTEELDTHLRDEHKVSRNFELVGRVNLDQLEQMKEKIESSSSEDEDKDDEMSSKAEDRELMRFADRGPGVNTEKRFPCEFCGRAFSQGSEWERHVLRHGMSLHDTNQVSRNEIHTKEMVEESMQLPSIEAKEDDEPIGIDFPLKSETVTICVVAADKSLLEDAEAKNE
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Zinc finger nuclear factor involved in transcription by regulating chromatin structure and organization. Involved in the pluripotency and differentiation of embryonic stem cells by regulating SOX2, POU5F1/OCT4, and NANOG. By binding PBX1, prevents the heterodimerization of PBX1 and HOXA9 and their binding to DNA. Regulates neuronal development and neural cell differentiation.
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B1AWN4
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AT10B_MOUSE
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Phospholipid-transporting ATPase VB (EC 7.6.2.1)
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MTCSLDFSWLRWKWRTQDGFSQSPSETTPLLSPETDRQSHNTAEQRVVYPNNSMCHQDWKKVCRRYPGNSICTTKYTLLTFLPQNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITIFPLATVLLIIMVKDGIEDFKRYCFDREMNSASIQIYERKEQRYMLKRWQDVRVGDFVQMQCNEIVPADILLLFSSDPSGVCHLETANLDGETNLKQRRVVKGFSQPEVQFQPEHFHSTIVCEKPNNHLSKFKGYMEHPDQTRTGFGSESLLLRGCTIRNTEVAAGIVIYAGHETKAMLNNSGPRYKRSKIERRINTDIFFCIGLLFLMCLIGAVGHSLWNGTFKEHPPFDVPDADGNFLSLALGGFYMFLTMIILLQVLIPISLYVSIELVKLGQVFLLHNDLDLYDEETDLSIQCRALNITEDLGQIQYIFSDKTGTLTENKMVFRRCTIVGSEYCHQENAKRLEMPKELDSDGEEWTQYQCLSFPPRWAQGSTTMRSQGGAQPLRRCHSARVPIQSHCRQRSVGRWETSQPPVAFSSSIEKDVTPDKNLLSKVRDAALWLETSDTRPAKPSHSTTASIADFFLALTICNSVMVSTTTEPRKRVTTPPANKALGTSLEKIQQLFQRLKLLSLSQSFSSTAPSDTDLGESLGPNLPTIDSDEKDDTSVCSGDCSTDGGYRSSTWEQGDILGSESGTSLEEGLEAPTLSQDEPELCYEAESPDEAALVHAARAYSFTLVSRTPEQVTVRLPQGICLTFDLLFTLGFDSVRKRMSVVVRHPLTDEIIVYTKGADSVIMDLLEDPACESNIDVEKKLKRIRARTQKHLDLYARDGLRTLCIAKKVVDEEDFQRWASFRREAEASLDNREELLMETAQHLENHLTLLGATGIEDRLQEGVPDTIAALREAGIQLWVLTGDKQETAVNIAYSCKLLDQTDTVYSINTENQETCESILNCTLEDIKRFHEPQQPARKLCGHRIPPKMPSVNSGAMAPEIGLVIDGKTLNAIFQGKLENKFLELTQYCRSVLCCRSTPLQKSMIVKLVRDKLSVMTLSIGDGANDVSMIQAADIGIGISGQEGMQAVMSSDFAIARFSHLKKLLLVHGHWCYSRLARMVVYYFYKNVCYVNLLFWYQFFCGFSGSTMIDYWQMIFFNLFFTSLPPIIFGVLDKDVSAETLLALPELYKSGQNSECYNLPTFWVSMADAFYQSLICFFIPYLTYRGSDIDVFTFGTPINTISLTTILLHQAMEMKTWTVLHGLVLLGSFLMYFVVSLIYNATCVTCNSPTNPYWVMERQLSDPTFYLICLLTPVVALLPRYFLLSLQGTYGKSLISKAQKIDKLPIDKRNLEIQNWRSKQRPAPASASASASAPATGTVHTRPPCHPVPPEAQQNFGASTSKSSGPPRQKHVEDRVLQDPRCSREHSRDDTCTVDTLAKLSSGECLLDPNRTVAPTAYSRGQKDVSRHSSKGSHRRSQSSLTI
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Catalytic component of a P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of glucosylceramide (GlcCer) from the outer to the inner leaflet of lysosome membranes (By similarity). Plays an important role in the maintenance of lysosome membrane integrity and function in cortical neurons.
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B1AWN6
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SCN2A_MOUSE
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Sodium channel protein type 2 subunit alpha (Voltage-gated sodium channel subunit alpha Nav1.2)
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MAQSVLVPPGPDSFRFFTRESLAAIEQRIAEEKAKRPKQERKDEDDENGPKPNSDLEAGKSLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAISRFSATSALYILTPFNPIRKLAIKILVHSLFNVLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPDNSTFEINITSFFNNSLDWNGTAFNRTMNMFNWDEYIEDKSHFYFLEGQNDALLCGNSSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAAAAAASAESRDFSGAGGIGVFSESSSVASKLSSKSEKELKNRRKKKKQKEQAGEEEKEDAVRKSASEDSIRKKGFRFSLEGSRLTYEKRFSSPHQSLLSIRGSLFSPRRNSRASLFSFKGRVKDIGSENDFADDEHSTFEDNDSRRDSLFVPHRHGERRPSNVSQASRASRGIPTLPMNGKMHSAVDCNGVVSLVGGPSALTSPVGQLLPEGTTTETEIRKRRSSSYHVSMDLLEDPTSRQRAMSMASILTNTMEELEESRQKCPPCWYKFANMCLIWDCCKPWLKVKHVVNLVVMDPFVDLAITICIVLNTLFMAMEHYPMTEQFSSVLSVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVSLSLMELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKISNDCELPRWHMHDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLTVFMMVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDFVKRKIREFIQKAFVRKQKALDEIKPLEDLNNKKDSCISNHTTIEIGKDLNYLKDGNGTTSGIGSSVEKYVVDESDYMSFINNPSLTVTVPIAVGESDFENLNTEEFSSESDMEESKEKLNATSSSEGSTVDIGAPAEGEQPEAEPEESLEPEACFTEDCVRKFKCCQISIEEGKGKLWWNLRKTCYKIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQMYFTNAWCWLDFLIVDVSLVSLTANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCINYTTGEMFDVSVVNNYSECQALIESNQTARWKNVKVNFDNVGLGYLSLLQVATFKGWMDIMYAAVDSRNVELQPKYEDNLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTKQVFDISIMILICLNMVTMMVETDDQSQEMTNILYWINLVFIVLFTGECVLKLISLRHYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKREVGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSGPPDCDPEKDHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFCKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEERFMASNPSKVSYEPITTTLKRKQEEVSAIVIQRAYRRYLLKQKVKKVSSIYKKDKGKEDEGTPIKEDIITDKLNENSTPEKTDVTPSTTSPPSYDSVTKPEKEKFEKDKSEKEDKGKDIRESKK
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Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. Implicated in the regulation of hippocampal replay occurring within sharp wave ripples (SPW-R) important for memory.
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B1AXD8
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AKIR2_MOUSE
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Akirin-2
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MACGATLKRTLDFDPLLSPASPKRRRCAPLSAPASAAASPAAATAAAAASAAAASPQKYLRMEPSPFGDVSSRLTTEQILYNIKQEYKRMQKRRHLEASFQQADPGCTSDSQPHAFLISGPASPGTSSATSSPLKKEQPLFTLRQVGMICERLLKEREEKVREEYEEILNTKLAEQYDAFVKFTHDQIMRRYGEQPASYVS
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Molecular adapter that acts as a bridge between a variety of multiprotein complexes, and which is involved in embryonic development, immunity, myogenesis and brain development. Plays a key role in nuclear protein degradation by promoting import of proteasomes into the nucleus: directly binds to fully assembled 20S proteasomes at one end and to nuclear import receptor IPO9 at the other end, bridging them together and mediating the import of pre-assembled proteasome complexes through the nuclear pore (By similarity). Involved in innate immunity by regulating the production of interleukin-6 (IL6) downstream of Toll-like receptor (TLR): acts by bridging the NF-kappa-B inhibitor NFKBIZ and the SWI/SNF complex, leading to promote induction of IL6. Also involved in adaptive immunity by promoting B-cell activation. Involved in brain development: required for the survival and proliferation of cerebral cortical progenitor cells. Involved in myogenesis: required for skeletal muscle formation and skeletal development, possibly by regulating expression of muscle differentiation factors. Also plays a role in facilitating interdigital tissue regression during limb development.
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B1AY10
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NFX1_MOUSE
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Transcriptional repressor NF-X1 (m-Nfx.1) (EC 2.3.2.-) (Nuclear transcription factor, X box-binding protein 1)
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MAEAPPVSGTFKFNTDAAEFIPQERKTSGLNCGTQRRLDSSRIGRRNYSSSPPCHLPRHIPYEDISAVHQHSYASGSKPKSPQGFFQSSNKSLKNHGLQNQPWQKARNEKHQNRNKKAQGLSEQTSDTSSLESVARSESGTNPREHSPSESEKEVVIADPRGAKPKKAAQLTYNYGRGPKAKGRLRSEWGNRMSPKSEDENTRPVAISHTDSSDASCRKPVVDPCVCRRNEQRRYPQKRPPWEVEGARPRPGRNPPKQESQRHINAGPKTNMSPIPKDNLRERPTKSACDTGNLAVVSKSSRRVNQEKTAVRRQDPQVLSPFPRGKQNHMLKNVETHTGSLIEQLTTEKYECMVCCELVQVTAPVWSCQSCFHVFHLNCIKKWARSPASHADGQSGWRCPACQNVSAHVPNTYTCFCGKVKNPEWSRNEIPHSCGEVCRKKQPGQDCPHSCNLLCHPGPCPPCPAFTTKTCECGRTRHTVRCGQPVSVHCSNACENILNCGQHHCAELCHGGQCQPCRIILNQVCYCGSTSRDVLCGTDVGKSDGFGDFSCLKICGKDLKCGSHTCSQVCHPQPCQPCPRLPHLVRYCPCGQTPLSQLLEHGSNARKTCMDPVPSCGKVCGKPLACGSSDFIHTCEKLCHEGDCGPCSRTSVISCRCSFRTKELPCTSLKSEDATFMCDKRCNKKRLCGRHKCNEICCVDKEHKCPLICGRKLRCGLHRCEEPCHRGNCQTCWQASFDELTCHCGASVIYPPVPCGTRPPECTQTCARIHECDHPVYHSCHSEEKCPPCTFLTQKWCMGKHELRSNIPCHLVDISCGLPCSAMLPCGMHKCQRLCHKGECLVDEACKQPCTTPRGDCGHPCMAPCHPSLPCPVTACKAKVELQCECGRRKEMVICSEASGTYQRIVAISMASKITDMQLGDSVEISKLITKKEVQQARLQCDEECAALERRKRLAEAFDITDDSDPFNVRSSASKFSDSLKDDARKDLKFVSDVEKEMETLVEAVNKGKNNKKSHCFPPMNRDHRRIIHDLAQVYGLESISYDSEPKRNVVVTAVRGKSVCPPTTLTSVIERETQTRPPPPIPHHRHQADKAPGSSTLQKIVKEAVIDYFDVQD
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Binds to the X-box motif of MHC class II genes and represses their expression. May play an important role in regulating the duration of an inflammatory response by limiting the period in which MHC class II molecules are induced by interferon-gamma. Together with PABPC1 or PABPC4, acts as a coactivator for TERT expression. Mediates E2-dependent ubiquitination.
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B1AY15
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UBP51_MOUSE
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Ubiquitin carboxyl-terminal hydrolase 51 (EC 3.4.19.12) (Deubiquitinating enzyme 51)
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MRGTQGAQEMKPELWPEPKPTSENLTSRGSGSYEKVLPSIPAACHTSSSSVCPRRKPRPRPQPRSRSRGGRGLKAPPPPPAKPPPPPPAPPPPPLPKQRSVAWRNSRRRSRPGPRPQTRKSYSSDHGSSRDSDGSENSLLEVGSNKGPTGCCHVESFKVAKNWQRNLRMIYQRFIWSGTPETRKRKAKSCICQICSTHKNRLHSCLSCVFFGCFTDKHIHIHAETTQHNLAVDLCHGVIYCFMCRDYVYDKDIEKIAKETKEKILGLLSSPTGDASYQQLMASEVEENQLTCESKDQETSLVKPKKKRRKKTMYYTVGFRGLINLGNTCFMNCIVQVLTHIPLLKEFFLSNKHKCMMTSPSLCLVCEMSLLFQAMYSGNQSPHIPYKLLHLIWIHAEHLAGYRQQDAQEFLIAILDVLHRHSRDDGIDQEGNSNCCNCIIDHIFTGSLQSDLTCQVCHGVSTTIDPCWDISLDLPGPYTPGRASSSTSSRDGQKPRVISLTDCLKWFTRPEDLGSSAKIKCSQCQSYQESTKQLTMKKLPIVACFHLKRFEHLGKQRRKINSFISFPLELDMTPFLASTKESIMKGQPLTECVPSENKYSLFAVINHHGTLESGHYTSFVRQEKDQWFSCDDAVVTKATMEELLNSEGYLLFYHRQDIEKE
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Deubiquitinates histone H2A at 'Lys-13' and 'Lys-15' and regulates DNA damage response. USP51 is recruited to chromatin after DNA damage and regulates the dynamic assembly/disassembly of TP53BP1 and BRCA1 foci.
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B1AZ99
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OTUD3_MOUSE
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OTU domain-containing protein 3 (EC 3.4.19.12)
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MSRKQAAKSRPGSGGRRAEAERKRDERAARRALAKERRNRPDPGGSGCEEEFVSFANQLQALGLKLREVPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIRQREDFEPFVEDDIPFEKHVASLSKPGTFAGNDAIVAFARNHQLNVVIHQLNAPLWQIRGTDKGSTRELHIAYRYGEHYDSVRRINDNSEAPAHLLTDFQMLHQDGANKKEKMKTKGVDVKDGLRDDVEDAVHKVGSATGCTDFNLIVQNLEAENYNIKSAITALLQVNQGTGNDAEENHEPGDRVKQRGPSREEAGSGRRLSGNQGRNEGRMETSEARASPAEESKAHKSQLPKVTNKQRREQQRLEKKKRQEERHRLKALENRNGSRDTGRSEADMNTQVTLVKTFAALNI
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Deubiquitinating enzyme that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. Also hydrolyzes heterotypic (mixed and branched) and homotypic chains. Important regulator of energy metabolism. Glucose and fatty acids trigger its nuclear translocation by CBP-dependent acetylation. In the nucleus, deubiquitinates and stabilizes the nuclear receptor PPARD regulating the expression of various genes involved in glucose and lipid metabolism and oxidative phosphorylation. Also acts as a negative regulator of the ribosome quality control (RQC) by mediating deubiquitination of 40S ribosomal proteins RPS10/eS10 and RPS20/uS10, thereby antagonizing ZNF598-mediated 40S ubiquitination (By similarity).
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B1AZI6
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THOC2_MOUSE
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THO complex subunit 2 (Tho2)
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MAAAAVVVPAEWIKNWEKSGRGEFLHLCRILSENKSHDSSTYRDFQQALYELSYHVIKGNLKHEQASSVLNDISEFREDMPSILADVFCILDIETNCLEEKSKRDYFTQLVLACLYLVSDTVLKERLDPETLESLGLIKQSQQFNQKSVKIKTKLFYKQQKFNLLREENEGYAKLIAELGQDLSGNITSDLILENIKSLIGCFNLDPNRVLDVILEVFECRPEHDDFFISLLESYMSMCEPQTLCHILGFKFKFYQEPSGETPSSLYRVAAVLLQFNLIDLDDLYVHLLPADNCIMDEYKREIVEAKQIVRKLTMVVLSSEKLDERDKEKDKDDEKVEKPPDNQKLGLLEALLKVGDWQHAQNIMDQMPPYYAASHKLIALAICKLIHITVEPLYRRVGVPKGAKGSPVSALQNKRAPKQVESFEDLRRDVFNMFCYLGPHLSHDPILFAKVVRIGKSFMKEFQSDGSKQEDKEKTEVILSCLLSITDQVLLPSLSLMDCNACMSEELWGMFKTFPYQHRYRLYGQWKNETYNGHPLLVKVKAQTIDRAKYIMKRLTKENVKPSGRQIGKLSHSNPTILFDYILSQIQKYDNLITPVVDSLKYLTSLNYDVLAYCIIEALANPEKERMKHDDTTISSWLQSLASFCGAVFRKYPIDLAGLLQYVANQLKAGKSFDLLILKEVVQKMAGIEITEEMTMEQLEAMTGGEQLKAEGGYFGQIRNTKKSSQRLKDALLDHDLALPLCLLMAQQRNGVIFQEGGEKHLKLVGKLYDQCHDTLVQFGGFLASNLSTEDYIKRVPSIDVLCNEFHTPHDAAFFLSRPMYAHHISSKYDELKKSEKGSKQQHKVHKYITSCEMVMAPVHEAVVSLHVSKVWDDISPQFYATFWSLTMYDLAVPHTSYEREVNKLKVQMKAIDDNQEMPPNKKKKEKERCTALQDKLLEEEKKQMEHVQRVLQRLKLEKDNWLLAKSTKNETITKFLQLCIFPRCIFSAIDAVYCARFVELVHQQKTPNFSTLLCYDRVFSDIIYTVASCTENEASRYGRFLCCMLETVTRWHSDRATYEKECGNYPGFLTILRATGFDGGNKADQLDYENFRHVVHKWHYKLTKASVHCLETGEYTHIRNILIVLTKILPWYPKVLNLGQALERRVNKICQEEKEKRPDLYALAMGYSGQLKSRKSHMIPENEFHHKDPPPRNAVASVQNGPGGGTSSSSIGNASKSDESGAEETDKSRERSQCGTKAVNKASSTTPKGNSSNGNSGSNSNKAVKENDKEKVKEKEKEKKEKTPATTPEARALGKDSKEKPKEERPNKEDKARETKERTPKSDKEKEKFKKEEKAKDEKFKTTVPIVESKSTQEREREKEPSRERDVAKEMKSKENVKGGEKTPVSGSLKSPVPRSDISEPDREQKRRKIDSHPSPSHSSTVKDSLIDLKDSSAKLYINHNPPPLSKSKEREMDKKDLDKSRERSREREKKDEKDRKERKRDHSNNDREVPPDITKRRKEENGTMGVSKHKSESPCESQYPNEKDKEKNKSKSSGKEKSSSDSFKSEKMDKISSGGKKESRHDKEKIEKKEKRDSSGGKEEKKHHKSSDKHR
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Required for efficient export of polyadenylated RNA and spliced mRNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. Plays a role for proper neuronal development.
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B1AZP2
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DLGP4_MOUSE
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Disks large-associated protein 4 (DAP-4) (PSD-95/SAP90-binding protein 4) (SAP90/PSD-95-associated protein 4) (SAPAP-4)
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MKGLGDSRPRHLSDSLDPPHEPLFAGPDRNPYLLSPTEAFAREARFPGQNTLPGDGLFPLNNQLPPPSSTFPRIHYNSHFEVPEESPFPSHAQATKINRLPANLLDQFEKQLPIHRDGFSTLQFPRGEAKARGESPGRIRHLVHSVQRLFFTKAPSMEGTAGKVGGNGSKKGGLEDGKGRRAKSKERAKAGEPKRRSRSNISGWWSSDDNLDGEGGAFRSGPASGLMTLGRQQERTQPRYFMHAYNTISGHMLKTTKNTTTELTAPPPPPAPPATCPSLGVGTDTNYVKRGSWSTLTLSHAHEVCQKTSATLDKSLLKSKSCHQGLAYHYLQVPGGGGEWSTTLLSPRDMDSTAEGPIPCRRMRSGSYIKAMGDEDSDESGGGSPKPSPKTAARRQSYLRATQQSLGEQSNPRRSLDRLDSVDMLLPSKCPSWEDDYNPISDSLNDSSCISQVFGQASLIPQLFGHDQQVREADLSDQYEAACESACSEAESTTAEALDLPLPSYFRSRSHSYLRAIQAGCSQEEDSVSLQSLSPPPSTGSLSNSRTLPSSSCLVAYKKTPPPVPPRTTSKPFISVTVQSSTESAQDTYLDSQDHKSEVTSQSGLSNSSDSLDSSTRPPSVTRGGITPGPEAPEPPPKHAALKSEQGTLTSSESHSEAIPKRKLSSIGIQVDCIQPVPKEEPSPATKFQSIGIQVEDDWRSSAPSHSMSSRRDTDSDTQDANDSSCKSSERSLPDCTSHPNSISIDAGPRQAPKIAQIKRNLSYGDNSDPALEASSLPPPDPWLETSSSSPAEPAQPGACRRDGYWFLKLLQAETERLEGWCCQMDKETKENNLSEEVLGKVLSAVGSAQLLMSQKFQQFRGLCEQNLNPDANPRPTAQDLAGFWDLLQLSIEDISMKFDELYHLKANSWQLVETPEKRKEEKKPPPPVPKKPAKSKAAVSRDKASDAGDKQRQEARKRLLAAKRAASVRQNSATESADSIEIYVPEAQTRL
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May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane (By similarity).
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B1B0V2
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EZHIP_MOUSE
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EZH inhibitory protein (K27M-like inhibitor of PRC2)
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MASSSSPERGLEALRDTDESEGEAPGPSGPRGRGGPSGAGSALRLRSLEAEMAAACVTSTAGEDLGTFSEPGSQHGDPEGGGGPDLELGHARPMMRSQRELGLTPKGGGKADQGGKGRKGGSGSPPHTKSSRKREQPNPNRSLMAQGAAGPPLPGARGSPAMPQPESSLSPRPDQSHHFDFPVGNLEAPGPTLRSSTSQGSGSTPVPEALRCAESSRAESDQSSPAGRELRQQASPRAPDDDDDGDGGPDPRGSGTPEGWVLRSGVVPFGRRSSASEVSPEEVRPEAQCTGWNLRPRPRSSASAVSPEARPKAQSAGRNLRPRPRSSASVVSPEARPKAQSAGRNLRPRPRSSASVVSPEARPEAQSAGRNLRPRATPRVPVAPSSTTRSSSDRGSSRAPRSRSRSRSCSTPRLGSDHQRSRKIKMRLDLQVDREPESEAEQEEQELESEPGPSSRPQASRSSSRFAVPGRSSLAAEDSPPRRPVRMRASSPSPPGRLYPLPKHYFEGVHSPSSSSSESSSVSSSHSPLNKAPDPGSSPPLSSLSGPNPFWLALIADLDNLDSSSPRVPGEEIEAAPHTREEEDKKCRG
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Inhibits PRC2/EED-EZH1 and PRC2/EED-EZH2 complex function by inhibiting EZH1/EZH2 methyltransferase activity, thereby causing down-regulation of histone H3 trimethylation at 'Lys-27' (H3K27me3). Probably inhibits methyltransferase activity by limiting the stimulatory effect of cofactors such as AEBP2 and JARID2 (By similarity). Inhibits H3K27me3 deposition during spermatogenesis and oogenesis.
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B1B534
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EHD2_ORYSJ
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Protein EARLY HEADING DATE 2 (Ehd2) (Protein RICE INDETERMINATE 1) (OsID) (OsID1)
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MLLSDLSSDQEATGSNSHGGGGGDRMVVGSHGAAHVVLSNLFLPPAAAAAATMLLPAAPVMVRPAAMAAAQEPRAKKKRSLPGNPDPEAEVIALSPRALVATNRFVCEVCNKGFQRDQNLQLHRRGHNLPWKLRHRAAAVSAVTTAAPAPRKRVYVCPEPTCVHHDPARALGDLTGIKKHFSRKHGEKRWRCERCGKRYAVHSDWKAHVKNCGTREYRCDCGILFSRKDSLLTHRAFCDALAEESARLLAAANNSSSITTTTCNNSNISSNNNNNNINSISNSNNLLITSSSSSPPLFLPFSTTPAENPNPNQLLFLQQHQAAHHQLLLPQFQQPPSSPPAYFDHLAFGGGGGVITGSSCNDDNSSIAGDVMVAAGGDSVSFGLTSEGSVTMHAGDVGRRRLTRDFLGVDHDAGEVDELELDELPADLSTTAAACQGCNFAAATTAACCATDFTTGSRQYLGRLPPVNETWSHNF
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Transcription activator that acts as a flowering master switch in both long and short days, independently of the circadian clock. Promotes flowering upstream of HD1 by up-regulating FTL1, FTL4, FTL5, FTL6, EHD1, HD3A and RFT1. Seems to repress FTL11 expression. May recognize the consensus motif 5'-TTTGTCGTAAT-3' in target gene promoters.
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B1H134
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FLRT3_XENTR
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Leucine-rich repeat transmembrane protein FLRT3 (Fibronectin-like domain-containing leucine-rich transmembrane protein 3)
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MSTETWNLFVAWAQLLLLFRISPQYVNAKPCPSVCRCDGGFIYCNDRDLTSIPSGIPDDATTLYLQNNQINNAGIPSDLRGLDKVERIYLYRNSLDEFPINLPKNVKELHLQENNIRTITYDALSQIPSIEELHLDDNSVSAVSIEDGAFRDNIFLRLLFLSRNHLSTIPWGLPRTIEELRLDDNRISTIAEISLQDLTNLKRLVLDGNLLNNNGLGERVFMNLINLTELSLVRNSLTSPPANLPGTNLRKLYLQENHMNYVPPNAFADLTQLYRLDMSNNNITALPQGIFDDLDNLTQLFLRNNPWYCGCKMKWVRDWLQSLPSKVNVRGLMCQAPERVRGMTIKDLNKELFDCKDRIGSNTIHVTTTVLNSLLPAQGQWPVPVTKQPEIRPPDINKIFRTTPIPVKKIITIQVKSITTETIYISWKVALPMTALRLSWQLGHSPVFGSITETIVTGDRTEYLLTALEPESPYRICMVPMETGNIYLSDETPVCIETETAPLKMYNPTTTLNREQEKEPYKNSSLPLAAIIGGAVALVAITLLALVCWYVHRNGSLFSRNCAYSKGRRRKDDYAEAGTKKDNSILEIRETSFPMIPINSDPISKEEFIIHTIFPPNGVSLYKNSHSESSSNRSYRDSGIPDSDHSHS
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Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners (By similarity). Modulates cadherin-dependent cell-cell adhesion and cell sorting (By similarity). Plays a role in the spatial organization of brain neurons. Plays a role in vascular development. Plays a role in cell-cell adhesion via its interaction with latrophilins that are expressed at the surface of adjacent cells. Mediates axon attraction towards cells expressing ntn1. mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with unc-5 family members. Plays a role in the regulation of the density of glutamaergic synapses (By similarity). Plays a role in signaling cascades downstream of fgfr1, and possibly also other fgfr family members (By similarity). Plays a role in embryonic morphogenesis, but not in embryonic patterning.
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B1H1X1
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FXL17_XENLA
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F-box/LRR-repeat protein 17 (F-box and leucine-rich repeat protein 17)
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MGHVAPHASKKEHVAPHAAEKDHVAPHASKKEHVAPHAAEKGQVAPYAAGEGQVAPNAAGERPVAPYAAGEGQVAPYAAGEGQVAPYAAGEGQVAPYAAGEGQVAPYAAGEAQVAPHAAGEGRVAPHAAGDGQVEHCTVEDREEGHIGTTEQGHMSHYTSKLEHMAPPSAQTEAVVSYVAGERHAPPDCTVSGPAMCCSAEARQTTPDWTTTGPEISQGTLPGLTVLHVGGTWQTFAAEDEPCVTTLLSPVKPLSSSRKYAPYNLQIPSYSESEPQAHKGLSSETFGPCEPLHINQLPSSLLLKIFSNLSLNERCILASLVCKYWRDLCLDSQFWKQLDLSNRQQIKDNILEEIASRSQNITEINISDCFSVSDQGVCVVALKCPGLVKYTAYRCKQLSDISLIALAAHCPSLQKVHVGNQDKLSDEALIQMGRRCKELKDIHFGQCYKISDEGLIVIAKGCQKLQKIYMQENKLVSDESVKAFAEHCPGLQYVGFMGCSVTSEGVINLTKLKHLSSLDLRHITELDNETVMEIVKQCQHLTSLNLCLNRSINDRCVEVIAKEGRSLKELYLVTCKITDYALIAIGRYSKSIETVDVGWCKEITDYGAKQIAQSSKSIRYLGLMRCDKVNEATVEQLVQQYPHITFSTVLQDCKRTLERAYQMGWTPNASPAT
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Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). FBXL17 specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition: aberrant BTB dimer are then ubiquitinated by the SCF(FBXL17) complex and degraded by the proteasome (By similarity). The ability of the SCF(FBXL17) complex to eliminate compromised BTB dimers is required for the differentiation and survival of neural crest and neuronal cells.
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B1H234
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FLRT3_RAT
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Leucine-rich repeat transmembrane protein FLRT3 (Fibronectin-like domain-containing leucine-rich transmembrane protein 3)
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MISPAWSLFLIGTKIGLFFQVAPLSVMAKSCPSVCRCDAGFIYCNDRSLTSIPVGIPEDATTLYLQNNQINNVGIPSDLKNLLKVQRIYLYHNSLDEFPTNLPKYVKELHLQENNIRTITYDSLSKIPYLEELHLDDNSVSAVSIEEGAFRDSNYLRLLFLSRNHLSTIPGGLPRTIEELRLDDNRISTISSPSLHGLTSLKRLVLDGNLLNNHGLGDKVFFNLVNLTELSLVRNSLTAAPVNLPGTSLRKLYLQDNHINRVPPNAFSYLRQLYRLDMSNNNLSNLPQGIFDDLDNITQLILRNNPWYCGCKMKWVRDWLQSLPVKVNVRGLMCQAPEKVRGMAIKDLSAELFDCKDSGIVSTVQITTAIPNTAYPAQGQWPAPVTKQPDIKNPKLTKDQRTTGSPSRKTILITVKSVTPDTIHISWRLALPMTALRLSWLKLGHSPAFGSITETIVTGERSEYLVTALEPESPYRVCMVPMETSNLYLFDETPVCIETQTAPLRMYNPTTTLNREQEKEPYKNPNLPLAAIIGGAVALVSIALLALVCWYVHRNGSLFSRNCAYSKGRRRKDDYAEAGTKKDNSILEIRETSFQMLPISNEPISKEEFVIHTIFPPNGMNLYKNNLSESSSNRSYRDSGIPDLDHSHS
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Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners. Plays a role in the spatial organization of brain neurons. Plays a role in vascular development in the retina (By similarity). Plays a role in cell-cell adhesion via its interaction with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells (By similarity). Interaction with the intracellular domain of ROBO1 mediates axon attraction towards cells expressing NTN1. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5B, and possibly also other UNC-5 family members (By similarity). Promotes neurite outgrowth (in vitro) (By similarity). Mediates cell-cell contacts that promote an increase both in neurite number and in neurite length. Plays a role in the regulation of the density of glutamaergic synapses. Plays a role in fibroblast growth factor-mediated signaling cascades. Required for normal morphogenesis during embryonic development, but not for normal embryonic patterning. Required for normal ventral closure, headfold fusion and definitive endoderm migration during embryonic development. Required for the formation of a normal basement membrane and the maintenance of a normal anterior visceral endoderm during embryonic development (By similarity).
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B1H267
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SNX5_RAT
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Sorting nexin-5
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MAAVPELLEQQEEDRSKLRSVSVDLNVDPSLQIDIPDALSERDKVKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLTETTDYAGLIIPPAPTKPDFDGPREKMQKLGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVSSHEVFLQRLSSHPVLSKDRNFHVFLEYDQDLSVRRKNTKEMFGGFFKSVVKSADEVLFSGVKEVDDFFEQEKNFLINYYNRIKDSCAKADKMTRSHKNVADDYIHTAACLHSLALEEPTVIKKYLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLKSKDVKLAETHQQECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQSCIDLFKNN
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Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol lipids. Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC). Does not have in vitro vesicle-to-membrane remodeling activity. Involved in retrograde transport of lysosomal enzyme receptor IGF2R. May function as link between endosomal transport vesicles and dynactin. Plays a role in the internalization of EGFR after EGF stimulation. Involved in EGFR endosomal sorting and degradation the function involves PIP5K1C and is retromer-independent. Together with PIP5K1C facilitates HGS interaction with ubiquitinated EGFR, which initiates EGFR sorting to intraluminal vesicles (ILVs) of the multivesicular body for subsequent lysosomal degradation. Involved in E-cadherin sorting and degradation inhibits PIP5K1C-mediated E-cadherin degradation. Plays a role in macropinocytosis (By similarity).
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B1H278
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TRI11_RAT
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E3 ubiquitin-protein ligase TRIM11 (EC 2.3.2.27) (Tripartite motif-containing protein 11)
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MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECREVSAQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCAAHREPLTTFCGDDLSLLCPTCERSEHWAHRVRPLQEAADDLKGRLEKSLEHLRKQMEDAMLFQAQAEETCALWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQKLEEEELEVLPRLREGAARLGQQSTQLAALVSELESRCQLPALGLLQDIKDALCRVQDVKLQPPAVVPMELRTVCRVPGLVETLRRFRGDITLDPDTANPELVLSEDRRSVQRGEQRQALPDSPERFDPGPCVLGQERITSGRHYWEVEVGDQTSWALGVCKETVNRKEKGELSAGNGFWILVFLGSFYNSNERAFSPLRDPPKRVGIFLDYEAGHLSFYSATDGSLLFIFPETPFSGTLRPLFSPLSSSPTPMTICRLIGVSGDTLGPQ
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E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway (By similarity). Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle. Acts as an inhibitor of the AIM2 inflammasome by promoting autophagy-dependent degradation of AIM2. Mechanistically, undergoes autoubiquitination upon DNA stimulation, promoting interaction with AIM2 and SQSTM1/p62, leading to AIM2 recruitment to autophagosomes (By similarity).
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B1H3E1
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NLK2_XENTR
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Serine/threonine-protein kinase NLK2 (EC 2.7.11.24) (Nemo-like kinase 2) (Nlk.2)
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MAFQGPGRSLPGQLCAGVFGGLIQPPLGQKFYCPNGGSGGGGVPAVPSPLPQALSAPQCNGDGRGEPEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPQIDCFEEIYVITELMQTDLHKVIVSPQPLSSDHIKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESQHMTQEVVTQYYRAPEILMGSRHYRSAIDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPPLTAMRSACEGARAHILRGPHKPPSLSVLYMLSGEATHEAVHLLCRMLLFDPLKRISAKDALAHPYLEEGRLRYHTCMCHCCYSVSSGRVYTADFEPTATNRFDDSYEKSLTSVWQVKELVHRFITDQQQGKRPPLCINPHSAAFKTFIRSTAWHSSKVSKKEER
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Negatively regulates Wnt/beta-catenin-signaling during development. Plays a role together with sox11 in neural induction during early embryogenesis. Involved in TGFbeta-mediated mesoderm induction in early embryos, acting downstream of map3k7/tak1 to phosphorylate stat3. Augments the rnf138/narf-directed ubiquitination and degradation of tcf/lef by enhancing the association of rnf138/narf and tcf/lef. Phosphorylates mef2a to play a role in anterior neural development, including eye formation (By similarity).
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B1INP5
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BXB_CLOBK
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Botulinum neurotoxin type B (BoNT/B) (Bontoxilysin-B) [Cleaved into: Botulinum neurotoxin B light chain (LC) (EC 3.4.24.69); Botulinum neurotoxin B heavy chain (HC)]
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MPVTINNFNYNDPIDNNNIIMMEPPFARGTGRYYKAFKITDRIWIIPERYTFGYKPEDFNKSSGIFNRDVCEYYDPDYLNTNDKKNIFLQTMIKLFNRIKSKPLGEKLLEMIINGIPYLGDRRVPLEEFNTNIASVTVNKLISNPGEVERKKGIFANLIIFGPGPVLNENETIDIGIQNHFASREGFGGIMQMKFCPEYVSVFNNVQENKGASIFNRRGYFSDPALILMHELIHVLHGLYGIKVDDLPIVPNEKKFFMQSTDAIQAEELYTFGGQDPSIITPSTDKSIYDKVLQNFRGIVDRLNKVLVCISDPNININIYKNKFKDKYKFVEDSEGKYSIDVESFDKLYKSLMFGFTETNIAENYKIKTRASYFSDSLPPVKIKNLLDNEIYTIEEGFNISDKDMEKEYRGQNKAINKQAYEEISKEHLAVYKIQMCKSVKAPGICIDVDNEDLFFIADKNSFSDDLSKNERIEYNTQSNYIENDFPINELILDTDLISKIELPSENTESLTDFNVDVPVYEKQPAIKKIFTDENTIFQYLYSQTFPLDIRDISLTSSFDDALLFSNKVYSFFSMDYIKTANKVVEAGLFAGWVKQIVNDFVIEANKSNTMDKIADISLIVPYIGLALNVGNETAKGNFENAFEIAGASILLEFIPELLIPVVGAFLLESYIDNKNKIIKTIDNALTKRNEKWSDMYGLIVAQWLSTVNTQFYTIKEGMYKALNYQAQALEEIIKYRYNIYSEKEKSNINIDFNDINSKLNEGINQAIDNINNFINGCSVSYLMKKMIPLAVEKLLDFDNTLKKNLLNYIDENKLYLIGSAEYEKSKVNKYLKTIMPFDLSIYTNDTILIEMFNKYNSEILNNIILNLRYKDNNLIDLSGYGAKVEVYDGVELNDKNQFKLTSSANSKIRVTQNQNIIFNSVFLDFSVSFWIRIPKYKNDGIQNYIHNEYTIINCMKNNSGWKISIRGNRIIWTLIDINGKTKSVFFEYNIREDISEYINRWFFVTITNNLNNAKIYINGKLESNTDIKDIREVIANGEIIFKLDGDIDRTQFIWMKYFSIFNTELSQSNIEERYKIQSYSEYLKDFWGNPLMYNKEYYMFNAGNKNSYIKLKKDSPVGEILTRSKYNQNSKYINYRDLYIGEKFIIRRKSNSQSINDDIVRKEDYIYLDFFNLNQEWRVYTYKYFKKEEEKLFLAPISDSDEFYNTIQIKEYDEQPTYSCQLLFKKDEESTDEIGLIGIHRFYESGIVFEEYKDYFCISKWYLKEVKRKPYNLKLGCNWQFIPKDEGWTE
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[Botulinum neurotoxin type B]: Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotoxin B which has 2 coreceptors complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway. When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the HC forms pores that allows the light chain (LC) to translocate into the cytosol. Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release (By similarity). [Botulinum neurotoxin B light chain]: Has proteolytic activity. After translocation into the eukaryotic host cytosol, LC hydrolyzes the '76-Gln-|-Phe-77' bond in synaptobrevin-2/VAMP2, blocking neurotransmitter release (By similarity). [Botulinum neurotoxin B heavy chain]: Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD). The RBD is responsible for the adherence of the toxin to the cell surface. It simultaneously recognizes 2 coreceptors polysialated gangliosides and host synaptotagmin-1 and -2 (SYT1 and SYT2) which bind simultaneously to adjacent but separate sites at the tip of the HC. The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) in the active site it may also prevent premature LC dissociation from the translocation channel and protect toxin prior to translocation (By similarity). The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol (By similarity).
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B1IZU5
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HCHA_ECOLC
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Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
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MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG
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Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}.
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B1J5A5
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FADB_PSEPW
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MIYEGKAITVKALESGIVELKFDLKGESVNKFNRLTLDELRQAVEAIKADASVKGVIVSSGKDVFIVGADITEFVDNFKLPEAELVAGNLEANRIFNAFEDLEVPTVAAINGIALGGGLEMCLAADYRVMSTSAKIGLPEVKLGIYPGFGGTVRLPRLIGSDNAIEWIAAGKENRAEDALKVGAVDAVVAPELLQAGALDLVKRAISGELDYKAKRQPKLEKLKLNAIEQMMAFETAKGFVAGQAGPNYPAPVEAIKSIQKAANFGRDKALEVEAAGFAKLAKTSVAQSLIGLFLNDQELKRKAKAHDEIAHDVKQAAVLGAGIMGGGIAYQSAVKGTPILMKDIREEAIQLGLNEASKLLGNRVEKGRLTPAKMAEALNAIRPTLSYGDFANVDIVVEAVVENPKVKQAVLAEVEGQVKEDAILASNTSTISINLLAKALKRPENFVGMHFFNPVHMMPLVEVIRGEKSSEVAVATTVAYAKKMGKNPIVVNDCPGFLVNRVLFPYFGGFAKLVSAGVDFVRIDKVMEKFGWPMGPAYLMDVVGIDTGHHGRDVMAEGFPDRMKDERRSAVDALYEANRLGQKNGKGFYAYETDKRGKPKKVFDATVLDVLKPIVFEQREVTDEDIINWMMVPLCLETVRCLEDGIVETAAEADMGLVYGIGFPPFRGGALRYIDSIGVAEFVALADQYADLGPLYHPTAKLREMAKNGQRFFS
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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B1KCZ3
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FADB_SHEWM
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MIYQSPTIQVELLEDNIARLCFNAAGSVNKLDRETIDSLNAALDAIKQDTNIQGLVLTSGKGAFIVGADITEFLGLFAQEESVLLPWIAEANVVFNKIEDLPFPTISAINGFALGGGFETVLATDFRIADTTAKLGLPETKLGLIPGFGGTVRLPRLIGADNALEWITTGKDHKPEAALKVGAIDAVVAPENLEASAIAMLKEALSEKLDWQARRAKKQAPLNLPKLEAMMSFATAKGMVFKVAGKHYPAPMTAISVIEQAARSERADALMVEHQAFIKLAKTDVAQALIGIFLNDQLVKGKAKKAGKLAKNVDSAAVLGAGIMGGGIAYQSASKGTPIVMKDIAQPALDLGLGEASKLLAAQIKRGRSTPEKMAKVLNNITATLDYAPVKDVDVVVEAVVEHPKVKSMVLAEVEQNVSDDAIITSNTSTISINLLAKSLKKPERFCGMHFFNPVHKMPLVEVIRGENSSEETIASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSGLLADGADFAAIDKVMEKQFGWPMGPAYLLDVVGIDTGHHAQAVMAEGFPDRMGKDGKDAIDIMFDSERFGQKNNKGFYAYSVDRRGKPKKDLDPTSYELLGAEFGDLKAFESDEIIARTMIPMIIETVRCLEEGIIATPAEADMGLVFGLGFPPFRGGVFRYIDTMGVANFVALADKYAHLGGLYQVTDAMRELAANNGSYYQA
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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B1LQP2
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HCHA_ECOSM
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Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
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MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG
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Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}.
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B1MK49
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PHY_MYCA9
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Phloretin hydrolase (EC 3.7.1.4) (mPhlG)
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MHPITYYPVDTQRLVRSNAERIRHKPYAHYFNPDVAVPEEVFAALKAPLEPEQVLGTSSTELNRLLEPGYLEGETGYCGLPDGAGYTSSLVRFPGATPEMFRWWFWWHSFEPERYSLWHPWCHADIWRTDPETETAPNLTDEQRYVGSTHHINEYIGQDPLDIEITFIDPARWGFDADGFAAAGIGAHACGSVLMKGSHMRLATMVHLARITDDGFELRSRYWIADRAEPRHDPVAGIAQLTTVPGFSGERQAYEQLVHDQTEFNHLATFLPDIYQEFGPR
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Catalyzes the hydrolytic C-C cleavage of phloretin to phloroglucinol and 3-(4-hydroxyphenyl)propionic acid. Can also hydrolyze monoacetylphloroglucinol (MAPG) but not 2,4-diacetylphloroglucinol (DAPG).
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B1MTB0
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HMGB1_PLEMO
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High mobility group protein B1 (High mobility group protein 1) (HMG-1)
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MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEDEEEDDDDE
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Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as danger associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance. Has proangiogenic activity. May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins. Nuclear functions are attributed to fully reduced HGMB1. Associates with chromatin and binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA, DNA-containing cruciforms or bent structures, supercoiled DNA and ZDNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity. May be involved in nucleotide excision repair (NER), mismatch repair (MMR) and base excision repair (BER) pathways, and double strand break repair such as non-homologous end joining (NHEJ). Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). In vitro can displace histone H1 from highly bent DNA. Can restructure the canonical nucleosome leading to relaxation of structural constraints for transcription factor-binding. Enhances binding of sterol regulatory element-binding proteins (SREBPs) such as SREBF1 to their cognate DNA sequences and increases their transcriptional activities. Facilitates binding of TP53 to DNA. May be involved in mitochondrial quality control and autophagy in a transcription-dependent fashion implicating HSPB1. Can modulate the activity of the telomerase complex and may be involved in telomere maintenance. In the extracellular compartment (following either active secretion or passive release) involved in regulation of the inflammatory response. Fully reduced HGMB1 (which subsequently gets oxidized after release) in association with CXCL12 mediates the recruitment of inflammatory cells during the initial phase of tissue injury the CXCL12:HMGB1 complex triggers CXCR4 homodimerization. Induces the migration of monocyte-derived immature dendritic cells and seems to regulate adhesive and migratory functions of neutrophils implicating AGER/RAGE and ITGAM. Can bind to various types of DNA and RNA including microbial unmethylated CpG-DNA to enhance the innate immune response to nucleic acids. Proposed to act in promiscuous DNA/RNA sensing which cooperates with subsequent discriminative sensing by specific pattern recognition receptors. Promotes extracellular DNA-induced AIM2 inflammasome activation implicating AGER/RAGE. Disulfide HMGB1 binds to transmembrane receptors, such as AGER/RAGE, TLR2, TLR4 and probably TREM1, thus activating their signal transduction pathways. Mediates the release of cytokines/chemokines such as TNF, IL-1, IL-6, IL-8, CCL2, CCL3, CCL4 and CXCL10. Promotes secretion of interferon-gamma by macrophage-stimulated natural killer (NK) cells in concert with other cytokines like IL-2 or IL-12. TLR4 is proposed to be the primary receptor promoting macrophage activation and signaling through TLR4 seems to implicate LY96/MD-2. In bacterial LPS- or LTA-mediated inflammatory responses binds to the endotoxins and transfers them to CD14 for signaling to the respective TLR4:LY96 and TLR2 complexes. Contributes to tumor proliferation by association with ACER/RAGE. Can bind to IL1-beta and signals through the IL1R1:IL1RAP receptor complex. Binding to class A CpG activates cytokine production in plasmacytoid dendritic cells implicating TLR9, MYD88 and AGER/RAGE and can activate autoreactive B cells. Via HMGB1-containing chromatin immune complexes may also promote B cell responses to endogenous TLR9 ligands through a B-cell receptor (BCR)-dependent and ACER/RAGE-independent mechanism. Inhibits phagocytosis of apoptotic cells by macrophages the function is dependent on poly-ADP-ribosylation and involves binding to phosphatidylserine on the cell surface of apoptotic cells. In adaptive immunity may be involved in enhancing immunity through activation of effector T-cells and suppression of regulatory T (TReg) cells. In contrast, without implicating effector or regulatory T-cells, required for tumor infiltration and activation of T-cells expressing the lymphotoxin LTA:LTB heterotrimer thus promoting tumor malignant progression. Also reported to limit proliferation of T-cells. Released HMGB1:nucleosome complexes formed during apoptosis can signal through TLR2 to induce cytokine production. Involved in induction of immunological tolerance by apoptotic cells its pro-inflammatory activities when released by apoptotic cells are neutralized by reactive oxygen species (ROS)-dependent oxidation specifically on Cys-106. During macrophage activation by activated lymphocyte-derived self apoptotic DNA (ALD-DNA) promotes recruitment of ALD-DNA to endosomes.
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B1NF19
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C719D_ARGME
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Trifunctional (S)-stylopine synthase/(S)-nandinine synthase/(S)-canadine synthase (STS) (EC 1.14.19.64) (EC 1.14.19.68) (EC 1.14.19.73) (Cytochrome P450 719A13)
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MEEKIMTNNSPWILTSSTTTTTTILLSLLFTIFIILRRNKSSSSKMVWPTGPKTLPIIGNMNILGGTALHVVLHNLAKTYGNVMTIWIGSWRPVIVVSDIDRAWEVLVNKSSDYSARDMPEITKLATADWKTISSSDSGPFWTNLRKGLQNVALSPQNLSSQSKFQERDIIKTIQNLKEEAKMNNGIVKPLDHLKKAMVRLISRLIYGQDFDNDEYVEEMHHTIEELIRVSGYARLAEAFYYAKYLPSHKKAVREVLQANQRVQNLVRPLLSLNSPTNTYLHFLRSQNYEDEVIIFAIFEAYLLGVDSTSSTTAWALAYLIREPNVQEKLYEELKNFTNDNDRKMVKFEDLNKLQYLQAVVKETMRMKPIAPLAIPHKACRETSLMGRKVNQGTRVMVNIYALHHNQNVWKEPYKFNPERFLQKNQDGVDGKAMEQSLLPFSAGMRICAGMELGKLQFSFALANLVNAFKWSCVSDGVFPDMSDQLGFVLLMKTPLEAGIVPRM
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Methylenedioxy bridge-forming cytochrome P450 involved in the biosynthesis of isoquinoline alkaloids. Converts (S)-cheilanthifoline to (S)-stylopine, (S)-scoulerine to (S)-nandinine and (S)-tetrahydrocolumbamine to (S)-canadine. Can be involved in both sanguinarine and berberine biosynthesis. Catalyzes an oxidative reaction that does not incorporate oxygen into the product.
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B1NWR6
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NA228_NEMVE
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N.vectensis toxin 1 3 (Nv1) (Delta-edwarditoxin-Nvc1c) (Delta-EWTX-Nvc1c) (Delta-edwarditoxin-Nvc1d) (Delta-EWTX-Nvc1d) (Neurotoxin Nv1-116.28.1) (Neurotoxin Nv1-13) (Neurotoxin Nv1-15) (Neurotoxin Nv1-17) (Neurotoxin Nv1-18) (Neurotoxin Nv1-19) (Neurotoxin Nv1-2) (Neurotoxin Nv1-4) (Neurotoxin Nv1-5) (Neurotoxin Nv1-8)
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MASFKIVIVCLALLVAVACARRRDMMSDDELDFHLSKRGIPCACDSDGPDIRSASLSGIVWMGSCPSGWKKCKSYYSIVADCCNQ
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Binds to site 3 of voltage-gated sodium channels and inhibits the inactivation process. Is highly active on DmNav1/TipE (drosophila) and is only extremely weakly active on rat Nav1.4-beta-1/SCN4A-SCN1B, and on human Nav1.5-beta-1/SCN5A-beta-1. This reveals high specificity for arthropod over mammalian channels. In vivo, when released into the medium, this recombinant toxin induces impaired swimming, paralysis and death of the crustacean A.nauplii within several hours. Also causes paralysis of cherry shrimps immediately after injection at very low doses. Its effect on zebrafish (D.rerio) larvae is also rapid, since it induces tail twitching accompanied by impaired swimming after 20 minutes and complete paralysis within 45 minutes. It has also been observed to cause death of zebrafish larvae within 1 hour.
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B1NWS4
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NA225_NEMVE
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N.vectensis toxin 1 1 (Nv1) (Delta-edwarditoxin-Nvc1b) (Delta-EWTX-Nvc1b) (Neurotoxin Nv1-10) (Neurotoxin Nv1-116.25.1) (Neurotoxin Nv3-2)
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MASFKIVIVCLALLVAVACARRRDMMSDDELDFHLSKRGIPCACDSDGPDIRSASLSGIVWMGSCPSGWKKCKSYYSIVADCCNQ
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Binds to site 3 of voltage-gated sodium channels and inhibits the inactivation process. Is highly active on DmNav1/TipE (drosophila) and is only extremely weakly active on rat Nav1.4-beta-1/SCN4A-SCN1B, and on human Nav1.5-beta-1/SCN5A-beta-1. This reveals high specificity for arthropod over mammalian channels. In vivo, when released into the medium, this recombinant toxin induces impaired swimming, paralysis and death of the crustacean A.nauplii within several hours. Also causes paralysis of cherry shrimps immediately after injection at very low doses. Its effect on zebrafish (D.rerio) larvae is also rapid, since it induces tail twitching accompanied by impaired swimming after 20 minutes and complete paralysis within 45 minutes. It has also been observed to cause death of zebrafish larvae within 1 hour.
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B1P1D9
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JZ11F_CHIGU
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Kappa-theraphotoxin-Cg1a 6 (Kappa-TRTX-Cg1a) (Jingzhaotoxin-11.6) (JZTX-11.6) (Jingzhaotoxin-XI.6) (JZTX-XI.6) (Peptide F4-13.64)
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MKVSVLITLAVLGVMFVWASAAELEERGSDQRDSPAWLKSMERIFQSEERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK
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This toxin acts as a voltage-dependent gating-modifier. It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A. It significantly shifts the activation to more depolarized voltages and decreases the deactivation of Nav1.5 currents upon extreme depolarization, but only slightly affects voltage-dependence of steady-state inactivation. In addition, this toxin causes an approximately five-fold decrease in the rate of recovery from inactivation and an approximately 1.9-fold reduction in the closed-state inactivation rate. This toxin integrates the functions of site 3 toxins (alpha-scorpion toxins) with site 4 toxins (beta-scorpion and spider toxins) by targeting multiple sites on Nav1.5. Also shows inhibition of voltage-gated potassium channels (5 uM completely inhibits Kv2.1/KCNB1, whereas 5 uM moderately inhibits Kv4.2/KCND2 Kv4.1/KCND1 channels).
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B1P1E0
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JZ11C_CHIGU
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Kappa-theraphotoxin-Cg1a 3 (Kappa-TRTX-Cg1a) (Jingzhaotoxin-11.3) (JZTX-11.3) (Jingzhaotoxin-XI.3) (JZTX-XI.3) (Peptide F4-13.64)
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MKVSVLITLAVLGVMFVWASAAELEERGSDQRDSPAWLKSMERIFRSEERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK
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This toxin acts as a voltage-dependent gating-modifier. It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A. It significantly shifts the activation to more depolarized voltages and decreases the deactivation of Nav1.5 currents upon extreme depolarization, but only slightly affects voltage-dependence of steady-state inactivation. In addition, this toxin causes an approximately five-fold decrease in the rate of recovery from inactivation and an approximately 1.9-fold reduction in the closed-state inactivation rate. This toxin integrates the functions of site 3 toxins (alpha-scorpion toxins) with site 4 toxins (beta-scorpion and spider toxins) by targeting multiple sites on Nav1.5. Also shows inhibition of voltage-gated potassium channels (5 uM completely inhibits Kv2.1/KCNB1, whereas 5 uM moderately inhibits Kv4.2/KCND2 Kv4.1/KCND1 channels).
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B1P1E1
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JZ11B_CHIGU
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Kappa-theraphotoxin-Cg1a 2 (Kappa-TRTX-Cg1a) (Jingzhaotoxin-11.2) (JZTX-11.2) (Jingzhaotoxin-XI.2) (JZTX-XI.2) (Peptide F4-13.64)
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MKVSVVITLAVLGVMFVWASAAELEERGSDQRDSPAWLKSMERIFQSEERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK
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This toxin acts as a voltage-dependent gating-modifier. It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A. It significantly shifts the activation to more depolarized voltages and decreases the deactivation of Nav1.5 currents upon extreme depolarization, but only slightly affects voltage-dependence of steady-state inactivation. In addition, this toxin causes an approximately five-fold decrease in the rate of recovery from inactivation and an approximately 1.9-fold reduction in the closed-state inactivation rate. This toxin integrates the functions of site 3 toxins (alpha-scorpion toxins) with site 4 toxins (beta-scorpion and spider toxins) by targeting multiple sites on Nav1.5. Also shows inhibition of voltage-gated potassium channels (5 uM completely inhibits Kv2.1/KCNB1, whereas 5 uM moderately inhibits Kv4.2/KCND2 Kv4.1/KCND1 channels).
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B1P1E2
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JZ11D_CHIGU
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Kappa-theraphotoxin-Cg1a 4 (Kappa-TRTX-Cg1a) (Jingzhaotoxin-11.4) (JZTX-11.4) (Jingzhaotoxin-XI.4) (JZTX-XI.4) (Peptide F4-13.64)
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MKASVLITLAVLGVMFVWASAAELEERGSDQRDSPAWLKSMERIFQSEERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK
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This toxin acts as a voltage-dependent gating-modifier. It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A. It significantly shifts the activation to more depolarized voltages and decreases the deactivation of Nav1.5 currents upon extreme depolarization, but only slightly affects voltage-dependence of steady-state inactivation. In addition, this toxin causes an approximately five-fold decrease in the rate of recovery from inactivation and an approximately 1.9-fold reduction in the closed-state inactivation rate. This toxin integrates the functions of site 3 toxins (alpha-scorpion toxins) with site 4 toxins (beta-scorpion and spider toxins) by targeting multiple sites on Nav1.5. Also shows inhibition of voltage-gated potassium channels (5 uM completely inhibits Kv2.1/KCNB1, whereas 5 uM moderately inhibits Kv4.2/KCND2 Kv4.1/KCND1 channels).
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B1P1E3
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JZ11E_CHIGU
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Kappa-theraphotoxin-Cg1a 5 (Kappa-TRTX-Cg1a) (Jingzhaotoxin-11.5) (JZTX-11.5) (Jingzhaotoxin-XI.5) (JZTX-XI.5) (Peptide F4-13.64)
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MKVSVLITLAVLGVMFVWTSAAELEERGSDQRDSPAWLKSMERIFQSEERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK
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This toxin acts as a voltage-dependent gating-modifier. It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A. It significantly shifts the activation to more depolarized voltages and decreases the deactivation of Nav1.5 currents upon extreme depolarization, but only slightly affects voltage-dependence of steady-state inactivation. In addition, this toxin causes an approximately five-fold decrease in the rate of recovery from inactivation and an approximately 1.9-fold reduction in the closed-state inactivation rate. This toxin integrates the functions of site 3 toxins (alpha-scorpion toxins) with site 4 toxins (beta-scorpion and spider toxins) by targeting multiple sites on Nav1.5. Also shows inhibition of voltage-gated potassium channels (5 uM completely inhibits Kv2.1/KCNB1, whereas 5 uM moderately inhibits Kv4.2/KCND2 Kv4.1/KCND1 channels).
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B1P1F5
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JZT32_CHIGU
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U18-theraphotoxin-Cg1a (U18-TRTX-Cg1a) (Jingzhaotoxin-32) (JZTX-32) (Jingzhaotoxin-9) (JzTx-9) (Jingzhaotoxin-IX) (JzTx-IX) (Peptide F6-16.24)
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KASVLITLAVLGVMFVWTSAAELEERGSDQRDSPALIKSMAKVFQSEERECTKLLGGCTKDSECCPHLGCRKKWPYHCGWDGTFGK
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Inhibits TTX-sensitive and TTX-insensitive sodium currents (IC(50) is 0.6 uM and 0.95 uM respectively) on rat dorsal root ganglion (DRG) neurons. Inhibits muscular subtypes sodium channels Nav1.4/SCN4A and Nav1.5/SCN5A transiently transfected in to HEK293 cells (IC(50) is 5.42 uM and 0.45 uM respectively). Also blocks Kv2.1/KCNB1 potassium channels expressed in X.laevis oocytes with an IC(50) of 604 nM. Injection of the toxin in mice was immediately followed by general ataxia, lack of response to stimuli and semiparalysis.
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B1PRL5
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CAVN4_RAT
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Caveolae-associated protein 4 (Muscle-related coiled-coil protein) (Muscle-restricted coiled-coil protein)
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MEHNGSASNAGKIHQNRLSSVTEDEDQDAALTIVTVLDRVATVVDSVQASQKRIEERHREMGNAIKSVQIDLLKLSQSHSNTGYVVNKLFEKTRKVSAHIKDVKARVEKQQVRVTKVETKQEEIMKKNKFRVVIFQEDVPCPASLSVVKDRSLPENEEEAEEVFDPPIDLSSDEEYYVEESRSARLRKSGKEHIDHIKKAFSKENMQKTRQNFDKKVSGIRTRIVTPERRERLRQSGERLRQSGERLRQSGERFKKSISNATPSKEAFKIRSLRKPKDPKAEGQEVDRGMGVDIISGSLALGPIHEFHSDGFSETEKEVTKVGYIPQEGGDPPTPEPLKVTFKPQVRVEDDESLLLELKQSS
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Modulates the morphology of formed caveolae in cardiomyocytes, but is not required for caveolar formation. Facilitates the recruitment of MAPK1/3 to caveolae within cardiomyocytes and regulates alpha-1 adrenergic receptor-induced hypertrophic responses in cardiomyocytes through MAPK1/3 activation. Contributes to proper membrane localization and stabilization of caveolin-3 (CAV3) in cardiomyocytes (By similarity). Induces RHOA activation and activates NPPA transcription and myofibrillar organization through the Rho/ROCK signaling pathway.
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B1PVZ9
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KARG_METEN
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Arginine kinase Met e 2 (AK) (EC 2.7.3.3) (allergen Met e 2)
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MADAAVIEKLEAGFKKLEAATDCKSLLKKYLTKEVFDKLKDKKTSLGATLLDVIQSGVENLDSGVGIYAPDAEAYTLFAPLFDPIIEDYHVGFKQTDKHPNKDFGDVNSFVNVDPEGKFVISTRVRCGRSMQGYPFNPCLTESQYKEMEAKVSSTLSSLEGELKGTYYPLTGMSKEVQQKLIDDHFLFKEGDRFLQAANACRYWPAGRGIYHNDNKTFLVWVNEEDHLRIISMQMGGDLGQVFRRLTSAVNEIEKRIPFSHHDRLGFLTFCPTNLGTTVRASVHIKLPKLAANREKLEEVAGKYNLQVRGTRGEHTEAEGGIYDISNKRRMGLTEFQAVKEMQDGILELIKIEKEMI
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Catalyzes the reversible transfer of high energy ATP gamma-phosphate group to L-arginine.
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B1Q005
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MBOA4_RAT
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Ghrelin O-acyltransferase (EC 2.3.1.-) (Membrane-bound O-acyltransferase domain-containing protein 4)
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MDWLQFFFLHPVSLYQGAAFPFALLFNYLCITESFPTRARYLFLLAGGGVLALAAMGPYALLIFIPALCAVAMISSLSPQEVHGLTFFFQMGWQTLCHLGLHYKEYYLCEPPPVRFYITLSSLMLLTQRVTSLSLDISEGKVEAAWRGTRSRSSLCEHLWDALPYISYLLFFPALLGGSLCSFQRFQACVQRPRSLYPSISFWALTWRGLQILGLECLKVALRRVVSAGAGLDDCQRLECIYIMWSTAGLFKLTYYSHWILDDSLLHAAGFGSEAGQRPGEERYVPDVDIWTLETTHRISLFARQWNRSTAQWLKRLVFQRSRRWPVLQTFAFSAWWHGLHPGQVFGFLCWSVMVKADYLIHTFANGCIRSWPLRLLYRSLTWAHTQIIIAYVMLAVEGRSFSSLCRLCCSYNSIFPVTYCLLLFLLARRKHKCN
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Catalyzes ghrelin acylation at 'Ser-3' using preferentially octanoyl-CoA, hexanoyl-CoA and decanoyl-CoA as acyl-CoA donors leading to ghrelin activity (By similarity). In vitro uses also acyl-CoA donors of different lengths from short-chain (C2) to long-chain fatty acids (C16) knowing that acyl-CoA donors from butanoyl-CoA (C4) to dodecanoyl-CoA (C12) are more efficient compared to longer acyl-CoA donors, such as myristoyl-CoA (C14) and palmitoyl-CoA (C16) that are not efficient (By similarity).
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B1Q006
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MBOA4_DANRE
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Ghrelin O-acyltransferase (EC 2.3.1.-) (Membrane-bound O-acyltransferase domain-containing protein 4)
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MIDLLWISSDGHPQLFYQFINIPFAFLFHCLSSQGHLSIINRYVYLAMGGFMLAIATMGPYSSLLFLSAIKLLLLIHYIHPMHLHRWILGLQMCWQTCWHLYVQYQIYWLQEAPDSRLLLAISALMLMTQRISSLSLDFQEGTISNQSILIPFLTYSLYFPALLGGPLCSFNAFVQSVERQHTSMTSYLGNLTSKISQVIVLVWIKQLFSELLKSATFNIDSVCLDVLWIWIFSLTLRLNYYAHWKMSECVNNAAGLGVYFHKHSGQTSWDELSDGSVLVTEASSRPSVFARKWNQTTVDWLRKIVFNRTSRSPLFMTFGFSALWHGLHPGQILGFLIWAVTVQADYKLHRFSHPKLNSLWRKRLYVCVNWAFTQLTVACVVVCVELQSLASVKLLWSSCIAVFPLLSALILIIL
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Catalyzes ghrelin acylation at 'Ser-3' using preferentially octanoyl-CoA, hexanoyl-CoA and decanoyl-CoA as acyl-CoA donors leading to ghrelin activity (By similarity). In vitro uses also acyl-CoA donors of different lengths from short-chain (C2) to long-chain fatty acids (C16) knowing that acyl-CoA donors from butanoyl-CoA (C4) to dodecanoyl-CoA (C12) are more efficient compared to longer acyl-CoA donors, such as myristoyl-CoA (C14) and palmitoyl-CoA (C16) that are not efficient (By similarity).
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B1Q236
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SYG1_CAEEL
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Synaptogenesis protein syg-1 (Synaptogenesis abnormal protein 1)
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MVRWQTWPLLLLFQLVTCQQLQQRIVEAPKDTLAAVGETAILTCRVEHQQGPVQWMKDDFGLGTDRDKPLPGNKRYRMVGSAANGEYNLEISNVTLFDDDDFACQISESDHAKAVVSSKAKLTVLVRPTPPKIVKSHHSLKAIAGDPITQSCLSRKGKPPPTIGWAIASDEHGKHIVSWLGESRSKFGGIHAKPEISQETVIAHVNETTQVEEGGNNSREDSSIYSIMSNLSFIPRPEDDHKYLICISQHMTFPNKIEVDSVKLSLRYAPQINLTVASKLPLRENGSALLACNVNAKPLDNVKISWYKGNQKLRETGDTLTFETLKMEDHNRDIFCEATNEIGTTRGSIKLNVAFGARIMSTSQDKEVNEGDNAFFHCATLANPAPAIFWTRGDSDEIIGHGENLTLENVRTWQQGNYNCTATVEGFRKQILSHYLHIRGPPTVSMKDEVSASLDEATEIICEISGRPKTNNVRWTVNGKEINFNNGRITVHQYPKPYGKESILKIKDLKEEDFGVYNCSANNGLGFDNRGTLLKKRNILDWIVITAKFDRMVALAIISAGVLLVSLLCCLCMCRSNCRSRKSKFIDDQSDVTVKCEALDGQYFPEMYSSSPVDNVHLSTKDYISIPQNNPDLDFLGATGSFGPPGGLYPKCFNNSANEYIYNRYEHSYGSFGSGLSTPGGVSDMYGVAMSDKLPVMETLQEVETPKTSNYNFLSSPEVVRPISRTSTHV
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Cell adhesion protein. Involved in synapse formation in the HSNL egg-laying motor neuron. Inhibits assembly of the SCF(sel-10) E3 ubiquitin ligase complex at synapses, and protects them from elimination. Also required for F-actin assembly at the synaptic region and for axon branch formation.
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B1Q257
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GCY10_CAEEL
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Receptor-type guanylate cyclase gcy-10 (EC 4.6.1.2) (Odorant response abnormal protein 1)
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MLKSLLIIVIVFLHRELCDGIQLILFDNWPSAQNVCASAVADATANGQCTTKSIQKHLELLTVIILLKLFGVFHRINQQHGCSGDNSVKSASYAINAVASRTSGELDFVFVGPTCTTDIRTIGDFAEIWKSPVIGYEPVFEARGVQELTSVINVAQFSVGGVAETLVFLMKELEQVEITLVGSVKVLPNGLSLSNDLRSYNEIMNSFKIREYVEVDENDVDWTKVDQKIKRGARMIVVCADFYDIYSAFYNIGIRSLSGFRFIIVVILNKPPDEILNQPNVKNLLYGSNAFIISPLQEQYSDAFSIMQDVIPNLADDQFTTFLRIYHACYAYCVGSVNGAETQTDNYHTAMSGKAVTTKYGTFTFDNSGSVLTNYAVFTINPAEMTFESILTLKSVAKSCDTYNCFQLSPNKTSDLLWTLKDMDPPDDCVAKSSCVNYIPHIIAAVVIVTIIVIAIVIIVKQRRHKLNIYKLTWKVPKESLKIIVNKNADAKMQRELENRASNTDNAAALTSRRRVFGSYALVGTQRAEYVQFKQIRKINFPETTLDYLYSLKQLQHDNLAKFYGIQVNDDIMTMTILHTLVERGTLEEFCLDRDFGMDDTFKSAFMRDILKGLQYLHKSSIGYHGHLQASTCLIDINWVLKLTLYGVSNFMSDQLDAENIKVPEQAAHMITYPQYVCFPPEHIREYDDSGKQPPRVVRGSPKGDIYCVGMIFYMMVEREDPYHLIHSVERPNATLIKQILNENHMPRITDDYRQENMLLEMCKECWDRNPDKRPTIKKLIESISTVYPLSKGNLVDQMIRMSEKYADELEQMVAIRTADLADAQMQTMRLLNEMLPASIAKDLKNGLIMPPRSYESATVMFVQICDFNALMKRSSPEQVIAFLNDIYDQFDTVIKRHDAYKVETTGETYMVASGVPHENEGRHIFEVAEISLEIREISYIYVLQHDKNYKLRIRIGFHAGPIAAGVIGIRSPRYCLFGDTVNFASRMQSNCPPNQIQTSEITARLLFDSHEYKFVKRGIVHVKGKGEVNCYWLNEHLHEETEPPLPPMTPVPNPLRRGSIVPLQKA
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Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). Regulates chemotaxis responses toward volatile odorants in AWC sensory neurons and their avoidance in AWB sensory neurons. May be involved in sensitivity to quinine by regulating egl-4 activity through the production of cGMP. Involved in phototransduction in ASJ neurons downstream of G protein coupled-photoreceptor lite-1. Required to maintain the expression of putative olfactory receptor str-2 in AWC neurons in adults. In AWB and AWC sensory neurons, mediates the recognition of food oders which subsequently allows for the detection of preferred food sources. Involved in AWB sensory neuron development and extension during postembryonic development, potentially via mediating localization of tub-1 and PI(4,5)P2 to membrane cilia.
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B1Q2B6
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OLIS_CANSA
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3,5,7-trioxododecanoyl-CoA synthase (EC 2.3.1.206) (Olivetol synthase) (EC 4.4.1.-) (Polyketide synthase-1) (Tetraketide synthase)
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MNHLRAEGPASVLAIGTANPENILLQDEFPDYYFRVTKSEHMTQLKEKFRKICDKSMIRKRNCFLNEEHLKQNPRLVEHEMQTLDARQDMLVVEVPKLGKDACAKAIKEWGQPKSKITHLIFTSASTTDMPGADYHCAKLLGLSPSVKRVMMYQLGCYGGGTVLRIAKDIAENNKGARVLAVCCDIMACLFRGPSESDLELLVGQAIFGDGAAAVIVGAEPDESVGERPIFELVSTGQTILPNSEGTIGGHIREAGLIFDLHKDVPMLISNNIEKCLIEAFTPIGISDWNSIFWITHPGGKAILDKVEEKLHLKSDKFVDSRHVLSEHGNMSSSTVLFVMDELRKRSLEEGKSTTGDGFEWGVLFGFGPGLTVERVVVRSVPIKY
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Involved in the biosynthesis of cannabinoids-related terpenophenolic natural products, which have pharmacological activity. Polyketide synthase responsible for olivetol biosynthesis, from a C(12)-polyketide, probably 3,5,7-trioxododecanoyl-CoA (PubMed:19454282, Ref.3). Catalyzes the first step in the cannabinoids biosynthetic pathway. The preferred substrate is hexanoyl-CoA, but accepts also CoA esters with C4 to C8 aliphatic side chains. When using malonyl-CoA and hexanoyl-CoA as substrates, produces undetermined compounds distinct form olivetol or olivetolic acid that could be hexanoyl triacetic acid lactone (HTAL) and pentyl diacetic acid lactone (PDAL). Produces olivetolic acid when acting in concert with olivetolic acid cyclase (OAC).
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B1Q3J6
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DNM1B_ORYSJ
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DNA (cytosine-5)-methyltransferase 1B (OsMET1b) (EC 2.1.1.37) (DNA methyltransferase 1-2) (OsMET1-2)
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MVKSPCSPVTTGKKRCRAKPQKKDEDTTDKGKLDEGPLDATKEMNGVGKGDSRAACKRPRRAAACSDFKEKSVRLSDKSSVVATNGNKMEEEEMDAVKLTKLGPEVQRPCRKLIDFILHDADGKLQPFEMSEIDDFFITALIMPMDDDLEKDRQKGVRCEGFGRIEDWAISGYDEGTAVVWVSTEVADYECVKPAGNYKSYYDHFYEKAQVCVEVYRKLARSVGGNPNLGLEELLASVVRSINAIKGYSGTLSKDFVISNGEFVYNQLIGLDETANTDDEKFATLPVLLALRDGCKSRVEVSKLQPNISNGSLKINDAECKEVSEDDDEKLARLLQQEEEWKMMKQRGKRGTTSQKNVYIKISEAEIANDYPLPAYYKPSSQEMDEYIFDSEDSFYSDVPVRILNNWALYNADSRLIPLELIPMKAGAENDIVVFGSGFMREDDGSCCSTAESAKLSSSSSSNHQDAGVSIYLSPIKEWVIEFGGSMICITIRTDVAWYKLRQPTKQYAPWCEPVLKTARLSVSIITLLKEQSRASKLSFADVIKKVAEFDKGSPAFVSSNVALVERYIVVHGQIILQQFSDFPDETIRRSAFATGLLMKMEQRRHTKLVMKKKVQVMRGENLNPSATMGPASRRKVMRATTTRLINRIWSDYYTHHFPEDSKDADVNEAKEIDDELEENEDEDAEEEAQIEEENVSKTPPSTRSRKLVSQTCKEIRWEGEAIGKTPSGEALYKCAYVRELRINLGRTVALEDDSGELVMCFVEYMFQKLNGAKMVHGRLLQKGSETVLGNAANERDLFLTNECLEFELEDIKELMSVNLQSLPWGHKYRKENAEADRIERAKAEDRKKKGLPMEYLCKSLYWPEKGAFFSLPHDKLGLGNGFCSSCQQKEPDCDELQILSKNSFIYRNITYNVNDYLYIRPDFFSQEEDRATFKGGRNVGLKPYVVCHLLDVHEPAGSRKIHPASTKISVRRFYRPDDISSAKAYVSDIREVYYSENIVKVPVDMIEGKCEVKKKIDISNSDVPVMVEHEFFCEHFYDPATGALKQLPPNVKLMSVQQKATGALKKNKGKQICESDQVDSDKCTKVSKENRLATLDIFAGCGGLSEGLQQAGVSFTKWAIEYEEPAGEAFTKNHPEAAVFVDNCNVILKAIMDKCGDADDCISTSEAAEQAAKFSQDNIMNLPVPGEVEFINGGPPCQGFSGMNRFNQSPWSKVQCEMILAFLSFAEYFRPRFFLLENVRNFVSFNKGQTFRLTVASLLEMGYQVRFGILEAGTFGVAQSRKRAFIWAAAPGETLPDWPEPMHVFASPELKINLPDGKYYAAAKSTAGGAPFRAITVRDTIGDLPKVENGASKLLLEYGGEPISWFQKKIRGNTIALNDHISKEMNELNLIRCQRIPKRPGCDWHDLPDEKVKLSSGQLVDLIPWCLPNTAKRHNQWKGLYGRLDWEGNFPTSVTDPQPMGKVGMCFHPDQDRIITVRECARSQGFPDNYQFAGNIQSKHRQIGNAVPPPLAFALGRKLKEAVDAKRQ
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Major CG methylase that methylates chromatin CpG residues and maintains DNA methylation. Plays a major role in genomic imprinting, regulation of embryogenesis and seed viability. Maintains DNA methylation at the FIE1 gene locus in the embryo.
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B1V8A0
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SH3GH_CAEEL
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Endophilin-A homolog (Endophilin-1 homolog) (Uncoordinated protein 57)
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MSLSGLRKQFNKANQYLSETMGAAEPTKLDDVFNEMEKNVDTTYNLITDLVAGTNEYLQPNPATRAKMATQVALSKVRGTTKTSPYPQTEGMLADVMQKYGQQLGDNSDLGKSLNDAAETYRQMADIKYQMEDNVKQNFLDPLTHLQNNELKDVNHHRTKLKGRRLDYDCKKRQQRRDDEMIQAEEKLEESKRLAEMSMFNVLSNDVEQISQLRALIEAQLDFHRQTAQCLENLQQQLGHRIKDAAARPREEHVPLSVLANESRTPRSSFRSPAPSDMSHNSTAAAAFKMPPQNGGGITQAPPSYQGPPPGGLPPPLSQQQKPQCRALFDFDAQSEGELDFKEGTLIELVSQIDENWYEGRVNGKTGLFPVTYVQVLVPLK
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Involved in synaptic vesicle (SV) recycling in neurons probably by regulating clathrin-mediated endocytosis. By controlling SV endocytosis, regulates the rate of excitatory postsynaptic currents (EPSCs) at neuromuscular junctions and thus locomotion. In a similar manner, involved in necrotic neuronal cell death induced by abnormal hyperactivation of ion channels. Plays a minor role in responses to mechanical stimuli. Plays a minor role in unc-26/synaptojanin localization to synapses.
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B1VB63
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PDUB_CITFR
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Bacterial microcompartment shell protein PduB (Bacterial microcompartment protein homotrimer) (BMC-T) (Propanediol utilization protein PduB)
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MSSNELVDQIMAQVIARVATPEQQAIPENNPPTRETAMAEKSCSLTEFVGTAIGDTVGLVIANVDSALLDAMKLEKRYRSIGILGARTGAGPHIMAADEAVKATNTEVVSIELPRDTKGGAGHGSLIILGGNDVSDVKRGIEVALKELDRTFGDVYANEAGHIEMQYTARASYALEKAFGAPIGRACGVIVGAPASVGVLMADTALKSANVEVVAYSSPAHGTSFSNEAILVISGDSGAVRQAVISAREIGKTVLGTLGSEPKNDRPSYI
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The two proteins produced are among the major shell proteins of the bacterial microcompartment (BMC) shell dedicated to 1,2-propanediol (1,2-PD) degradation. Overexpression of the gene gives large amorphous intracellular structures when only PduB is overexpressed large circular bodies are observed which contain concentric rings, whereas with PduB' overexpression internal bodies with regular straight-lined structures were generated. The N-terminus of the long form (PduB) is required for correct formation of BMCs. May play a major role in binding the enzyme contents to the shell (By similarity). Expression of a cosmid containing the full 21-gene pdu operon in E.coli allows E.coli to grow on 1,2-propanediol (1,2-PD) with the appearance of BMCs in its cytoplasm. The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low.
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B1VB77
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PDUS_CITFR
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Cobalamin reductase PduS (Corrin reductase) (Propanediol utilization protein PduS)
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MKTAMTAESTLYDAQTIRERVRAAGVVGAGGAGFPAHVKLQAQVDTFLVNAAECEPMLKVDQQLMAVQAERLIRGVQYAMTATGARAGIIALKEKYQRAINALTPLLPAGIRLHILPDVYPAGDEVLTIWMATGRRVPPAALPVSVGVVVNNVQTVLNITRAVEQQYPVTRRTLTVNGAVARPITLTVPIGMSLREVLALAGGATVDDPGFINGGPMMGGLITSLDTPVSKTTGGLLVLPKSHALIQRRMQDERTVLSVAKTVCEQCRLCTDLCPRHLIGHELSPHLLVRAVNYQQAATPQLLLTALTCSECNVCESVACPVGISPMRINRMLKRELRALNHRYEGPLNPEDEMAKYRLIPVKRLITKLGLSDWYHDAPLTETDYPTDKTTLLLRQHIGASAIPCVLQGEHVVRGQCVADVPSGALGAPVHASIDGIVSEITEQSITVIRG
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A bifunctional cobalamin reductase that converts cob(III)alamin to cob(II)alamin and then to cob(I)alamin in the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. PduS and PduO allow regeneration of the adenosylcobalamin cofactor within the BMC. Cobalamin reduction probably occurs spontaneously in the presence of free reduced flavin nucleotides, this protein may be involved in electron transfer for this reduction (By similarity). Expression of a cosmid containing the full 21-gene pdu operon in E.coli allows E.coli to grow on 1,2-propanediol (1,2-PD) with the appearance of BMCs in its cytoplasm. The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low.
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B1VTI5
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GRIF_STRGG
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Grixazone synthase (EC 1.10.3.15) (Phenoxazinone synthase) (PHS) (o-aminophenol oxidase) (EC 1.10.3.4)
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MVHVRKNHLTMTAEEKRRFVHAVLEIKRRGIYDRFVKLHIQINSTDYLDKETGKRLGHVNPGFLPWHRQYLLKFEQALQKVDPRVTLPYWDWTTDHGENSPLWSDTFMGGNGRPGDRRVMTGPFARRNGWKLNISVIPEGPEDPALNGNYTHDDRDYLVRDFGTLTPDLPTPQELEQTLDLTVYDCPPWNHTSGGTPPYESFRNHLEGYTKFAWEPRLGKLHGAAHVWTGGHMMYIGSPNDPVFFLNHCMIDRCWALWQARHPDVPHYLPTVPTQDVPDLNTPLGPWHTKTPADLLDHTRFYTYDQ
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Involved in the biosynthesis of the parasiticide antibiotic grixazone. Catalyzes the oxidation of 3-amino-4-hydroxybenzoate (3,4-AHBOA) to yield the corresponding quinone imine which is then non-enzymatically conjugated with the thiol group of N-acetylcysteine. The resultant compound is oxidized to its quinone imine enzymatically and is then dimerized non-enzymatically with another quinone imine oxidized by GriF to yield grixazone B. 3-amino-4-hydroxybenzaldehyde (3,4-AHBAL) can also be used as substrate to yield grixazone A. In the grixazone biosynthetic pathway, it can also function as an o-aminophenol oxidase that catalyzes the formation of the phenoxazinone chromophore from alpha-aminophenol. It can also use 2-amino-4-methylphenol, and to a lesser extent, 3,4-dihydroxybenzaldehyde, catechol and 3,4-dihydroxy-L-phenylalanine (L-DOPA) as substrates. In contrast to tyrosinases, it does not display monophenolase activity.
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B1W019
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GCOA_STRGG
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(+)-caryolan-1-ol synthase (EC 4.2.1.138) ((+)-beta-caryophyllene synthase) (EC 4.2.3.89)
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MSQITLPAFHMPFQSAGCHPGLAETREAAWEWAAAEGLDLSVPARRKMIRTRPELWISLIFPQATQAHLDLFCQWLFWAFLVDDEFDDGPAGRDPLMCERAIARLVDVFDGAAPNGPMERALAGLRDRTCRGRSPQWNRQFRRDTAAWLWTYYAEAVERAAGQVPSRAEFAKHRRDSVAMQPFLCLHEITAGIDLPDSARSLPAYIALRNAVTDHSGLCNDICSFEKEAALGYEHNAVRLIQRDRGSTLQEAVDEAGIQLARIAERVQRAERELIEEIEAAGIDGPTRTALERCVRDYRGLVRGDFDYHARAERYTRPDLVELDERDSLSRHFAA
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Sesquiterpene cyclase that first catalyzes the cyclization of farnesyl diphosphate (FPP) to the bicyclic sesquiterpene (+)-beta-caryophyllene intermediate, and then its conversion to (+)-caryolan-1-ol via a second cyclization and the addition of a water molecule.
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B1WAR9
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GWL_XENTR
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Serine/threonine-protein kinase greatwall (GW) (GWL) (EC 2.7.11.1) (Microtubule-associated serine/threonine-protein kinase-like) (MAST-L)
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MGVVVAETSQNGDISLLSEKKFTVPQPPSIEEFSIVKPISRGAFGKVYLARRKNNNKLFAVKVVKKADMINKNMVQQVQAERDALALSKSPFIVHLYYSLQSANNIYLIMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLKRELSMMDILTTPSMAKPKRDYSRTPGQVLSLISSLGFNTPVGGRTQGSIAQQTEGMRGNASTPLLMKKKENSVKGNKLMISCPEAGLSSPSMPVKCLTPNLLKCRTPFTTSSTSSQSRICLSSLESECGMSPRWENCSQDAEAPPYLNSSRVKDCSSEQARSKKPMGSSASQNLKHLEFAFSPIVDRRTGKKAGFQDETGELSDTPLATLGAKGVIRKCLYDNNAQEKHKDLGKDDQGELEKLTISPDSPPWLANGSVAPIQFNDDEIIEKMGIKRNYDLVEKSPEQEVLQDKKTNTDYKRGCTITGYPVSQSTGLTMEINSLFLSELRSSTNNYASDRKSEDDYISAPRTHENLGSGNTIAKNLLCELDDNCERDGEANSNSGCEEGENQKESLNQDSESSSADMSVTENQIERELCQVDKSIKELSFEESPSESNEETTPENKGMAFMAENDALKREPNRSVLPETLHNVLASPAPTSAMAHPRRKPMVAFRSYNSPINGSNLSEPSRISMNSADKIHFSLGCTGSFPMAVTPAQKKVQGLTETPYRTPKTVRRGGLQAENERILGTPDYLAPELLLGKSHGPAVDWWALGVCLFEFLTGIPPFNDETPSQVFQNILNRDIPWPEEEETLSVNAQSAIEILLAIDQTKRAGLKDLKAHHLFHAIEWDDLQNLPMPFIPQPDDETDTTYFEARNNAQHLKVSGFSL
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Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of arpp19 and ensa at 'Ser-67', 2 phosphatase inhibitors that specifically inhibit the ppp2r2d (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited (By similarity).
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B1WBP0
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MPPD2_RAT
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Metallophosphoesterase MPPED2 (EC 3.1.-.-) (239FB) (Fetal brain protein 239 homolog) (Metallophosphoesterase domain-containing protein 2)
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MAHGIPSQGKVTITVDEYSSNPTQAFTHYNINQSRFQPPHVHMVDPIPYDTPKPAGHTRFVCISDTHSRTDGIQMPYGDILLHTGDFTELGLPSEVKKFNDWLGNLPYEYKIVIAGNHELTFDKEFMADLVKQDYYRFPSVSKLKPEDFDNVQSLLTNSIYLQDSEVTVKGFRIYGAPWTPWFNGWGFNLPRGQSLLDKWNLIPEGTDILMTHGPPLGFRDWVPKELQRVGCVELLNTVQRRVRPKLHVFGGIHEGYGTMTDGYTTYINASTCTVSFQPTNPPIIFDLPNPQGS
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Displays low metallophosphoesterase activity (in vitro). May play a role in the development of the nervous system (Probable).
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B1WC10
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FRITZ_RAT
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WD repeat-containing and planar cell polarity effector protein fritz homolog (WD repeat-containing and planar cell polarity effector protein)
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MSFCLTELHLWSLKSTLHIADRDIGVYQYYDKKDLPVSAAEHGNLEEKQRLAESRDYPWTLKNRRPEKLRDSLKELEELMQNSQCVLCQWKSKHICQLLFGSGVLVSLSLSGPQLEKVVIDRSLVGKLISDTISDALLTDSFIILSFLAQNKLCFIQFAKKMDSLDVNKRLEKLSALDYKISYHDIPGPATRTVDRHLAINSTQDLAVCWWPLLSDDAWPWTPIASEKDRANMLLLGFTQGGLEVLSSVRTEWNPLDVHFGTRQPYQVFTVECSFSVDQEPMADSCIYESVRNKLHCVSVTRIPLRSKAISCCKNSTEDKLIVGCEDSSVILYEAHRGVTLLAQAELMPSLISCHPSGAILLVGSNQGELQVFDIALSPINIQLLAEDCLPKETLQFNKFFDFSSSLVHMQWIAPPIVFQKPKRGEICDLLFLRFNRGPLGVLLFKLGVLRRGQLGLVDLIFQYIHCDEVYEAVSVLSSMNWDTLGQQCFISMSTIVNHLLRQRLTPEREAQLEASLGTFYAPARPLLDTTVLAYRDPVGTYARRLFHHLLRYQRFEKAFLLAVDIGARDLFMDIHYLALDMGELALAEVARRRADDIDVESVCSGVELLGPLDRRDMLNEGFAGSALTPEGGNPFPDLLPSSGSTPKHTIQQKIPNGPSNRRAIERKNEVMEETEEEEEEEEEAAACTDSSVATTWDAEGELREDHRRQDTEDVGSLRMVHFGLV
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Probable effector of the planar cell polarity signaling pathway which regulates the septin cytoskeleton in both ciliogenesis and collective cell movements. Together with FUZ and WDPCP proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies (By similarity).
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B1WC40
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NCBP2_RAT
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Nuclear cap-binding protein subunit 2 (20 kDa nuclear cap-binding protein) (NCBP 20 kDa subunit) (CBP20)
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MSGGLLKALRSDSYVELSEYRDQHFRGDNEEQEKLLKKSCTLYVGNLSFYTTEEQIYELFSKSGDIKKIIMGLDKMKKTACGFCFVEYYSRADAENAMRYINGTRLDDRIIRTDWDAGFKEGRQYGRGRSGGQVRDEYREDYDAGRGGYGKLAQKQ
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Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5' end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2, thereby being required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP2/CBP20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure. The conventional cap-binding complex with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus (By similarity).
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B1WC58
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CTIP_RAT
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DNA endonuclease RBBP8 (EC 3.1.-.-) (CtBP-interacting protein) (CtIP) (Retinoblastoma-binding protein 8) (RBBP-8) (Retinoblastoma-interacting protein and myosin-like) (RIM) (Sporulation in the absence of SPO11 protein 2 homolog) (SAE2)
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MSISGSSCGSPNSTDISSDFKELWTKLKEYHDKEVQGLQIKVTKLKKERILDAQRLEEFFTKNQQLRDQQKVLQETIKILEDRLRAGLCDRCAVTEEHMHKKQQEFENIRQQNLRLITELMNEKSALQEENKKLSEQLQQKMESGQQDQVAELECEENIIPDSPITSFSFSGINRLRRKENLHVRYVEQTHTKLEHSACTSELRKFSKGSTPAPVNSEEHEILVADTCDQSHSPLSKICGTSSYPADKLSSNLDAVVAETLGLDGQEESEPQGPVSPLGNELYHCLKEDHKKQPFMESAIRNEDNVRFSDSASKAPPRELTTRGSSPVFGPTSTVKTHLGLKTSFSPSLLDSGKKNLLSTAPFSSISVSRSEKVRSKSEDNALFTQQSAGSEVKVISQSFPSKQILTSKNVSDSVDEQGGADHMKDAVSDKHLVPLKSLGGKASKRKRTEEEGEHAVHCPQTCFDKENALPFPMENQFPVNGDHVMDKPLDLSDRFAANQRQEKNHGDETCKHKLKQVTIYEALKPVPKGSSSGRKALSGACTLAQDSAETYCLQQRTLQCSSKFSPDHNTQLQIKEENPVFKTPPRSQESLETENLFGDVKGIGSLVPIKVKGRSAHGGCELASVLQLNPCRVAKTKSLPSNHDMSFENIQWSVDPGADLSQYKMDVTVIDTKDSSHSRLGGETVDMDCTLVSETMLLKMKKQEQREKSPNGDIKMNDSLEDMFDRTTHEEYESCLADNFSQVPDEEELSDTTKKPNIHGDKQDGIKQKAFVEPYFKDKERETSIQNFPHIEVVRKKEERRKLLGHTCKECEIYYADLPAEEREKKLASCSRHRFRYIPTNTPENFWEVGFPSTQTCLERGYIKEDLDPCPRPKRRQPYNAVFSPKGKEQRT
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Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway. HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse. Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ). Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA. Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage (By similarity). During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations (By similarity).
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B1WC61
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ACAD9_RAT
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Complex I assembly factor ACAD9, mitochondrial (Acyl-CoA dehydrogenase family member 9) (ACAD-9) (EC 1.3.8.-)
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MSGYVLFSRGATAAAAAARASRVLRVFTERRRTLHTSLQSCSFAKELFLGHIQQKGVFPFPEVSQEELSEINQFVGPLEKFFNEEVDSRKIDQEGKIPADTLAKLKSLGLFGIQVPEEYGGLGLSNTMYARLGEIISMDASITVTLAAHQAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDKKYFVLNGSKVWITNGGLANIFTVFAKTEVVDSDGSIKDKMTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAMNILNSGRFSMGSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFIALTGLQHAGRILTSRIKELKSGNVTTVMETIGRKLRDSLGRTVDLGLSSNIAVVHPSLGDSANKLEENVHYFGRTVETLLLRFGKTIVEEQLVLKRVANILINLYGMTAVLSRASRSIRIGLKNHDHEILLANMFCVEAYFQNLFSLSQLDKYAPENLDEQIKKVSQQILEKRAYICAHPLDRAS
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As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation. This moonlighting protein has also a dehydrogenase activity toward a broad range of substrates with greater specificity for long-chain unsaturated acyl-CoAs. However, in vivo, it does not seem to play a primary role in fatty acid oxidation. In addition, the function in complex I assembly is independent of the dehydrogenase activity of the protein.
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B1WC68
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HDAC8_RAT
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Histone deacetylase 8 (HD8) (EC 3.5.1.98) (Protein deacetylase HDAC8) (EC 3.5.1.-) (Protein decrotonylase HDAC8) (EC 3.5.1.-)
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MEIPEEPANSGHSLPPVYIYSPEYVSICDSLVKVPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHPDSIEYGLGYDCPATEGIFDYAAAIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV
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Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility. In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones.
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