ID   TIKI1_AMPQE             Reviewed;         510 AA.
AC   I1FQB6; I6TUB5;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Metalloprotease TIKI homolog;
DE            EC=3.4.-.-;
DE   Flags: Precursor;
OS   Amphimedon queenslandica (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Haplosclerida; Niphatidae; Amphimedon.
OX   NCBI_TaxID=400682;
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].
RA   Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA   Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA   Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA   Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA   Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA   Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT   evolution of animal complexity.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the TIKI family. {ECO:0000305}.
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DR   EMBL; JQ653423; AFN02889.1; -; mRNA.
DR   RefSeq; NP_001266208.1; NM_001279279.1.
DR   AlphaFoldDB; I1FQB6; -.
DR   STRING; 400682.PAC_15718307; -.
DR   GeneID; 100633175; -.
DR   KEGG; aqu:100633175; -.
DR   eggNOG; ENOG502QPR1; Eukaryota.
DR   InParanoid; I1FQB6; -.
DR   OrthoDB; 1407303at2759; -.
DR   Proteomes; UP000007879; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004175; F:endopeptidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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   Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..510
FT                   /note="Metalloprotease TIKI homolog"
FT                   /id="PRO_0000419454"
FT   TOPO_DOM        31..489
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        490..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          435..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        383
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        417
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   510 AA;  56555 MW;  E50D50C79F036A59 CRC64;
     MQVKIVQVFP CLVLLVKLVL LSVLLPSATG SYHCSNNATQ NSYLWRIEAS PPIYLFGTMH
     VPYKKLWDDV PDNVKSVLSL SEHLCVELRL TDSETSKNLS ACRYLPKNET LESVLPGGLY
     VRVLKYFVRI QNQFPKWLFG NASINGLSRI ESDRLFHAMI GNWNRLRPVW LLMLISSLSR
     ENVQERSIPL LDVFLDRAAE GMGKNVEAVE VYKEQCRPFN RLNNTKVFVA LRKLLDYLEP
     LADGPISSTD SDLETYNCGD FKSLVSARPI LPLPSSSKLP NLTSEEAGDL ESINEFLVSQ
     IVYRRNRRMS KTIMSLLSRQ RNETYLFAIG AGHFVGERNV VHMLKKKGYS VNRLSVTETI
     PGPPLPKNII SLGDPSSQLT ILNISSTIPT LPPNRPSHVP PTLSPETIAR IIQSVFNNTQ
     SIYTVDSVEV TPTTTSLNSA TASTTVATPT SSVTPPTSSS SQTRSLTISD SQRTSDDSAF
     IPSASSGLRY NIGLVCVTLF FVLLIITSAL