NAS18_CAEEL
ID NAS18_CAEEL Reviewed; 410 AA.
AC Q21179;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Zinc metalloproteinase nas-18;
DE EC=3.4.24.21 {ECO:0000250|UniProtKB:P07584};
DE AltName: Full=Nematode astacin 18;
DE Flags: Precursor;
GN Name=nas-18; ORFNames=K03B8.3;
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 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:P07584}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of peptide bonds in substrates containing five or
CC more amino acids, preferentially with Ala in P1', and Pro in P2'.;
CC EC=3.4.24.21; Evidence={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}.
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DR EMBL; Z74039; CAA98502.1; -; Genomic_DNA.
DR PIR; T23264; T23264.
DR RefSeq; NP_001309451.1; NM_001322588.1.
DR AlphaFoldDB; Q21179; -.
DR SMR; Q21179; -.
DR STRING; 6239.K03B8.3; -.
DR MEROPS; M12.A32; -.
DR PaxDb; Q21179; -.
DR EnsemblMetazoa; K03B8.3.1; K03B8.3.1; WBGene00003537.
DR GeneID; 186924; -.
DR KEGG; cel:CELE_K03B8.3; -.
DR UCSC; K03B8.3; c. elegans.
DR CTD; 186924; -.
DR WormBase; K03B8.3; CE51528; WBGene00003537; nas-18.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00970000196148; -.
DR HOGENOM; CLU_671285_0_0_1; -.
DR InParanoid; Q21179; -.
DR OMA; YANISTM; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q21179; -.
DR PRO; PR:Q21179; -.
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_0000442665"
FT CHAIN ?..410
FT /note="Zinc metalloproteinase nas-18"
FT /id="PRO_0000028922"
FT DOMAIN 73..262
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 256..295
FT /note="EGF-like"
FT ACT_SITE 169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 168
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 BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 141..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 263..283
FT /evidence="ECO:0000250"
FT DISULFID 285..294
FT /evidence="ECO:0000250"
SQ SEQUENCE 410 AA; 46271 MW; 0101D9E1D151EA6C CRC64;
MCASCLHNAN AASFLMETFS RHRLNFICIG KMNIFYNVTS LDNKYSFHNP SAPVPHSSHA
LSSRQAHFTS FRAPVAPPSR PRRSQLPSSA KLLYCFDSSF STEKRELMLF SMNFISSQTC
VTFEENCSIP NRVQLVNGKG CSSYIGMNNI VQHLTFNDTC IDFGTAVHEL MHALGVIHTH
SRLDRDNFLN INLTNVSKEM MHNYAIFNQS TNVVPYEYGS TMHYYANIST MFPKKSEYSA
TLGIGRVTFY DMVILNTAYN CKCPNELLCG NGGYTNPSKC SECICPLGYG GVLCDRPSLI
GKDTGLPLEV KDKIIEVKVV GIDNFFSYPT CLINGLEIKY MGDPRITNPI YCSADLINGK
SFRSKLNPLL MNIHTLFGKN KVTFHYRYVT ERLSGYNKTT NGYDNYEYYD
