ID NAS1_CAEEL Reviewed; 270 AA.
AC O62243;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 27-MAR-2024, entry version 142.
DE RecName: Full=Zinc metalloproteinase nas-1;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 1;
DE Flags: Precursor;
GN Name=nas-1; ORFNames=F45G2.1;
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}.
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; Z93382; CAB07610.2; -; Genomic_DNA.
DR PIR; T22233; T22233.
DR RefSeq; NP_499768.2; NM_067367.6.
DR AlphaFoldDB; O62243; -.
DR SMR; O62243; -.
DR STRING; 6239.F45G2.1.1; -.
DR MEROPS; M12.A14; -.
DR PaxDb; 6239-F45G2-1; -.
DR EnsemblMetazoa; F45G2.1.1; F45G2.1.1; WBGene00003520.
DR GeneID; 185811; -.
DR KEGG; cel:CELE_F45G2.1; -.
DR UCSC; F45G2.1; c. elegans.
DR AGR; WB:WBGene00003520; -.
DR WormBase; F45G2.1; CE33784; WBGene00003520; nas-1.
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_017286_0_0_1; -.
DR InParanoid; O62243; -.
DR OMA; MHYEANE; -.
DR OrthoDB; 2876645at2759; -.
DR PhylomeDB; O62243; -.
DR PRO; PR:O62243; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003520; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
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; Collagenase (Catalytic Domain); 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 PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF798; ZINC METALLOPROTEINASE NAS-1; 1.
DR Pfam; PF01400; Astacin; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000442649"
FT CHAIN ?..270
FT /note="Zinc metalloproteinase nas-1"
FT /id="PRO_0000028906"
FT DOMAIN 71..266
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT ACT_SITE 163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 113..265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 135..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 270 AA; 30756 MW; F6F551EE966818CC CRC64;
MLPIVVSILL ATPLALCQAP FWMPNMQQFS FLTETDFRNA LLLPTTNTRR VRSLYHDMRI
PFQRFKRGGG VAVAAEKDKW PNGRVPYILS AAYTSAQRAV LARAFDTYAK RTCIRFVPKS
PADKDYIVIQ KLDGCYADFS RVGGRQQVSL ADECIDYATI IHELMHVIGF IHEHQREDRD
SYVSILYQNV IQGANTDFDK LSNLGLSYYG EHYDYSSIMH YEANEGSRNG KNTIEAKNSH
FTAIMGKASD FSTSDLRRVN RAYKCSIFAF
//
