ID   NAS4_CAEEL              Reviewed;         315 AA.
AC   P55112; Q7Z0N7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 4.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Zinc metalloproteinase nas-4;
DE            EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE   AltName: Full=Nematode astacin 4;
DE   Flags: Precursor;
GN   Name=nas-4; ORFNames=C05D11.6;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 33-244, AND TISSUE SPECIFICITY.
RC   STRAIN=Bristol N2;
RX   PubMed=14653817; DOI=10.1046/j.1432-1033.2003.03891.x;
RA   Moehrlen F., Hutter H., Zwilling R.;
RT   "The astacin protein family in Caenorhabditis elegans.";
RL   Eur. J. Biochem. 270:4909-4920(2003).
CC   -!- FUNCTION: Metalloprotease (By similarity). May be involved in
CC       digestion. {ECO:0000250|UniProtKB:A8Q2D1, ECO:0000303|PubMed:14653817}.
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:0000305}.
CC   -!- TISSUE SPECIFICITY: Digestive tract. Found in the pharynx cells of the
CC       procorpus, metacorpus, isthmus and terminal bulb, and in the terminal
CC       bulb lumen. {ECO:0000269|PubMed:14653817}.
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DR   EMBL; FO080365; CCD63195.1; -; Genomic_DNA.
DR   EMBL; AJ561201; CAD99204.1; -; mRNA.
DR   PIR; B88482; B88482.
DR   RefSeq; NP_001254939.1; NM_001268010.1.
DR   AlphaFoldDB; P55112; -.
DR   SMR; P55112; -.
DR   STRING; 6239.C05D11.6b; -.
DR   MEROPS; M12.A19; -.
DR   PaxDb; P55112; -.
DR   EnsemblMetazoa; C05D11.6a.1; C05D11.6a.1; WBGene00003523.
DR   EnsemblMetazoa; C05D11.6a.2; C05D11.6a.2; WBGene00003523.
DR   GeneID; 182259; -.
DR   UCSC; C05D11.6; c. elegans.
DR   CTD; 182259; -.
DR   WormBase; C05D11.6a; CE37080; WBGene00003523; nas-4.
DR   eggNOG; KOG3714; Eukaryota.
DR   HOGENOM; CLU_017286_2_2_1; -.
DR   InParanoid; P55112; -.
DR   PhylomeDB; P55112; -.
DR   PRO; PR:P55112; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00003523; Expressed in larva and 3 other tissues.
DR   ExpressionAtlas; P55112; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
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; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..?
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000442652"
FT   CHAIN           ?..315
FT                   /note="Zinc metalloproteinase nas-4"
FT                   /id="PRO_0000028909"
FT   DOMAIN          95..290
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   REGION          291..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        188
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        137..289
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        160..179
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   315 AA;  35743 MW;  0EBC9A73BDF3FCDF CRC64;
     MMTIQRYSLV FCAIFATCWT ASVVNNKQVI DTSVPQTETT LNDADFHSDL HQRYDLQTLG
     IKVKDDPTIG NYSEGDILLE SPKKFVEENN KLGRNAIKQI YRRWPNNEIP YTLSSQYGSY
     ARSVIANAMN EYHTKTCVKF VARDPSKHHD YLWIHPDEGC YSLVGKTGGK QPVSLDSGCI
     QVGTIVHELM HAVGFFHEQS RQDRDSYIDV VWQNVMNGAD DQFEKYNLNV ISHLDEPYDY
     ASIMHYGPYA FSGSGKKTLV PKKSGSERMG QRVKFSDIDV RKINKLYNCP GVSGNNNNNN
     NNQINSNSIV NHPQV