ID   NAS23_CAEEL             Reviewed;         537 AA.
AC   Q7Z0M7;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 3.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Zinc metalloproteinase nas-23;
DE            EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE   AltName: Full=Nematode astacin 23;
DE   Flags: Precursor;
GN   Name=nas-23; ORFNames=R10H1.5;
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 170-228, AND NOMENCLATURE.
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).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=20109220; DOI=10.1186/1471-213x-10-14;
RA   Park J.O., Pan J., Moehrlen F., Schupp M.O., Johnsen R., Baillie D.L.,
RA   Zapf R., Moerman D.G., Hutter H.;
RT   "Characterization of the astacin family of metalloproteases in C.
RT   elegans.";
RL   BMC Dev. Biol. 10:14-14(2010).
CC   -!- FUNCTION: Metalloprotease. {ECO:0000250|UniProtKB:P07584}.
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: Expressed in the hypodermis, rectum and to a lesser
CC       extent in pharyngeal muscles and intestine.
CC       {ECO:0000269|PubMed:20109220}.
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; FO080701; CCD65953.1; -; Genomic_DNA.
DR   EMBL; AJ561213; CAD99214.1; -; mRNA.
DR   RefSeq; NP_001022281.1; NM_001027110.1.
DR   AlphaFoldDB; Q7Z0M7; -.
DR   SMR; Q7Z0M7; -.
DR   BioGRID; 533310; 1.
DR   STRING; 6239.R10H1.5; -.
DR   MEROPS; M12.A37; -.
DR   PaxDb; Q7Z0M7; -.
DR   PeptideAtlas; Q7Z0M7; -.
DR   PRIDE; Q7Z0M7; -.
DR   EnsemblMetazoa; R10H1.5.1; R10H1.5.1; WBGene00003542.
DR   GeneID; 3565992; -.
DR   KEGG; cel:CELE_R10H1.5; -.
DR   CTD; 3565992; -.
DR   WormBase; R10H1.5; CE38212; WBGene00003542; nas-23.
DR   eggNOG; KOG3714; Eukaryota.
DR   GeneTree; ENSGT00940000169152; -.
DR   HOGENOM; CLU_017286_1_5_1; -.
DR   InParanoid; Q7Z0M7; -.
DR   OMA; VAKINRH; -.
DR   OrthoDB; 241999at2759; -.
DR   PhylomeDB; Q7Z0M7; -.
DR   PRO; PR:Q7Z0M7; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00003542; Expressed in larva.
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; 2.60.120.290; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR034035; Astacin-like_dom.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   Pfam; PF01400; Astacin; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF49854; SSF49854; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..111
FT                   /evidence="ECO:0000250|UniProtKB:P13497"
FT                   /id="PRO_0000442670"
FT   CHAIN           112..537
FT                   /note="Zinc metalloproteinase nas-23"
FT                   /id="PRO_0000028927"
FT   DOMAIN          116..311
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DOMAIN          306..346
FT                   /note="EGF-like"
FT   DOMAIN          356..471
FT                   /note="CUB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   ACT_SITE        208
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         217
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        481
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        156..310
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        178..199
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        314..334
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DISULFID        336..345
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DISULFID        356..385
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DISULFID        412..433
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
SQ   SEQUENCE   537 AA;  59872 MW;  9F73484062DA733E CRC64;
     MRFLILVLAG SIGIYGVNLP KIPKLSDLVN PFQQFKLKDI LSTLTALDTP DIAADSAGVS
     LPKHEYTDRL SSISDLNRSK RDLLFQGDIH LSFEHLSNIV REQLDHSRTK RTAFRNAMYP
     KTIWLPNVPF ELHGSLSAKS RSSLVAAMAF WEKHTCVAFK KRTSEKVYLL MSGQEEGCWS
     TVGRDEAQGA QILNIGTGCE MFGITSHEIA HALGLFHEQS RYDRDNYVQI VKSRIAQTNF
     YDFAVVGKKN METYGQKYDI GSVMHYRPTE FSLDGGNSII AKDVNMQNTM GQFRGPSFID
     VAKINRHYNC EKNCKNKITC LNGGYQHPKN CKICVCPPGY GGSDCKGIEA SSPAKCTGVL
     VAGETQRKFT ANIKPNKNAK GIRKCNYHIE APPGKRIVII VDSVIGNCVQ GCYEEGVELK
     MYEDKTVTGA RFCCKLQKPQ TLISQGNTVP LMLVAGKAQA FVQLRYSTVD GPQNRSPKDG
     NATSIGVNPF LLEKYQDNSI DSEAIRKEYH IQSDNVNQED FETLVRSEFI DENTADI