GenomeNet

Database: UniProt
Entry: A0A0C5PRQ1
LinkDB: A0A0C5PRQ1
Original site: A0A0C5PRQ1 
ID   NAS35_TELCI             Reviewed;         614 AA.
AC   A0A0C5PRQ1;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2015, sequence version 1.
DT   07-NOV-2018, entry version 24.
DE   RecName: Full=Zinc metalloproteinase dpy-31 {ECO:0000250|UniProtKB:P98060};
DE            EC=3.4.24.- {ECO:0000269|PubMed:25736599, ECO:0000269|PubMed:26546217};
DE   AltName: Full=Nematode astacin 35 {ECO:0000250|UniProtKB:P98060};
DE   AltName: Full=Procollagen C-proteinase {ECO:0000250|UniProtKB:P98060};
DE   Flags: Precursor;
GN   Name=dpy-31 {ECO:0000312|EMBL:AJQ21780.1};
GN   Synonyms=nas-35 {ECO:0000250|UniProtKB:P98060};
OS   Teladorsagia circumcincta (Brown stomach worm) (Ostertagia
OS   circumcincta).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Trichostrongyloidea; Haemonchidae; Teladorsagia.
OX   NCBI_TaxID=45464 {ECO:0000312|EMBL:AJQ21780.1};
RN   [1] {ECO:0000312|EMBL:AJQ21780.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND ACTIVITY
RP   REGULATION.
RX   PubMed=25736599; DOI=10.1016/j.ijpara.2015.01.004;
RA   Stepek G., McCormack G., Winter A.D., Page A.P.;
RT   "A highly conserved, inhibitable astacin metalloprotease from
RT   Teladorsagia circumcincta is required for cuticle formation and
RT   nematode development.";
RL   Int. J. Parasitol. 45:345-355(2015).
RN   [2]
RP   CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=26546217; DOI=10.1016/j.bmcl.2015.10.077;
RA   France D.J., Stepek G., Houston D.R., Williams L., McCormack G.,
RA   Walkinshaw M.D., Page A.P.;
RT   "Identification and activity of inhibitors of the essential nematode-
RT   specific metalloprotease DPY-31.";
RL   Bioorg. Med. Chem. Lett. 25:5752-5755(2015).
CC   -!- FUNCTION: Metalloprotease which cleaves the carboxyl terminus of
CC       procollagens to mature collagens. Probably involved in cuticular
CC       collagen maturation. {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   -!- ACTIVITY REGULATION: Inhibited by marimastat and tripeptide
CC       hydroxamic acids (PubMed:26546217). Inhibited by 1,10-
CC       phenanthroline (PubMed:25736599). {ECO:0000269|PubMed:25736599,
CC       ECO:0000269|PubMed:26546217}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
DR   EMBL; KM272923; AJQ21780.1; -; Genomic_DNA.
DR   ChEMBL; CHEMBL3739251; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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   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; IPR013032; EGF-like_CS.
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   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; PS01186; EGF_2; 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; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   PROPEP       25    150       {ECO:0000250|UniProtKB:P13497}.
FT                                /FTId=PRO_0000442247.
FT   CHAIN       151    614       Zinc metalloproteinase dpy-31.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_5005111502.
FT   DOMAIN      150    349       Peptidase M12A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01211}.
FT   DOMAIN      344    384       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      394    510       CUB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      513    562       TSP type-1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   ACT_SITE    246    246       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       245    245       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       249    249       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       255    255       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   CARBOHYD    190    190       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    461    461       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   DISULFID    193    348       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    216    237       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    352    372       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    374    383       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    394    422       {ECO:0000255|PROSITE-ProRule:PRU00059}.
FT   DISULFID    525    556       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    529    561       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    541    546       {ECO:0000255|PROSITE-ProRule:PRU00210}.
SQ   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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