ID   TIKI1_NEMVE             Reviewed;         471 AA.
AC   A7RX69; I6UYT4;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Metalloprotease TIKI homolog;
DE            EC=3.4.-.-;
DE   Flags: Precursor;
GN   ORFNames=v1g27680;
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351;
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=CH2 X CH6;
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDO43979.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; JQ653422; AFN02888.1; -; mRNA.
DR   EMBL; DS469549; EDO43979.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001636042.1; XM_001635992.1.
DR   AlphaFoldDB; A7RX69; -.
DR   STRING; 45351.EDO43979; -.
DR   MEROPS; G04.001; -.
DR   GeneID; 5515928; -.
DR   KEGG; nve:5515928; -.
DR   eggNOG; ENOG502QPR1; Eukaryota.
DR   HOGENOM; CLU_103594_0_0_1; -.
DR   InParanoid; A7RX69; -.
DR   OrthoDB; 1407303at2759; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IBA:GO_Central.
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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..471
FT                   /note="Metalloprotease TIKI homolog"
FT                   /id="PRO_0000419455"
FT   TOPO_DOM        25..449
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        450..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        471
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          369..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..405
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   471 AA;  55044 MW;  C0C9A6818DF51B42 CRC64;
     MAAFTLWILV LNVFLLGFQA RKLASNLKFP IQKCDDSTPQ KNFNSFLWLV KRTPPAYFYG
     TIHVPYTRVW DFIPMNSKQA FTASQHVYFE LDLTDEKTMR ALMKCQMLPS GTMLRQTLPR
     KMFKRLKSHL RYIKRMIPKW IKHRDQETSS AGPYANKLYE MLTKDWDKKR PIWVMLMVNS
     LTESDIKTRG IPVLDQYLAL EASRNHKLIG AVENVDEQCK PLNALNASQV VFALNQSLHF
     QERLRRGQVQ VTYTTDDLID HYNCGDLKSV LFSTQTSLPT LTVNSSLEQR ERKRAQEIDQ
     YFRNELIFQR NKRMAQRVIT LLNNHPEKDF FFAFGAGHFL GNHSIIDIMK KHGYDVEYVK
     PEQELPSFKA KKSLNTRRER RKGCRGRRKK SKRCQKKKKR KRPDYSRVRL LQVATRRWNP
     TRKPYPTKLS EAPGARDISS RKAAASCTPI WTVSLALTCA VTCLLTYSGF R