TIKI1_DANRE
ID TIKI1_DANRE Reviewed; 494 AA.
AC E7F6V0; I6UWG3;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Metalloprotease TIKI1;
DE EC=3.4.-.-;
DE AltName: Full=TRAB domain-containing protein 2A;
DE Flags: Precursor;
GN Name=trabd2a; Synonyms=tiki1; ORFNames=wu:fc66h01;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Metalloprotease that acts as a negative regulator of the Wnt
CC signaling pathway by mediating the cleavage of the N-terminal residues
CC of a subset of Wnt proteins. Following cleavage, Wnt proteins become
CC oxidized and form large disulfide-bond oligomers, leading to their
CC inactivation (By similarity). {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: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TIKI family. {ECO:0000305}.
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DR EMBL; JQ653419; AFN02885.1; -; mRNA.
DR EMBL; CABZ01071835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01071836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01071837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01071838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01071839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01071840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01071841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01071842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001289159.1; NM_001302230.1.
DR AlphaFoldDB; E7F6V0; -.
DR STRING; 7955.ENSDARP00000108636; -.
DR PaxDb; E7F6V0; -.
DR Ensembl; ENSDART00000127504; ENSDARP00000108636; ENSDARG00000089701.
DR GeneID; 564021; -.
DR KEGG; dre:564021; -.
DR CTD; 129293; -.
DR ZFIN; ZDB-GENE-030131-4053; trabd2a.
DR eggNOG; ENOG502QPR1; Eukaryota.
DR GeneTree; ENSGT00940000165000; -.
DR InParanoid; E7F6V0; -.
DR OrthoDB; 1407303at2759; -.
DR PRO; PR:E7F6V0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000089701; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; E7F6V0; baseline.
DR GO; GO:0031301; C:integral component of organelle membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0017147; F:Wnt-protein binding; ISS:UniProtKB.
DR GO; GO:0060322; P:head development; ISS:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt signaling pathway; 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 Cell membrane; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Wnt signaling pathway.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..494
FT /note="Metalloprotease TIKI1"
FT /id="PRO_0000419450"
FT TOPO_DOM 26..467
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 459
FT /note="E -> D (in Ref. 1; AFN02885)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="R -> W (in Ref. 1; AFN02885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 56839 MW; 8F40E8EA2072EBB7 CRC64;
MTMMTMMMVS WSAFLQICWI LMVRANQFNP GEPSGCRTNT PQSDLNSFLW TIKRDPPSYL
YGTIHVPYTR VWDFIPQNSK QAFQESSVVY FELELTDPST ISALSRCQLL PAGQNLQDVL
PPELYLRLKT HLEYVRLMLP SWMTPDQRGK GLYAEYLFNA IAGNWERKRP VWVMLMVNSL
TEADIKTRGV PVLDLYLAQE AERMKKQTGA VEKVEEQCSP LNTLDFSQVI FALNQTLLQQ
ESVRAGSLQV PYTTEHLITH YNCGDLHSII SHDTAQVPNF NNVTLRPSDQ VTAQQIDSYF
RRELIYKRNE RMGRRVTALL QEQPHKTFFF AFGAGHFLGN NSVIDVLRRE GYEVEHTPAG
QPLHRRSGWR SADPADTDAA LQPFLHHSRH HELQLLEGLE LLEKVEHKLK KKHRRNKLKK
QRQFNDLWVR MEDSVTAEAP PPLIHIINGY ITVQTHPQEH ERANHDRTFS GSSSRTGPAL
SALAVCVQML RLLL
