ID   NAS5_CAEEL              Reviewed;         360 AA.
AC   P91828;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Zinc metalloproteinase nas-5;
DE            EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE   AltName: Full=Nematode astacin 5;
DE   Flags: Precursor;
GN   Name=nas-5; ORFNames=T23H4.3;
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   NOMENCLATURE.
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. {ECO:0000250|UniProtKB:A8Q2D1}.
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}.
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DR   EMBL; Z83240; CAB05814.2; -; Genomic_DNA.
DR   PIR; T25210; T25210.
DR   RefSeq; NP_492616.1; NM_060215.1.
DR   AlphaFoldDB; P91828; -.
DR   SMR; P91828; -.
DR   STRING; 6239.T23H4.3; -.
DR   MEROPS; M12.A45; -.
DR   PaxDb; P91828; -.
DR   PeptideAtlas; P91828; -.
DR   EnsemblMetazoa; T23H4.3.1; T23H4.3.1; WBGene00003524.
DR   GeneID; 188819; -.
DR   KEGG; cel:CELE_T23H4.3; -.
DR   UCSC; T23H4.3; c. elegans.
DR   CTD; 188819; -.
DR   WormBase; T23H4.3; CE25126; WBGene00003524; nas-5.
DR   eggNOG; KOG3714; Eukaryota.
DR   HOGENOM; CLU_795077_0_0_1; -.
DR   InParanoid; P91828; -.
DR   OMA; CIRLIPR; -.
DR   OrthoDB; 681837at2759; -.
DR   PhylomeDB; P91828; -.
DR   PRO; PR:P91828; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00003524; Expressed in adult organism and 1 other tissue.
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:0043050; P:pharyngeal pumping; IGI:WormBase.
DR   GO; GO:0060465; P:pharynx development; IGI:WormBase.
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   InterPro; IPR010909; PLAC.
DR   Pfam; PF01400; Astacin; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS50900; PLAC; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..?
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000442653"
FT   CHAIN           ?..360
FT                   /note="Zinc metalloproteinase nas-5"
FT                   /id="PRO_0000028910"
FT   DOMAIN          61..269
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DOMAIN          299..336
FT                   /note="PLAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        111..268
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        134..157
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   360 AA;  40772 MW;  31F91C70EC4832C8 CRC64;
     MDIKQLLLSI ILTVSVVNGR GRRINIYGAE NGKSDIVQLR GPAEQLVYSS PIRERRPIFR
     NALLSNSPLR WSKMQDLDGN YLIPYVISGN YDTVERDTIK TAMEKIANNT CIRLIPRTNQ
     PDYAEINNKK GQGCYASIGR FPGKNVVMLE SNDDQSCIQE DTVIHELFHV IGLWHEHMRA
     DRDAFINVLY KNIEPAQYPQ FEKLSSRDAT TYSVPYDYNS VMHYDENAFA KPGKISMMTK
     DSKFQKVIGH PKDASSNDYK KVCAIYHCSK CMHQDFQQIV EQEHIELNNP IITNAPVQQG
     DSCTDRLGIC PMLKSREMLN CKVMATFCCS SCSAPTSTTT TTSGTPSDGS LWQRIKSIFQ