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Zinc metalloproteinase dpy-31 (EC 3.4.24.-) (Nematode astacin 35) (Procollagen C-proteinase)

 NAS35_TELCI             Reviewed;         614 AA.
A0A0C5PRQ1;
22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
29-APR-2015, sequence version 1.
31-JAN-2018, entry version 21.
RecName: Full=Zinc metalloproteinase dpy-31 {ECO:0000250|UniProtKB:P98060};
EC=3.4.24.- {ECO:0000269|PubMed:25736599, ECO:0000269|PubMed:26546217};
AltName: Full=Nematode astacin 35 {ECO:0000250|UniProtKB:P98060};
AltName: Full=Procollagen C-proteinase {ECO:0000250|UniProtKB:P98060};
Flags: Precursor;
Name=dpy-31 {ECO:0000312|EMBL:AJQ21780.1};
Synonyms=nas-35 {ECO:0000250|UniProtKB:P98060};
Teladorsagia circumcincta (Brown stomach worm) (Ostertagia
circumcincta).
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Strongylida; Trichostrongyloidea; Trichostrongylidae;
Trichostrongylinae; Teladorsagia.
NCBI_TaxID=45464 {ECO:0000312|EMBL:AJQ21780.1};
[1] {ECO:0000312|EMBL:AJQ21780.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND ENZYME
REGULATION.
PubMed=25736599; DOI=10.1016/j.ijpara.2015.01.004;
Stepek G., McCormack G., Winter A.D., Page A.P.;
"A highly conserved, inhibitable astacin metalloprotease from
Teladorsagia circumcincta is required for cuticle formation and
nematode development.";
Int. J. Parasitol. 45:345-355(2015).
[2]
CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=26546217; DOI=10.1016/j.bmcl.2015.10.077;
France D.J., Stepek G., Houston D.R., Williams L., McCormack G.,
Walkinshaw M.D., Page A.P.;
"Identification and activity of inhibitors of the essential nematode-
specific metalloprotease DPY-31.";
Bioorg. Med. Chem. Lett. 25:5752-5755(2015).
-!- FUNCTION: Metalloprotease which cleaves the carboxyl terminus of
procollagens to mature collagens. Probably involved in cuticular
collagen maturation. {ECO:0000250|UniProtKB:A8Q2D1}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|RuleBase:RU361183};
Note=Binds 1 zinc ion per subunit.
{ECO:0000255|RuleBase:RU361183};
-!- ENZYME REGULATION: Inhibited by marimastat and tripeptide
hydroxamic acids (PubMed:26546217). Inhibited by 1,10-
phenanthroline (PubMed:25736599). {ECO:0000269|PubMed:25736599,
ECO:0000269|PubMed:26546217}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- SIMILARITY: Belongs to the peptidase M12A family.
{ECO:0000255|RuleBase:RU004522, ECO:0000255|SAAS:SAAS00569975}.
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EMBL; KM272923; AJQ21780.1; -; Genomic_DNA.
ChEMBL; CHEMBL3739251; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IEA:InterPro.
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; 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; PF00431; CUB; 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; PS01180; CUB; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50092; TSP1; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Disulfide bond; EGF-like domain;
Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 24 {ECO:0000255}.
PROPEP 25 150 {ECO:0000250|UniProtKB:P13497}.
/FTId=PRO_0000442247.
CHAIN 151 614 Zinc metalloproteinase dpy-31.
{ECO:0000255}.
/FTId=PRO_5005111502.
DOMAIN 344 384 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 394 510 CUB. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 513 562 TSP type-1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
ACT_SITE 246 246 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 245 245 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 249 249 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 255 255 Zinc; catalytic.
{ECO:0000250|UniProtKB:P13497}.
CARBOHYD 190 190 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 461 461 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 348 358 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 352 372 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 374 383 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 394 422 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 525 556 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 529 561 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 541 546 {ECO:0000255|PROSITE-ProRule:PRU00210}.
SEQUENCE 614 AA; 69695 MW; BEB519E319F787C9 CRC64;
MSLLRCTTLL LVVVAIALPP CILGYSLHDG SRLDDFLTES AADRRPRRPT TAAQRRLMGL
TEEQYKTVHF YLNKLKELGN QRHPEGYDKD TTKDEADKWR KRMRDDIEGE LLNPEEYGRH
FEGDIILFPE QAKQIYENAL KTGQRRVKRK FIGSDLRRWD PTRPIVYSFD GSHTSREQRI
IELALEHWHN ITCLNFVRND NANSGNRIVF TDVDGCASNV GRHPLGEEQL VSLAPECIRL
GVIAHEVAHA LGFWHEQSRP DRDQFVNVRW ENIDKDSKGQ FLKEDPDDVD NAGVPYDYGS
IMHYRSKAFS RYDDLYTIST FVTDYQKTIG QRDQLSFNDI RLMNKIYCSN VCSRKLPCQR
GGYTDPRRCD RCRCPDGFTG QFCEQVMPGY GAVCGGRIQV NGGWTKFSSP GYPREFKEGQ
ECSWLLVAPH GQVVEMQFIG EFEMYCKVRH SLCMDYVEVR NSTDFANTGM RYCCYGTPST
SIRSATTDLV VLFRSFYRGG RGFEARARAL PANGQWASWS PWTPCTASCG ACGSRMRTRV
CSHGACAGEP VENQVCNTHP CNGLCAHKKT EDGECGGFLA LLRGVRCKQE RTVMEPCENA
CCPGFSVVGG RCVR


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