NAS36_CAEEL
ID NAS36_CAEEL Reviewed; 617 AA.
AC Q18206;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Zinc metalloproteinase nas-36;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:D5FM38};
DE AltName: Full=Nematode astacin 36;
DE Flags: Precursor;
GN Name=nas-36; ORFNames=C26C6.3;
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 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).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15255192; DOI=10.1515/bc.2004.069;
RA Suzuki M., Sagoh N., Iwasaki H., Inoue H., Takahashi K.;
RT "Metalloproteases with EGF, CUB, and thrombospondin-1 domains function in
RT molting of Caenorhabditis elegans.";
RL Biol. Chem. 385:565-568(2004).
CC -!- FUNCTION: Metalloprotease (By similarity). Involved in molting, a
CC process during larval stages in which a new cuticle is formed and the
CC old cuticle is shed (PubMed:15255192). {ECO:0000250|UniProtKB:D5FM38,
CC ECO:0000269|PubMed:15255192}.
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 hypodermal cells. Also detected in the
CC hypodermal seam cells in L4 larvae and young adults. In old adult
CC hermaphrodites, it localizes to the vulva (at protein level).
CC {ECO:0000269|PubMed:15255192}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit a trail of old cuticle that remains
CC attached to the posterior part of the body.
CC {ECO:0000269|PubMed:15255192}.
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DR EMBL; Z72503; CAA96596.2; -; Genomic_DNA.
DR PIR; T19477; T19477.
DR RefSeq; NP_492109.2; NM_059708.3.
DR AlphaFoldDB; Q18206; -.
DR SMR; Q18206; -.
DR BioGRID; 37948; 9.
DR STRING; 6239.C26C6.3; -.
DR MEROPS; M12.319; -.
DR EPD; Q18206; -.
DR PaxDb; Q18206; -.
DR PeptideAtlas; Q18206; -.
DR PRIDE; Q18206; -.
DR EnsemblMetazoa; C26C6.3.1; C26C6.3.1; WBGene00003552.
DR GeneID; 172506; -.
DR KEGG; cel:CELE_C26C6.3; -.
DR UCSC; C26C6.3; c. elegans.
DR CTD; 172506; -.
DR WormBase; C26C6.3; CE38281; WBGene00003552; nas-36.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000170755; -.
DR HOGENOM; CLU_017286_1_3_1; -.
DR InParanoid; Q18206; -.
DR OMA; GQGCYSM; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q18206; -.
DR PRO; PR:Q18206; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003552; Expressed in pharyngeal muscle cell (C elegans) and 3 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; IMP:WormBase.
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; IPR033957; NAS-36.
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 PANTHER; PTHR10127:SF849; PTHR10127:SF849; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00090; TSP_1; 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 SUPFAM; SSF82895; SSF82895; 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 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Developmental protein; Disulfide bond;
KW EGF-like domain; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..126
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442249"
FT CHAIN 127..617
FT /note="Zinc metalloproteinase nas-36"
FT /id="PRO_0000028940"
FT DOMAIN 127..322
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 317..358
FT /note="EGF-like"
FT DOMAIN 368..482
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 507..556
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT ACT_SITE 220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 169..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 192..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 325..346
FT /evidence="ECO:0000250"
FT DISULFID 348..357
FT /evidence="ECO:0000250"
FT DISULFID 368..397
FT /evidence="ECO:0000250"
FT DISULFID 425..445
FT /evidence="ECO:0000250"
FT DISULFID 519..550
FT /evidence="ECO:0000250"
FT DISULFID 523..555
FT /evidence="ECO:0000250"
FT DISULFID 535..540
FT /evidence="ECO:0000250"
SQ SEQUENCE 617 AA; 69462 MW; 4970A25BF228E719 CRC64;
MRLCHSIILF NSLISISICS KADDPALLVA SEFKEHFNVE EKQLETVEEL LIKMKKLAHS
RSFKGREFGH DAVEDSKKEV AISTQQGTIN KKVSPFLFEG DIFLSRRQAV DILKALSKDK
TKRLRRSFVS DKTATWKTMP IKYRFHESID FYTISQIIAA IRFWEDSTCI TFENVSDSPD
GDYIEFFSGQ GCYSMIGRNG GRQGISIGES CVKMGVIEHE IGHALGLWHE QSRPDALGYV
TIERDFILPS YISDFLQRDD EIDTLGIPYD LGSVMHYGST AFSVDQKSKT VVTRDSLYQQ
TIGQREKLSF YDVATINTAY CKDECKSEKT KCENGGYMRP SKCSECLCPD GLGGEKCEKN
EDSKNAECGG IIKLTEEWKE IESPNYPDPG YEADQKCSWL LKAEKGKRVE IEFIEDFSFL
CTSTCVDFVE LKISDDLRNT GFRFCCYDKP EISFVSQTDT AIIIFRSQLS TDIGFKIQAK
STDAEPRTTI APTIITTTLA PITVDAPNVW ADWGEWSMCS RTCGGCGIRS RVRSCRSKKC
EGRRQEFGTC NLKACPVDKH CAKLLSNNRL CNGKVCTKND IAISSCDAPQ CCPPFINVDG
VCQSDQENQH DELWLSI
