NAS7_CAEEL
ID NAS7_CAEEL Reviewed; 382 AA.
AC P55113; Q7Z0N5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Zinc metalloproteinase nas-7;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 7;
DE Flags: Precursor;
GN Name=nas-7; ORFNames=C07D10.4;
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 61-339, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, 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, AND DISRUPTION PHENOTYPE.
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 head of adult hermaphrodites but
CC not within pharynx cells (PubMed:14653817). Expressed in pharyngeal
CC muscles, mc cells, intestine, hypodermal seam cells, arcade cells,
CC spermatheca, vulva and rectal epithelial cells (PubMed:20109220).
CC {ECO:0000269|PubMed:14653817}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, expression is detected just before
CC hatching. {ECO:0000269|PubMed:14653817}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. In a nas-6 (hd108) mutant
CC background, enhances slow growth of nas-6 single mutant.
CC {ECO:0000269|PubMed:20109220}.
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DR EMBL; FO080415; CCD63532.1; -; Genomic_DNA.
DR EMBL; AJ561203; CAD99206.1; -; mRNA.
DR PIR; T15444; T15444.
DR RefSeq; NP_495552.2; NM_063151.2.
DR AlphaFoldDB; P55113; -.
DR SMR; P55113; -.
DR BioGRID; 47221; 1.
DR STRING; 6239.C07D10.4; -.
DR MEROPS; M12.A18; -.
DR PaxDb; P55113; -.
DR PeptideAtlas; P55113; -.
DR EnsemblMetazoa; C07D10.4.1; C07D10.4.1; WBGene00003526.
DR GeneID; 182368; -.
DR KEGG; cel:CELE_C07D10.4; -.
DR UCSC; C07D10.4; c. elegans.
DR CTD; 182368; -.
DR WormBase; C07D10.4; CE34663; WBGene00003526; nas-7.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00970000196428; -.
DR HOGENOM; CLU_017286_0_0_1; -.
DR InParanoid; P55113; -.
DR OMA; AKLWPNA; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; P55113; -.
DR PRO; PR:P55113; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003526; Expressed in embryo and 3 other 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: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; IPR017367; Caenorhab_nas-7/8.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR031062; Peptidase_M12A_nas7.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR003582; ShKT_dom.
DR PANTHER; PTHR10127:SF827; PTHR10127:SF827; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF01549; ShK; 1.
DR PIRSF; PIRSF038054; Nas7/Nas8_prd; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00254; ShKT; 1.
DR SMART; SM00235; ZnMc; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS51670; SHKT; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Disulfide bond; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted;
KW Signal; Zinc; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..79
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442655"
FT CHAIN 80..382
FT /note="Zinc metalloproteinase nas-7"
FT /id="PRO_0000028912"
FT DOMAIN 80..273
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 348..382
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT ACT_SITE 172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 171
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 BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 122..272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 144..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 348..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 355..375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 362..379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 382 AA; 43820 MW; 0462478E71FB77D2 CRC64;
MLLPWIITIV TVIPATLGHR NRVQDDEMLV ISDSTDSLNL EDFEFADKLT REELFGKHIP
VEVVNDFKSD IRLPRRHKRN GVSRAAKLWP NARIPYAISP HYSPHERALL AKAVKQYHEK
TCIRFVPRQT GEPDYLFIGK VDGCFSEVGR TSGVQVLSLD NGCMEYATII HEMMHVVGFY
HEHERWDRDN FIDIIWQNID RGALDQFGKV DLSKTSYYGQ PYDYKSILHY DSLAFSKNGF
PTMLPKVKSA TIGNARDFSD VDISKINRMY NCPVEKSVTA PFARARHVPI YSPQYHKYED
RPKIPLRSFD MQQGPINPPM AQIPSQSLVV SSSSGRVNYN SNKPSSQCED RITVCWWTAD
RCRSPAIYQV MSSLCPKTCK FC
