NAS35_TELCI
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 03-AUG-2022, entry version 32.
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 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 Teladorsagia
RT circumcincta is required for cuticle formation and 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 hydroxamic
CC acids (PubMed:26546217). Inhibited by 1,10-phenanthroline
CC (PubMed:25736599). {ECO:0000269|PubMed:25736599,
CC ECO:0000269|PubMed:26546217}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; KM272923; AJQ21780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C5PRQ1; -.
DR SMR; A0A0C5PRQ1; -.
DR BindingDB; A0A0C5PRQ1; -.
DR ChEMBL; CHEMBL3739251; -.
DR MEROPS; M12.321; -.
DR BRENDA; 3.4.24.21; 8716.
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 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; 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 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
FT /evidence="ECO:0000255"
FT PROPEP 25..150
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442247"
FT CHAIN 151..614
FT /note="Zinc metalloproteinase dpy-31"
FT /evidence="ECO:0000255"
FT /id="PRO_5005111502"
FT DOMAIN 150..349
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 344..384
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 394..510
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 513..562
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT ACT_SITE 246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 193..348
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 216..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 352..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 374..383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 394..422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 525..556
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 529..561
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 541..546
FT /evidence="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
