NAS24_CAEEL
ID NAS24_CAEEL Reviewed; 396 AA.
AC Q93542; Q7Z0M6;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Zinc metalloproteinase nas-24;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 24;
DE Flags: Precursor;
GN Name=nas-24; ORFNames=F20G2.4;
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 280-327, 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: 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; Z79753; CAB02084.2; -; Genomic_DNA.
DR EMBL; AJ561214; CAD99215.1; -; mRNA.
DR PIR; T21166; T21166.
DR RefSeq; NP_506409.2; NM_074008.2.
DR AlphaFoldDB; Q93542; -.
DR SMR; Q93542; -.
DR STRING; 6239.F20G2.4; -.
DR MEROPS; M12.A39; -.
DR PaxDb; Q93542; -.
DR PeptideAtlas; Q93542; -.
DR EnsemblMetazoa; F20G2.4.1; F20G2.4.1; WBGene00003543.
DR GeneID; 184744; -.
DR KEGG; cel:CELE_F20G2.4; -.
DR UCSC; F20G2.4; c. elegans.
DR CTD; 184744; -.
DR WormBase; F20G2.4; CE35860; WBGene00003543; nas-24.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000169788; -.
DR HOGENOM; CLU_017286_1_1_1; -.
DR InParanoid; Q93542; -.
DR OMA; THIHELM; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q93542; -.
DR PRO; PR:Q93542; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003543; 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:UniProtKB-KW.
DR Gene3D; 3.40.390.10; -; 1.
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.
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 Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc;
KW Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000442671"
FT CHAIN ?..396
FT /note="Zinc metalloproteinase nas-24"
FT /id="PRO_0000028928"
FT DOMAIN 44..230
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 224..263
FT /note="EGF-like"
FT ACT_SITE 138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 105..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 231..251
FT /evidence="ECO:0000250"
FT DISULFID 253..262
FT /evidence="ECO:0000250"
SQ SEQUENCE 396 AA; 45162 MW; D9ADF3608ADFC95A CRC64;
MTRVVHIIGA AFLLSSYAYC GLSRFNEHDI EGGDSYKRVK REFERLGSKW LGGTINYYYA
DNNNSVKEKV KSAIAYIANH TCIKFNEDPT HWQRLKIFTS ELSHCRSTIG APGTRSGSAG
ELSMETGWCA NIGSIVHEFS HSLGRYHEHT RPDRDNSLKV TSTDYEARPR PWGMTTMYGP
FEHGSIMMYH SSNYGVGKME PYDMEYKNTM GSRRVTFYDM YKINQYYGCG CSTQLECKNG
GYTSPSDCSR CNCPKGFFGK LCNERRQQDS YELKATYGRW QTQTISFNYK PEPVSDGFYS
TFVYITGEAN STIEITMEGL ENVICTAGCT WNGVEIKSRE DSRITSPVMC CKDEPLYKKV
FKSLHNPTII ELYSKETAPS TATFKYRFMN DKIVFG
