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TIKI1_CAEEL
ID   TIKI1_CAEEL             Reviewed;         420 AA.
AC   Q17678; H9G2V6; H9G2V7; I6U4Y5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 6.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Metalloprotease TIKI homolog;
DE            EC=3.4.-.-;
DE   Flags: Precursor;
GN   ORFNames=C05G5.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX   PubMed=22726442; DOI=10.1016/j.cell.2012.04.039;
RA   Zhang X., Abreu J.G., Yokota C., Macdonald B.T., Singh S., Coburn K.L.,
RA   Cheong S.M., Zhang M.M., Ye Q.Z., Hang H.C., Steen H., He X.;
RT   "Tiki1 is required for head formation via Wnt cleavage-oxidation and
RT   inactivation.";
RL   Cell 149:1565-1577(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Metalloprotease. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC       Note=Divalent metal cations. Mn(2+) or Co(2+). {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=a;
CC         IsoId=Q17678-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=Q17678-2; Sequence=VSP_044172;
CC       Name=c;
CC         IsoId=Q17678-3; Sequence=VSP_044171;
CC   -!- SIMILARITY: Belongs to the TIKI family. {ECO:0000305}.
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DR   EMBL; JQ653421; AFN02887.1; -; mRNA.
DR   EMBL; Z70203; CAA94108.5; -; Genomic_DNA.
DR   EMBL; Z70203; CCG28081.1; -; Genomic_DNA.
DR   EMBL; Z70203; CCG28080.1; -; Genomic_DNA.
DR   PIR; T18967; T18967.
DR   RefSeq; NP_001257247.1; NM_001270318.1. [Q17678-1]
DR   RefSeq; NP_001257248.1; NM_001270319.1. [Q17678-2]
DR   RefSeq; NP_001257249.1; NM_001270320.1. [Q17678-3]
DR   AlphaFoldDB; Q17678; -.
DR   BioGRID; 46468; 1.
DR   IntAct; Q17678; 1.
DR   STRING; 6239.C05G5.5a; -.
DR   PaxDb; Q17678; -.
DR   EnsemblMetazoa; C05G5.5a.1; C05G5.5a.1; WBGene00007351. [Q17678-1]
DR   EnsemblMetazoa; C05G5.5b.1; C05G5.5b.1; WBGene00007351. [Q17678-2]
DR   EnsemblMetazoa; C05G5.5c.1; C05G5.5c.1; WBGene00007351. [Q17678-3]
DR   GeneID; 181571; -.
DR   KEGG; cel:CELE_C05G5.5; -.
DR   UCSC; C05G5.5; c. elegans. [Q17678-1]
DR   CTD; 181571; -.
DR   WormBase; C05G5.5a; CE44185; WBGene00007351; -. [Q17678-1]
DR   WormBase; C05G5.5b; CE47145; WBGene00007351; -. [Q17678-2]
DR   WormBase; C05G5.5c; CE47387; WBGene00007351; -. [Q17678-3]
DR   eggNOG; ENOG502QPR1; Eukaryota.
DR   GeneTree; ENSGT00940000165000; -.
DR   InParanoid; Q17678; -.
DR   OMA; DHYDESP; -.
DR   OrthoDB; 1407303at2759; -.
DR   PhylomeDB; Q17678; -.
DR   PRO; PR:Q17678; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00007351; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR040230; TIKI1/2-like.
DR   InterPro; IPR002816; TraB/PrgY/GumN_fam.
DR   PANTHER; PTHR31120; PTHR31120; 1.
DR   Pfam; PF01963; TraB_PrgY_gumN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..420
FT                   /note="Metalloprotease TIKI homolog"
FT                   /id="PRO_0000346438"
FT   TOPO_DOM        23..400
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        420
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..174
FT                   /note="Missing (in isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_044171"
FT   VAR_SEQ         1..123
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_044172"
SQ   SEQUENCE   420 AA;  48815 MW;  7D4040E76F129558 CRC64;
     MTFYILVVSL YLSLFLVTVV QSDCDTDVEQ RERNIFLWSV KHPQFASSQG YLFGTIHVPF
     TEVWKEVSDR VRDAFAVSDT VLLEIDLHDE ATIHELIACK NLAYDETVHS YLSIELLERI
     EKIMEYLRSS FLAWAQKQNP RDTKKIKHAE DIYNNIIGDW WRKRPIWLLF LLYQMCENVF
     EKSSSPLLDL YIAQRATDEK KTIIPIETAE EQCNPVVSVS TNEIIFAIEH TVHYFEDKIL
     DNPSKDNESR SSLKELVEHY KCGTLKEDMF DKDGMSIIDY ATGTTERFKA DEINKKLKQD
     IFVKRNLRMA KRIEKILKGR NSNTVFSAIG AGHFFGSSSV LTYLEESGFI VQKLKNTDVI
     QPLRSPYRQT AKFKRVWTKE TAVRRKSIII EEVAPSSSRI ARLWLVPCIF LLHSIFAIFP
 
 
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