NAS16_CAEEL
ID NAS16_CAEEL Reviewed; 451 AA.
AC Q21180;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Zinc metalloproteinase nas-16;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 16;
DE Flags: Precursor;
GN Name=nas-16; ORFNames=K03B8.1;
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 IDENTIFICATION, AND 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}.
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DR EMBL; Z74039; CAA98503.1; -; Genomic_DNA.
DR PIR; T23265; T23265.
DR RefSeq; NP_505889.2; NM_073488.2.
DR AlphaFoldDB; Q21180; -.
DR SMR; Q21180; -.
DR BioGRID; 51634; 3.
DR STRING; 6239.K03B8.1; -.
DR MEROPS; M12.A30; -.
DR PaxDb; Q21180; -.
DR EnsemblMetazoa; K03B8.1.1; K03B8.1.1; WBGene00003535.
DR GeneID; 186922; -.
DR KEGG; cel:CELE_K03B8.1; -.
DR UCSC; K03B8.1; c. elegans.
DR CTD; 186922; -.
DR WormBase; K03B8.1; CE51407; WBGene00003535; nas-16.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00970000196148; -.
DR HOGENOM; CLU_017286_1_1_1; -.
DR InParanoid; Q21180; -.
DR OMA; NCTISTR; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q21180; -.
DR PRO; PR:Q21180; -.
DR Proteomes; UP000001940; Chromosome V.
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 Gene3D; 3.40.390.10; -; 1.
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 3: Inferred from homology;
KW Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Zinc; Zymogen.
FT PROPEP 1..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000442663"
FT CHAIN ?..451
FT /note="Zinc metalloproteinase nas-16"
FT /id="PRO_0000028920"
FT DOMAIN 70..273
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 267..306
FT /note="EGF-like"
FT ACT_SITE 176
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 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 127..272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 148..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 274..291
FT /evidence="ECO:0000250"
FT DISULFID 296..305
FT /evidence="ECO:0000250"
SQ SEQUENCE 451 AA; 51508 MW; 3F04B96F5606A5A6 CRC64;
MGNLFKFSLN CIKYRSENLE KSKMFYQYFY FHLTLSIVLI YGSDIGKDAN EHMSSVPKKI
IIEGTRQKRQ VVTKLFSPQW SNAKVFYCNA DSFSKLQLKK LKLKKNSDTV KRKLMKFAMN
FISSQTCVTF EENCTISTRI KFVDSTFCAS YVGMINSVQE IYFPDWCMRF GSAVHELMHA
LGVLHTHARF DRDNFLNVNL NKDDEDDSNF EIVSPPFSIN VVPYEYGSTL HYTADVSGTN
SLLPKQMEYY RTLGNRRVTF YDMLTINTAY NCKCPSELLC ANGGYTNPSN CLECICPLGY
GGVLCDRVVA CSVQLSADSY WKGSWISVGS SVLRDTTDPV KAFISINAPK DKIIEVKIVK
IENFSCDSGC NNNGVEIKYM GDPRITNPII CCENQVDPSN KGYKAKLNPL LINIYTFLGK
NKVTFHYRYV NERLSSYNKT TNGYDNYEYY A
