NAS38_CAEEL
ID NAS38_CAEEL Reviewed; 745 AA.
AC Q20942;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Zinc metalloproteinase nas-38;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 38;
DE Flags: Precursor;
GN Name=nas-38; ORFNames=F57C12.1;
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; FO081141; CCD69445.1; -; Genomic_DNA.
DR PIR; D89447; D89447.
DR RefSeq; NP_508120.2; NM_075719.4.
DR AlphaFoldDB; Q20942; -.
DR SMR; Q20942; -.
DR STRING; 6239.F57C12.1; -.
DR MEROPS; M12.A28; -.
DR EPD; Q20942; -.
DR PaxDb; Q20942; -.
DR PRIDE; Q20942; -.
DR EnsemblMetazoa; F57C12.1.1; F57C12.1.1; WBGene00003554.
DR UCSC; F57C12.1; c. elegans.
DR WormBase; F57C12.1; CE31188; WBGene00003554; nas-38.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000169640; -.
DR HOGENOM; CLU_017286_1_3_1; -.
DR InParanoid; Q20942; -.
DR OMA; SRWNNFQ; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q20942; -.
DR PRO; PR:Q20942; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003554; 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; 2.20.100.10; -; 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; 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 InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_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; SM00209; TSP1; 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; PS50092; TSP1; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
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..25
FT /evidence="ECO:0000255"
FT PROPEP 26..114
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442684"
FT CHAIN 115..745
FT /note="Zinc metalloproteinase nas-38"
FT /id="PRO_0000028942"
FT DOMAIN 113..312
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 306..345
FT /note="EGF-like"
FT DOMAIN 371..487
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 628..676
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 491..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 671
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 732
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 158..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 179..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 315..331
FT /evidence="ECO:0000250"
FT DISULFID 336..345
FT /evidence="ECO:0000250"
FT DISULFID 371..401
FT /evidence="ECO:0000250"
FT DISULFID 429..450
FT /evidence="ECO:0000250"
FT DISULFID 641..670
FT /evidence="ECO:0000250"
FT DISULFID 645..675
FT /evidence="ECO:0000250"
FT DISULFID 657..662
FT /evidence="ECO:0000250"
SQ SEQUENCE 745 AA; 83350 MW; B94630CE86366D95 CRC64;
MPSPSYNRHI IIASCFCCLL IFSSAARVPK ASKKHLARVK QLLNDEAERH NTLIQSDSVT
VFDDIQRNPN TGVHHDELAV NNADEYFQGD VDLSEQQVKI IEDQFTQGKR EKRKIGRNPL
YKKWDTRGPI SFDYAESIPF QTRQKIRSAM LLWQQHTCLR FEEGGPNVDR LEFFDGGGCS
SFVGRVGGTQ GISISTPGCD VVGIISHEIG HALGIFHEQA RPDQERHIAI NYNNIPLSRW
NNFQAVGENH AETYNLPYDT GSVMHYGPYG FASDPYTPTI RTLERVQQST IGQRAGPSFL
DYQAINMAYG CTESCADLPC LRNGYTHPNN CSMCACPEGL SGRYCEQVYP SNAQCARGKL
TRERHINERE CYQSAIWTAT KEVKYITSPN YPDKFPIDTE CNWIIAAPIE GRVFMEFEGD
FDFLCEDTCD KAYVEVKYHS DKRLTGARYC CSLLPKNRFI SFKNEMIIIM RGYRSSGAGF
KAKFWSNLGE PEGVSTPLPP TTAPLPEISE TTQKPEPTTV QSTTTYTTAI PRRTAKKQFF
TRKPITIPLT PLTSSSTTTE STTVSSTTQS TTWLPTEPSF ATGETEITTA SPTITLFPSL
STILPPINSL AGVLPSTQAP DIINSVLECG CGAWSEWQGE CSQQCGGCGH RLRKRECKKE
ACRKEEKRPC NFSACPDGTN FLINNAEFHI LWRGCCVGLF RSGDQCSALE TESNPFFKII
NSLLNIQDAK NNDTLIAKRM MRGEH
