ID   NAS21_CAEEL             Reviewed;         380 AA.
AC   Q22401; Q7Z0M8;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 3.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Zinc metalloproteinase-like protein nas-21 {ECO:0000305};
DE   AltName: Full=Nematode astacin 21;
DE   Flags: Precursor;
GN   Name=nas-21; ORFNames=T11F9.5;
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 157-238, GENE STRUCTURE, 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).
CC   -!- FUNCTION: May lack metalloprotease activity. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- CAUTION: Ser-137 is present instead of the conserved His which is
CC       expected to be zinc-binding residue. There is therefore some
CC       uncertainty concerning the enzymatic activity of this protein.
CC       {ECO:0000305}.
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DR   EMBL; Z74042; CAA98533.2; -; Genomic_DNA.
DR   EMBL; AJ561211; CAD99213.1; -; mRNA.
DR   PIR; T24841; T24841.
DR   RefSeq; NP_505907.2; NM_073506.4.
DR   AlphaFoldDB; Q22401; -.
DR   SMR; Q22401; -.
DR   STRING; 6239.T11F9.5; -.
DR   PaxDb; Q22401; -.
DR   PRIDE; Q22401; -.
DR   EnsemblMetazoa; T11F9.5.1; T11F9.5.1; WBGene00003540.
DR   GeneID; 188422; -.
DR   KEGG; cel:CELE_T11F9.5; -.
DR   UCSC; T11F9.5; c. elegans.
DR   CTD; 188422; -.
DR   WormBase; T11F9.5; CE41929; WBGene00003540; nas-21.
DR   eggNOG; KOG3714; Eukaryota.
DR   GeneTree; ENSGT00970000196541; -.
DR   HOGENOM; CLU_017286_1_1_1; -.
DR   InParanoid; Q22401; -.
DR   OMA; YFRTMGS; -.
DR   OrthoDB; 681837at2759; -.
DR   PhylomeDB; Q22401; -.
DR   PRO; PR:Q22401; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00003540; 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:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR017050; Metallopeptidase_nem.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   Pfam; PF01400; Astacin; 1.
DR   PIRSF; PIRSF036365; Astacin_nematoda; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..?
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000442668"
FT   CHAIN           ?..380
FT                   /note="Zinc metalloproteinase-like protein nas-21"
FT                   /id="PRO_0000028925"
FT   DOMAIN          46..234
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        90..233
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        110..130
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   380 AA;  44626 MW;  65B2877F3F384D0D CRC64;
     MNYFITFFFM HIAVLNFYFR FSNGNKIVMR VGGSPETKRL ERSKRQALRM DNEPRWPRGT
     INYFFDEQRF DENSRATVLR AMEKISNHTC IKFSPKDARI KLRIVSDKGC QAAIGRVGGD
     QQYLSFPTSC YSVGSASELI HVIGFLHSHQ RADRDEYLKL NLQPWRLNDW FQTMQYKKYL
     DQWWIVPYDY GSIMQYHDSD NEYGPKNSKY FRTMGSQIPS YFDYLMINEY YQCSCEGEEQ
     INCKNRGYPN PGNCSECNCP LESSEEWKNI TLNLDAGYMS LQNGTKLHQI DFVFRYLSIS
     APANKTIEVD IREITGVECN YGCYIGGIEV KTHEDRRMTS PRLCCKNDNE IYKSRNNPTI
     VMAFNSEGLD KYNIFYRFTD