ID NAS37_CAEEL Reviewed; 765 AA.
AC Q93243; Q5CZ39;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 27-MAR-2024, entry version 154.
DE RecName: Full=Zinc metalloproteinase nas-37;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 37;
DE Flags: Precursor;
GN Name=nas-37; ORFNames=C17G1.6;
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 [MRNA] (ISOFORM B), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, MUTAGENESIS OF HIS-214, AND DISRUPTION PHENOTYPE.
RX PubMed=15539494; DOI=10.1242/dev.01454;
RA Davis M.W., Birnie A.J., Chan A.C., Page A.P., Jorgensen E.M.;
RT "A conserved metalloprotease mediates ecdysis in Caenorhabditis elegans.";
RL Development 131:6001-6008(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 [3]
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 [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
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). Plays an essential role in
CC molting, a process during larval stages in which a new cuticle is
CC formed and the old cuticle is shed (PubMed:15255192). Required during
CC ecdysis, the opening of the cuticle to allow the worm to escape
CC (PubMed:15539494). {ECO:0000250|UniProtKB:A8Q2D1,
CC ECO:0000269|PubMed:15255192, ECO:0000269|PubMed:15539494}.
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:0000269|PubMed:15539494}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q93243-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q93243-2; Sequence=VSP_014343;
CC -!- TISSUE SPECIFICITY: Expressed in hypodermal cells. Not expressed in the
CC seam cells in L1 to L3 larvae, but it is present in seam cells of L4
CC larvae. Also expressed in attachment points of the cuticle at the
CC anterior end of larvae, in the arcade cells in the mouth, the anterior
CC pharynx, the amphid socket cells, and in the rectal epithelial cells at
CC the posterior end of the larvae (at protein level).
CC {ECO:0000269|PubMed:15255192, ECO:0000269|PubMed:15539494}.
CC -!- DEVELOPMENTAL STAGE: Present in hypodermal cells of the anterior
CC cuticle 4 hours before each molt and is shed in the cuticle after
CC ecdysis.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit incomplete ecdysis; at each molt
CC the cuticle fails to open sufficiently at the anterior end and the
CC partially shed cuticle is dragged behind the animal.
CC {ECO:0000269|PubMed:15539494}.
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DR EMBL; AY912076; AAX81408.1; -; mRNA.
DR EMBL; Z78415; CAB01675.2; -; Genomic_DNA.
DR EMBL; Z78415; CAI58633.1; -; Genomic_DNA.
DR PIR; T19366; T19366.
DR RefSeq; NP_001024413.1; NM_001029242.3. [Q93243-1]
DR RefSeq; NP_001024414.1; NM_001029243.4. [Q93243-2]
DR AlphaFoldDB; Q93243; -.
DR SMR; Q93243; -.
DR STRING; 6239.C17G1.6a.1; -.
DR MEROPS; M12.318; -.
DR GlyCosmos; Q93243; 1 site, No reported glycans.
DR EPD; Q93243; -.
DR PaxDb; 6239-C17G1-6a; -.
DR PeptideAtlas; Q93243; -.
DR EnsemblMetazoa; C17G1.6a.1; C17G1.6a.1; WBGene00003553. [Q93243-1]
DR EnsemblMetazoa; C17G1.6b.1; C17G1.6b.1; WBGene00003553. [Q93243-2]
DR GeneID; 181208; -.
DR KEGG; cel:CELE_C17G1.6; -.
DR UCSC; C17G1.6b; c. elegans. [Q93243-1]
DR AGR; WB:WBGene00003553; -.
DR WormBase; C17G1.6a; CE31417; WBGene00003553; nas-37. [Q93243-1]
DR WormBase; C17G1.6b; CE38034; WBGene00003553; nas-37. [Q93243-2]
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00970000196453; -.
DR InParanoid; Q93243; -.
DR OMA; NGCWSNV; -.
DR OrthoDB; 2875712at2759; -.
DR PhylomeDB; Q93243; -.
DR PRO; PR:Q93243; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003553; Expressed in adult organism and 1 other cell type or tissue.
DR GO; GO:0005576; C:extracellular region; IDA:WormBase.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:WormBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0040002; P:collagen and cuticulin-based cuticle development; IMP:WormBase.
DR GO; GO:0042395; P:ecdysis, collagen and cuticulin-based cuticle; IMP:WormBase.
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; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR000859; CUB_dom.
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 InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF876; ZINC METALLOPROTEINASE NAS-37; 1.
DR Pfam; PF01400; Astacin; 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; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cleavage on pair of basic residues;
KW Developmental protein; Disulfide bond; EGF-like domain; Glycoprotein;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..114
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442683"
FT CHAIN 115..765
FT /note="Zinc metalloproteinase nas-37"
FT /id="PRO_0000028941"
FT DOMAIN 115..308
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 303..343
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 350..458
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 576..627
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 513..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 156..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 177..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 311..331
FT /evidence="ECO:0000250"
FT DISULFID 333..342
FT /evidence="ECO:0000250"
FT DISULFID 350..374
FT /evidence="ECO:0000250"
FT DISULFID 400..420
FT /evidence="ECO:0000250"
FT DISULFID 588..621
FT /evidence="ECO:0000250"
FT DISULFID 592..626
FT /evidence="ECO:0000250"
FT DISULFID 604..611
FT /evidence="ECO:0000250"
FT VAR_SEQ 484..563
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:15539494"
FT /id="VSP_014343"
FT MUTAGEN 214
FT /note="H->R: In ox196; induces defects in protease involved
FT in ecdysis."
FT /evidence="ECO:0000269|PubMed:15539494"
SQ SEQUENCE 765 AA; 85180 MW; 8D9D9B43A584BA95 CRC64;
MKSQACLKVC LALIGLVSIV STAYIANDVV SDYAEVKELL AAFYRKHAKK YGHDYDPAAI
QAIAENMDKS VKNDKTEATV NRKLWNEVFE NDIILTLPQA ESLLSESNSP RSRRQAHPDP
RNFWPNLTIS YEFYGGEETW RQLIRSAIRH VEQNVCFKFK ENGGDRDGLR YYRGNGCWSN
VGRVGGRQLV SIGYGCDSLG IVSHETLHAL GLWHEQSRDD RDNFISIVAD KITRGTEGNF
AKRTAANSDN LGQPYDLGSV MHYGAKSFAY DWSSDTIKTR DWRYQNTIGQ RDGLSFKDAK
MINTRYCSNV CQRSLPCLNE GYTDPNNCGR CRCPSGYGGT YCETVEYTSC GGSLTASSSY
KKIESGIVQP DANCVWRIRN PGGNVEVMFD QVNFQCADPC QSYVEVKYLS QKTSTGARLC
CSLPSVIRSE GDDVIIILRG TPNTAVGWRG FTLKYRAIGG TPITPATVRP TYATTTRPYW
TRTASGWIHI KNPPLYKPDG QIYTSDEQSA ETKYSSEELY DPSTFLSPSS SSASPALLLP
SDASPQRPSA QEHDLSQLSQ NALTRPTPTT TVAPDTASWS AWGEWSACSQ PCGGCGTKTR
VRACYGGNQV CPGSNLDRES CNAHACAKPK KGMICNGRLL LPCDLLAKLN FGSNNYLNPK
LKQSGFARSS TLPLPRISQR KPVFVNELEV HPPTERFLSS STRRVKRQTA NRFCEKRFIY
QCPTALLTIQ MEYKPDTQGT NDAYFQQYPE CCSGYTPRRG VCYKN
//
