TIKI2_XENTR
ID TIKI2_XENTR Reviewed; 523 AA.
AC P0DJQ9; I6TUA9;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 37.
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;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
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].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
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. Able to cleave wnt8. Required for head formation.
CC {ECO:0000269|PubMed:22726442}.
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 -!- MISCELLANEOUS: Was named TIKI in reference to large-headed humanoid in
CC Polynesian mythology. {ECO:0000305|PubMed:22726442}.
CC -!- SIMILARITY: Belongs to the TIKI family. {ECO:0000305}.
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DR EMBL; JQ653418; AFN02884.1; -; mRNA.
DR RefSeq; XP_017949070.1; XM_018093581.1.
DR AlphaFoldDB; P0DJQ9; -.
DR MEROPS; G04.002; -.
DR Ensembl; ENSXETT00000091211; ENSXETP00000082508; ENSXETG00000035683.
DR GeneID; 101734068; -.
DR KEGG; xtr:101734068; -.
DR CTD; 388630; -.
DR Xenbase; XB-GENE-6050974; trabd2b.
DR InParanoid; P0DJQ9; -.
DR OrthoDB; 1407303at2759; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000035683; Expressed in 2-cell stage embryo and 10 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..523
FT /note="Metalloprotease TIKI2"
FT /id="PRO_0000419453"
FT TOPO_DOM 27..499
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 139
FT /note="M -> T (in Ref. 1; AFN02884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 60257 MW; 0417C266EB2BC3D4 CRC64;
MGKTMWARAV FLCFSVGTLL WQEVLTRRIP VDTGQCGLPK SQEDLNSFLW TVRRHPPAYL
FGTIHVPYTR VWDFIPQNSK KAFHDSNSVY FELDLTDPYT ISALANCQML PQGENLQDVL
PRDLYRRLKR HLEYVKHMMP HWMTPDQRGK GLYADYLFNA IAGNWERKRP VWVMLMVNSL
TEADIRSRGV PVLDLYLAQE ADRMKKKTGA VERVEEQCHP LNRLNLSQVL FALNQTLLQH
ESLRAGSFQA PYTTEDLIKH YNCGDLNAVI FSHDSSQLPN FINVTLPPHE QVTAQEIDIY
FRQELIYKRN ERMARRVIAL LKENKDKSFF FAFGAGHFLG NNTVIDVLRQ NGYEVEHTPA
GQTFTAAKPK TNPTSDDSMA TDSPAMKYFD HVPATASYFG ESDEEMLPPH LLLPDSISQL
EEFGKQNSWH RKHYRNQRPR QFNDLWVRLD DSTTTLPSNT RNTNGEQSAE SLVWLPEQDH
HNYLDVKLSH SQSNSSPKCL SASPAFLYTL VTLCLITTMR TRS
