NAS22_CAEEL
ID NAS22_CAEEL Reviewed; 367 AA.
AC Q22398; Q70MS9;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Zinc metalloproteinase nas-22;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 22;
DE Flags: Precursor;
GN Name=nas-22; ORFNames=T11F9.6;
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 133-195, 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 uterine seam (utse) cell.
CC {ECO:0000269|PubMed:20109220}.
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DR EMBL; Z74042; CAA98530.2; -; Genomic_DNA.
DR EMBL; AJ561212; CAE47484.1; -; mRNA.
DR PIR; T24838; T24838.
DR RefSeq; NP_505908.2; NM_073507.3.
DR AlphaFoldDB; Q22398; -.
DR SMR; Q22398; -.
DR BioGRID; 53089; 1.
DR DIP; DIP-26108N; -.
DR MEROPS; M12.A43; -.
DR PaxDb; Q22398; -.
DR EnsemblMetazoa; T11F9.6.1; T11F9.6.1; WBGene00003541.
DR GeneID; 188423; -.
DR KEGG; cel:CELE_T11F9.6; -.
DR UCSC; T11F9.6; c. elegans.
DR CTD; 188423; -.
DR WormBase; T11F9.6; CE44156; WBGene00003541; nas-22.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00970000196541; -.
DR HOGENOM; CLU_017286_1_1_1; -.
DR InParanoid; Q22398; -.
DR OMA; INKYYEC; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q22398; -.
DR PRO; PR:Q22398; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003541; Expressed in adult organism 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 Gene3D; 3.40.390.10; -; 1.
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 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..16
FT /evidence="ECO:0000255"
FT PROPEP 17..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000442669"
FT CHAIN ?..367
FT /note="Zinc metalloproteinase nas-22"
FT /id="PRO_0000028926"
FT DOMAIN 41..237
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 232..270
FT /note="EGF-like"
FT ACT_SITE 139
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 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 111..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 238..258
FT /evidence="ECO:0000250"
FT DISULFID 260..269
FT /evidence="ECO:0000250"
SQ SEQUENCE 367 AA; 42514 MW; 56D8AAE1B5F497F9 CRC64;
MKSFFILLSI LQECYGKDIV ARIGGRNVAE KIGGARHRRQ VLIRGSDEER RHKWFNNTVH
YYFYEENFDF TVKESILRAM ELISNHTCIK FSTEPSEKSI RMESDSTTIA CYAEIGQVRE
NQLFSFNSDC YSAGVAVHEL IHSLGFIHAH QRSDRDQYLE FKKNLDELNQ TYQEQYKIWE
YQEILVPYDV GSVMQYPNEE DEEYYPVRKY RTMANTMGSA IVAFYDYLMI NKYYECSCAN
NLSCKNHGYP NPSNCSQCNC PYGFGGADCS QRAEPGATFQ ATETWQNVTI SLDAGYRYLE
NNQKLPQVDF IYQFLWIMAP ANKTTQIRVE KFVEGKCLPG CIRGGVEIKT NEDPRLTSPR
LCCEETS
