NAS6_CAEEL
ID NAS6_CAEEL Reviewed; 344 AA.
AC Q9U3S9; Q7Z0N6;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Zinc metalloproteinase nas-6;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 6;
DE Flags: Precursor;
GN Name=nas-6; ORFNames=4R79.1;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 261-294, 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 pharyngeal and body wall muscles,
CC intestine, hypodermis and pharyngeal mc2 cells.
CC {ECO:0000269|PubMed:20109220}.
CC -!- DISRUPTION PHENOTYPE: 10 percent of animals are arrested at the larval
CC stage. Defects in the grinder of the pharynx result in reduced
CC pharyngeal pumping rates and a slower growth. In a nas-7 (hd116) mutant
CC background, growth is further reduced. {ECO:0000269|PubMed:20109220}.
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DR EMBL; AL031254; CAB63429.2; -; Genomic_DNA.
DR EMBL; AJ561202; CAD99205.1; -; mRNA.
DR RefSeq; NP_001040902.1; NM_001047437.1.
DR AlphaFoldDB; Q9U3S9; -.
DR SMR; Q9U3S9; -.
DR IntAct; Q9U3S9; 1.
DR STRING; 6239.4R79.1a; -.
DR MEROPS; M12.A38; -.
DR PaxDb; Q9U3S9; -.
DR EnsemblMetazoa; 4R79.1a.1; 4R79.1a.1; WBGene00003525.
DR GeneID; 181796; -.
DR KEGG; cel:CELE_4R79.1; -.
DR UCSC; 4R79.1a; c. elegans.
DR CTD; 181796; -.
DR WormBase; 4R79.1a; CE35820; WBGene00003525; nas-6.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000171076; -.
DR HOGENOM; CLU_017286_0_0_1; -.
DR InParanoid; Q9U3S9; -.
DR OMA; EYHDRTC; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q9U3S9; -.
DR PRO; PR:Q9U3S9; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003525; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q9U3S9; baseline and differential.
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; IMP:WormBase.
DR GO; GO:0060465; P:pharynx development; IMP: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; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR003582; ShKT_dom.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF01549; ShK; 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 Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000442654"
FT CHAIN ?..344
FT /note="Zinc metalloproteinase nas-6"
FT /id="PRO_0000028911"
FT DOMAIN 72..266
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 300..334
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
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 114..265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 135..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 300..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 307..327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 314..331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 344 AA; 39278 MW; E1426601EE51504C CRC64;
MLDHVLLLTY CLVSTVVRSQ PSADVFRSFA GYIPEDHRVT HHEWQNSGKF QGDIDGVDPN
LLKLPEGPVL FNALKNKQLT WEGGVIPYEM DTAFSPNEIK ILEKAFDSYR RTTCIRFEKR
EGQTDYLNIV KGYGCYSQVG RTGGKQEISL GRGCFFHEII VHELMHSVGF WHEHSRADRD
DHIKINWDNI LPGMKSQFDK ISAVLQDLQG ENYDYKSIMH YDSTAFSRNG RNTIETVENG
FTQVIGTAMD LSPLDIVKIN KLYSCKTKKK EKVKPATTEE PHQLIPQVVD KNSVDSGEKC
VDHFADCPHF AQYCTRASFF FVMKSYCPFT CKHCPGDRKL KKSG
