NAS25_CAEEL
ID NAS25_CAEEL Reviewed; 399 AA.
AC Q20459; Q7Z0M5;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Zinc metalloproteinase nas-25;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 25;
DE Flags: Precursor;
GN Name=nas-25; ORFNames=F46C5.3;
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 208-260, 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.
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 muscles, pharyngeal-
CC intestinal valve, rectal gland cells and arcade cells.
CC {ECO:0000269|PubMed:20109220}.
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DR EMBL; Z54281; CAA91045.3; -; Genomic_DNA.
DR EMBL; AJ561215; CAD99216.1; -; mRNA.
DR PIR; T22300; T22300.
DR RefSeq; NP_495880.1; NM_063479.4.
DR AlphaFoldDB; Q20459; -.
DR SMR; Q20459; -.
DR STRING; 6239.F46C5.3; -.
DR MEROPS; M12.A27; -.
DR PaxDb; Q20459; -.
DR EnsemblMetazoa; F46C5.3.1; F46C5.3.1; WBGene00003544.
DR GeneID; 174412; -.
DR KEGG; cel:CELE_F46C5.3; -.
DR UCSC; F46C5.3; c. elegans.
DR CTD; 174412; -.
DR WormBase; F46C5.3; CE28935; WBGene00003544; nas-25.
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_017286_1_1_1; -.
DR InParanoid; Q20459; -.
DR OMA; VMHYSAD; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q20459; -.
DR PRO; PR:Q20459; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003544; Expressed in larva 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 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.
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_0000442672"
FT CHAIN ?..399
FT /note="Zinc metalloproteinase nas-25"
FT /id="PRO_0000028929"
FT DOMAIN 41..237
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 232..275
FT /note="EGF-like"
FT ACT_SITE 135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 106..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 240..260
FT /evidence="ECO:0000250"
FT DISULFID 265..274
FT /evidence="ECO:0000250"
SQ SEQUENCE 399 AA; 45456 MW; 38EA62319A2CF172 CRC64;
MQIYLGITIC LVAFLTVIDC AIPYYRTHSN FGSLGRRKVR QVQRDLTYRW PNNTVPYYVG
NVTSTIKKSV RLAIEELQAW TCIRFQNVNE KYSDGDSVRI VDLGSCSSPI GRQQIGTQDV
SLTKNCWGMG TAIHELMHAI GIEHTQSRSD RNRYLDILAQ NIDNRDLPNF ELLSPRLWAN
LVPYDYGSVM HYSADSFSNK DDEQTMLPKD RSFIETMGSM IPNFYDFDQI NQYYQCYDSC
RNAGQLANCA NGGIPNPNNC QVCNCPMGYG GDLCDQRPEG CGSTLVATDR WQKQKLSVRF
SRNDDQYFTF CNSWIVGPSD RTLQVIYEIT SDSIRRQICS FGCYEGGIEV KHLQDPRITN
DRDCCLNTPL NLTTTVNPLP VILYTSGATV TYDFSYRYV
