TIKI2_DANRE
ID TIKI2_DANRE Reviewed; 518 AA.
AC E7F4V6;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Metalloprotease TIKI2;
DE EC=3.4.-.-;
DE AltName: Full=TRAB domain-containing protein 2B;
DE Flags: Precursor;
GN Name=trabd2b; Synonyms=tiki2; ORFNames=si:ch211-120j21.1;
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; JQ653420; AFN02886.1; -; mRNA.
DR EMBL; CR352292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001257406.1; NM_001270477.1.
DR AlphaFoldDB; E7F4V6; -.
DR STRING; 7955.ENSDARP00000107884; -.
DR PaxDb; E7F4V6; -.
DR Ensembl; ENSDART00000129193; ENSDARP00000107884; ENSDARG00000088816.
DR GeneID; 566028; -.
DR KEGG; dre:566028; -.
DR CTD; 388630; -.
DR ZFIN; ZDB-GENE-091204-381; trabd2b.
DR eggNOG; ENOG502QPR1; Eukaryota.
DR GeneTree; ENSGT00940000165000; -.
DR HOGENOM; CLU_035548_1_0_1; -.
DR InParanoid; E7F4V6; -.
DR OMA; RRRMEIY; -.
DR OrthoDB; 1407303at2759; -.
DR PhylomeDB; E7F4V6; -.
DR TreeFam; TF313392; -.
DR PRO; PR:E7F4V6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000088816; Expressed in pharyngeal gill and 13 other tissues.
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: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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..518
FT /note="Metalloprotease TIKI2"
FT /id="PRO_0000419452"
FT TOPO_DOM 23..499
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 518 AA; 59742 MW; 44F9F7A95FEA6F09 CRC64;
MNCQSGLRWL VTLCAFFQVG SARDTHESTR QCDKPVSQKD MNSFLWTVKR PRPFPPSYLF
GTIHVPYTRV WDYIPESSKR AFQTSNSVFF ELDLTDPLTI SKLTSCQLLP NGENLQTLLP
RDLYRRLKRH LDYVKHMMPF WMTADQRGRG LYADYLFNAI AGNWERKRPV WVMLMVNSLT
EADVRSRGTP VLDLFLAQEA ERLGKQTGAV ERVEEQCHPL NGLNFSQVLF ALNQTLLQHE
SLRAGILQGT FTTEDLIAHY NCGDLNSIIF NHDTSQLPHF INSSLPDHER LTAQQIDSYL
RQELIYKRNE RMARRVSALL QRNPNQSFFF AFGAGHFLGN HSVLDILRQE GYEVEHTPPQ
EPIIQSWSER EATTLNPTED SFESVTEWTS ETPELEEISQ EELSHMLLPD SLSQLEEFGR
YKHPRKTHHT HSRPRLFSDL WVRIGDSTTP HPSIRITNGY VTVEPPQIRQ EQQQRLRERL
KPLSEPTNPS ALDSAAPNPT YALTCFLACL ISQLLFAS
