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Zinc metalloproteinase nas-37 (EC 3.4.24.-) (Nematode astacin 37)

 NAS37_CAEEL             Reviewed;         765 AA.
Q93243; Q5CZ39;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 2.
12-SEP-2018, entry version 131.
RecName: Full=Zinc metalloproteinase nas-37;
EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
AltName: Full=Nematode astacin 37;
Flags: Precursor;
Name=nas-37; ORFNames=C17G1.6;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF HIS-214, AND DISRUPTION
PHENOTYPE.
PubMed=15539494; DOI=10.1242/dev.01454;
Davis M.W., Birnie A.J., Chan A.C., Page A.P., Jorgensen E.M.;
"A conserved metalloprotease mediates ecdysis in Caenorhabditis
elegans.";
Development 131:6001-6008(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
IDENTIFICATION, AND NOMENCLATURE.
PubMed=14653817; DOI=10.1046/j.1432-1033.2003.03891.x;
Moehrlen F., Hutter H., Zwilling R.;
"The astacin protein family in Caenorhabditis elegans.";
Eur. J. Biochem. 270:4909-4920(2003).
[4]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15255192; DOI=10.1515/BC.2004.069;
Suzuki M., Sagoh N., Iwasaki H., Inoue H., Takahashi K.;
"Metalloproteases with EGF, CUB, and thrombospondin-1 domains function
in molting of Caenorhabditis elegans.";
Biol. Chem. 385:565-568(2004).
-!- FUNCTION: Metalloprotease (By similarity). Plays an essential role
in molting, a process during larval stages in which a new cuticle
is formed and the old cuticle is shed (PubMed:15255192). Required
during ecdysis, the opening of the cuticle to allow the worm to
escape (PubMed:15539494). {ECO:0000250|UniProtKB:A8Q2D1,
ECO:0000269|PubMed:15255192, ECO:0000269|PubMed:15539494}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|PROSITE-ProRule:PRU01211};
Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
ProRule:PRU01211};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15539494}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=a;
IsoId=Q93243-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=b;
IsoId=Q93243-2; Sequence=VSP_014343;
-!- TISSUE SPECIFICITY: Expressed in hypodermal cells. Not expressed
in the seam cells in L1 to L3 larvae, but it is present in seam
cells of L4 larvae. Also expressed in attachment points of the
cuticle at the anterior end of larvae, in the arcade cells in the
mouth, the anterior pharynx, the amphid socket cells, and in the
rectal epithelial cells at the posterior end of the larvae (at
protein level). {ECO:0000269|PubMed:15255192,
ECO:0000269|PubMed:15539494}.
-!- DEVELOPMENTAL STAGE: Present in hypodermal cells of the anterior
cuticle 4 hours before each molt and is shed in the cuticle after
ecdysis.
-!- DISRUPTION PHENOTYPE: Worms exhibit incomplete ecdysis; at each
molt the cuticle fails to open sufficiently at the anterior end
and the partially shed cuticle is dragged behind the animal.
{ECO:0000269|PubMed:15539494}.
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EMBL; AY912076; AAX81408.1; -; mRNA.
EMBL; Z78415; CAB01675.2; -; Genomic_DNA.
EMBL; Z78415; CAI58633.1; -; Genomic_DNA.
PIR; T19366; T19366.
RefSeq; NP_001024413.1; NM_001029242.3. [Q93243-1]
RefSeq; NP_001024414.1; NM_001029243.4. [Q93243-2]
UniGene; Cel.5964; -.
ProteinModelPortal; Q93243; -.
STRING; 6239.C17G1.6a; -.
MEROPS; M12.318; -.
EPD; Q93243; -.
PaxDb; Q93243; -.
PeptideAtlas; Q93243; -.
PRIDE; Q93243; -.
EnsemblMetazoa; C17G1.6a; C17G1.6a; WBGene00003553. [Q93243-1]
GeneID; 181208; -.
KEGG; cel:CELE_C17G1.6; -.
UCSC; C17G1.6b; c. elegans. [Q93243-1]
CTD; 181208; -.
WormBase; C17G1.6a; CE31417; WBGene00003553; nas-37. [Q93243-1]
WormBase; C17G1.6b; CE38034; WBGene00003553; nas-37. [Q93243-2]
eggNOG; KOG3714; Eukaryota.
eggNOG; ENOG410ZPX7; LUCA.
GeneTree; ENSGT00760000119227; -.
HOGENOM; HOG000016555; -.
InParanoid; Q93243; -.
OMA; IGYGCDS; -.
OrthoDB; EOG091G0N5F; -.
PhylomeDB; Q93243; -.
PRO; PR:Q93243; -.
Proteomes; UP000001940; Chromosome X.
Bgee; WBGene00003553; Expressed in 3 organ(s), highest expression level in multi-cellular organism.
GO; GO:0005576; C:extracellular region; IDA:WormBase.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:WormBase.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0040002; P:collagen and cuticulin-based cuticle development; IMP:WormBase.
GO; GO:0042395; P:ecdysis, collagen and cuticulin-based cuticle; IMP:WormBase.
GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IMP:WormBase.
CDD; cd00041; CUB; 1.
CDD; cd04280; ZnMc_astacin_like; 1.
Gene3D; 2.20.100.10; -; 1.
Gene3D; 2.60.120.290; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR034035; Astacin-like_dom.
InterPro; IPR000859; CUB_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR017050; Metallopeptidase_nem.
InterPro; IPR001506; Peptidase_M12A.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR035914; Sperma_CUB_dom_sf.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
Pfam; PF01400; Astacin; 1.
Pfam; PF00090; TSP_1; 1.
PIRSF; PIRSF036365; Astacin_nematoda; 1.
PRINTS; PR00480; ASTACIN.
SMART; SM00042; CUB; 1.
SMART; SM00209; TSP1; 1.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF49854; SSF49854; 1.
SUPFAM; SSF82895; SSF82895; 1.
PROSITE; PS51864; ASTACIN; 1.
PROSITE; PS01180; CUB; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS50092; TSP1; 1.
1: Evidence at protein level;
Alternative splicing; Cleavage on pair of basic residues;
Complete proteome; Developmental protein; Disulfide bond;
EGF-like domain; Glycoprotein; Hydrolase; Metal-binding;
Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc;
Zymogen.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 114 {ECO:0000250|UniProtKB:P13497}.
/FTId=PRO_0000442683.
CHAIN 115 765 Zinc metalloproteinase nas-37.
/FTId=PRO_0000028941.
DOMAIN 115 308 Peptidase M12A. {ECO:0000255|PROSITE-
ProRule:PRU01211}.
DOMAIN 303 343 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 350 458 CUB. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 576 627 TSP type-1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
COMPBIAS 527 534 Poly-Ser.
ACT_SITE 205 205 {ECO:0000255|PROSITE-ProRule:PRU01211}.
METAL 204 204 Zinc; via tele nitrogen; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU01211}.
METAL 208 208 Zinc; via tele nitrogen; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU01211}.
METAL 214 214 Zinc; via tele nitrogen; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU01211}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 156 307 {ECO:0000255|PROSITE-ProRule:PRU01211}.
DISULFID 177 196 {ECO:0000255|PROSITE-ProRule:PRU01211}.
DISULFID 311 331 {ECO:0000250}.
DISULFID 333 342 {ECO:0000250}.
DISULFID 350 374 {ECO:0000250}.
DISULFID 400 420 {ECO:0000250}.
DISULFID 588 621 {ECO:0000250}.
DISULFID 592 626 {ECO:0000250}.
DISULFID 604 611 {ECO:0000250}.
VAR_SEQ 484 563 Missing (in isoform b).
{ECO:0000303|PubMed:15539494}.
/FTId=VSP_014343.
MUTAGEN 214 214 H->R: In ox196; induces defects in
protease involved in ecdysis.
{ECO:0000269|PubMed:15539494}.
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


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