TIKI1_XENTR
ID TIKI1_XENTR Reviewed; 508 AA.
AC F6PTN1; I6UYS9;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 46.
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;
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], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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: expressed in the Spemann-Mangold organizer and is
CC required for anterior-neural patterning in head formation in embryos.
CC Acts by mediating the cleavage of the N-terminal residues of a subset
CC of Wnt proteins. Following cleavage, Wnt proteins become oxidized and
CC form large disulfide-bond oligomers, leading to their inactivation.
CC Able to cleave wnt8. {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 -!- TISSUE SPECIFICITY: Zygotically expressed in the Spemann-Mangold
CC organizer, in particular in the head Spemann-Mangold organizer region
CC responsible for anterior patterning. {ECO:0000269|PubMed:22726442}.
CC -!- DEVELOPMENTAL STAGE: Detectable at stage 9 and prominently expressed
CC from stage 10 (early gastrula) to stage 30 (tadpole). Restricted to the
CC dorsal segment of the gastrula. At stage 10, expressed exclusively in
CC the dorsal blastopore lip and the Spemann-Mangold organizer. Excluded
CC from the dorsal margin of the Spemann-Mangold organizer. At stage 11,
CC expressed in the anterior prechordal plate. By blastopore closure,
CC expression restricted to the anterior midline. At early neurula,
CC expressed in the midline anterior to the tip of the notochord in cells
CC of the endoderm and overlying neural ectoderm.
CC {ECO:0000269|PubMed:22726442}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQ653417; AFN02883.1; -; mRNA.
DR EMBL; AAMC01056565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01056566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001269420.1; NM_001282491.1.
DR AlphaFoldDB; F6PTN1; -.
DR STRING; 8364.ENSXETP00000028687; -.
DR PaxDb; F6PTN1; -.
DR GeneID; 100491951; -.
DR KEGG; xtr:100491951; -.
DR CTD; 129293; -.
DR Xenbase; XB-GENE-6050964; trabd2a.
DR eggNOG; ENOG502QPR1; Eukaryota.
DR InParanoid; F6PTN1; -.
DR OrthoDB; 1407303at2759; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0017147; F:Wnt-protein binding; IDA:UniProtKB.
DR GO; GO:0060322; P:head development; IMP:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:ParkinsonsUK-UCL.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..508
FT /note="Metalloprotease TIKI1"
FT /id="PRO_0000419451"
FT TOPO_DOM 24..485
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 508 AA; 58544 MW; 4272C5C794B25783 CRC64;
MVIIWNIFLP AFLLVLAKAS LRSSRDSANC KLNKKQSQLN SFLWTIKRDP PSYFFGTIHV
PYTRVWDFIP ENSKTAFQQS NIVYFELDLT DPYTISALTS CQMLPQGENL QNVLPRDIYR
RLKRHLEYVK LMMPSWMTPD QRGKGLYADY LFNAIAGNWE RKRPVWVMLM VNSLTEVDIK
SRGVPVLDLY LAQEAERLKK RTGAVEQVEE QCHPLNGLNL SQVIFALNQT LLQQENLRAG
SVQVPYSTED LIKHYNCGDL NSIIFNHDSS QVPNFINSTL PPQERITAQE IDNYFRQELI
YKRNERMGKR VKDLLEQFPE KSFFFAFGAG HFLGNNTVID VLKRYGYDVL HTPAGRSIIN
NGKGKKNLLP SKFSSSSLPV GLSAPPCTVT SRIKQSINSH KDQESLPDIL LDDDIDQLDK
DERKYKKRKQ RKEKHRHFSD LWVRIQESST DTTPQIRIIN GYITVEPHPR EHGKDKYIKA
AQSVSFSLSI PSAFLLLAWC FQQVAVLQ
