NAS29_CAEEL
ID NAS29_CAEEL Reviewed; 532 AA.
AC Q20958; Q7Z0M3;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 4.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Zinc metalloproteinase nas-29;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 29;
DE Flags: Precursor;
GN Name=nas-29; ORFNames=F58A6.4;
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 197-286, GENE STRUCTURE, 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; FO080690; CCD65842.1; -; Genomic_DNA.
DR EMBL; AJ561218; CAD99218.1; -; mRNA.
DR PIR; T16493; T16493.
DR RefSeq; NP_494953.3; NM_062552.4.
DR AlphaFoldDB; Q20958; -.
DR SMR; Q20958; -.
DR MEROPS; M12.A29; -.
DR PaxDb; Q20958; -.
DR EnsemblMetazoa; F58A6.4.1; F58A6.4.1; WBGene00003547.
DR GeneID; 186488; -.
DR KEGG; cel:CELE_F58A6.4; -.
DR UCSC; F58A6.4; c. elegans.
DR CTD; 186488; -.
DR WormBase; F58A6.4; CE42691; WBGene00003547; nas-29.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000169152; -.
DR HOGENOM; CLU_017286_1_5_1; -.
DR InParanoid; Q20958; -.
DR OMA; HFGVTSH; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q20958; -.
DR PRO; PR:Q20958; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003547; Expressed in larva and 2 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:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 1.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000742; EGF-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 InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 1.
DR PIRSF; PIRSF036365; Astacin_nematoda; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 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 Cleavage on pair of basic residues; Disulfide bond; EGF-like domain;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..134
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442676"
FT CHAIN 135..532
FT /note="Zinc metalloproteinase nas-29"
FT /id="PRO_0000028933"
FT DOMAIN 135..335
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 330..370
FT /note="EGF-like"
FT DOMAIN 380..494
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT ACT_SITE 231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 179..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 201..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 338..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 360..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 380..408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 435..456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 532 AA; 60395 MW; 29FBD634CB685A08 CRC64;
MISKNTSFCG FLILVLATCM SAQFVSNESI KLHDILKPSA THRLFDTLQY SVEEQYSDSH
LSFDVSTIYN YSEKPISIGK LNKKYRDILF EGDMAISYKQ LSMIVNGSTE YRKAIKSRRR
GNKINGESTD RTKRQAYLDN NYPATIWKNG VAFMFHESLT PIAKTAILKA VHFWYRETCI
EFHPRTFQKE YLLFIGNDDG CWSTVGRDAS QGKQVVSIGN GCEHFGVTSH ELAHALGIFH
EQSRFDRDES VVFNPRVVER DLLFNFAKIS PRQMSTYGLP YDIGSVMHYT PTEFSNIPSI
PTLAAIDTNL QQTMGQLEGP SFVDVHIMNQ HYQCQEKCPT QAPCQNGGFT NSRNCKVCKC
PTGFGGAYCQ LIASSFSPFC GGYLNAEETT RRFDITIRQS TTTRSKTCVY HIKAPEGKRI
IIDILKIDSK CIEGCWQDGL ELKMKKDFRP VGYRFCCPES SRRKVISEGN MVPFMVFSKE
HDFSVSFEYS FVSTSAGFDD EKNDSDVIVD NLDGVFVSDT SLLQRIGFRR QL
