ID   VMP_NEMVE               Reviewed;         287 AA.
AC   K7Z9Q9;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Nematocyst expressed protein 6 {ECO:0000303|PubMed:23151943};
DE            Short=NEP-6 {ECO:0000303|PubMed:23151943};
DE            Short=NEP6 {ECO:0000250|UniProtKB:A7RJ12, ECO:0000305};
DE            EC=3.4.24.-;
DE   AltName: Full=Astacin-like metalloprotease toxin {ECO:0000305};
DE   Flags: Precursor;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=23151943; DOI=10.1007/s10126-012-9491-y;
RA   Moran Y., Praher D., Schlesinger A., Ayalon A., Tal Y., Technau U.;
RT   "Analysis of soluble protein contents from the nematocysts of a model sea
RT   anemone sheds light on venom evolution.";
RL   Mar. Biotechnol. 15:329-339(2013).
CC   -!- FUNCTION: Metalloprotease. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01211};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU01211};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23151943}.
CC       Nematocyst {ECO:0000269|PubMed:23151943}.
CC   -!- TISSUE SPECIFICITY: Nematocyte and pharyngeal gland.
CC       {ECO:0000269|PubMed:23151943}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the early planula stage of
CC       Nematostella in single cells of the ectoderm. These cells are thin and
CC       elongated as would be expected of developing nematocytes. In the later
CC       stages, the expression expands to an additional domain of large thick
CC       cells in the pharynx. The size and richness of vesicles suggest that
CC       these cells are not nematocytes but gland cells, and in the polyp
CC       stage, they become the major expression domain of this protein.
CC       {ECO:0000269|PubMed:23151943}.
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; JQ829079; AFY07204.1; -; mRNA.
DR   AlphaFoldDB; K7Z9Q9; -.
DR   SMR; K7Z9Q9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04280; ZnMc_astacin_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR034035; Astacin-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   Pfam; PF01400; Astacin; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Nematocyst;
KW   Protease; Secreted; Signal; Toxin; Zinc.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..287
FT                   /note="Nematocyst expressed protein 6"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000423642"
FT   DOMAIN          53..249
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   REGION          249..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        147
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        95..248
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        116..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   287 AA;  32594 MW;  AEF9A8F93D39F6C9 CRC64;
     MKGFIFAGVL VSALICLAEG KPFDNLELVE DDMLMTKEQK EAYLAHQNGR VRRAALRDRY
     LWPQGKIPYT FSDDIDQAGR ELAERAMNHW MSRTCLRFSP RRREHAYIEF QYDGRCRARV
     GYTGEARQKV SIGSALDPCP LGSVIHELGH GIGFFHEHSR PDRDEYVNIN VNNMREGAES
     NFRKDNGYFV DSRGQDYDYG SIMHYSKYQG NNAFNAVVME PIQRGAEIGQ RDGLSAGDIR
     QTNLMYKCNA QGDSELQPVN DEDEDKDGGD SKKKPDPKGP KPGEIEE