ID   NAS35_HAECO             Reviewed;         548 AA.
AC   D5FM34; D5FM33;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Zinc metalloproteinase dpy-31 {ECO:0000250|UniProtKB:P98060};
DE            EC=3.4.24.- {ECO:0000269|PubMed:19883650};
DE   AltName: Full=Nematode astacin 35 {ECO:0000303|PubMed:19883650};
DE   AltName: Full=Procollagen C-proteinase {ECO:0000250|UniProtKB:P98060};
DE   Flags: Precursor;
GN   Name=dpy-31 {ECO:0000303|PubMed:19883650};
GN   Synonyms=nas-35 {ECO:0000312|EMBL:ACZ64269.1};
OS   Haemonchus contortus (Barber pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Trichostrongyloidea; Haemonchidae; Haemonchus.
OX   NCBI_TaxID=6289 {ECO:0000312|EMBL:ACZ64269.1};
RN   [1] {ECO:0000312|EMBL:ACZ64269.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   ALTERNATIVE SPLICING.
RX   PubMed=19883650; DOI=10.1016/j.ijpara.2009.10.007;
RA   Stepek G., McCormack G., Page A.P.;
RT   "Collagen processing and cuticle formation is catalysed by the astacin
RT   metalloprotease DPY-31 in free-living and parasitic nematodes.";
RL   Int. J. Parasitol. 40:533-542(2010).
CC   -!- FUNCTION: Metalloprotease which cleaves the carboxyl terminus of
CC       procollagens to mature collagens. Probably involved in cuticular
CC       collagen maturation. {ECO:0000269|PubMed:19883650}.
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:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=dpy-31a {ECO:0000303|PubMed:19883650};
CC         IsoId=D5FM34-1; Sequence=Displayed;
CC       Name=dpy-31b {ECO:0000303|PubMed:19883650};
CC         IsoId=D5FM34-2; Sequence=VSP_059218;
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DR   EMBL; FJ812517; ACZ64268.1; -; Genomic_DNA.
DR   EMBL; FJ812517; ACZ64269.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5FM34; -.
DR   SMR; D5FM34; -.
DR   MEROPS; M12.321; -.
DR   BRENDA; 3.4.24.21; 2523.
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; 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   Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Signal; Zinc.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..150
FT                   /evidence="ECO:0000250|UniProtKB:P13497"
FT                   /id="PRO_0000442246"
FT   CHAIN           151..548
FT                   /note="Zinc metalloproteinase dpy-31"
FT                   /evidence="ECO:0000255|RuleBase:RU361183"
FT                   /id="PRO_5005126563"
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..547
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..546
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        529..546
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        541..546
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   VAR_SEQ         548
FT                   /note="C -> GEPVENQVCNTHPCNGLCAHKKTEDGECGGFLALLRGVRQANGPNFD
FT                   KSAVMACCHIVVGIVVLVEDVIFGVREIA (in isoform dpy-31b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_059218"
SQ   SEQUENCE   548 AA;  62762 MW;  2C37BD13F4B5B7FB CRC64;
     MSLLRSASLL LVVVTAALPP CTLGYSLHDG SRLDDVIAEF TAERRPRRLA TPAQRRLMGL
     TEEQHKTVQF YLDKLRELGN RRHPESYNKD SPKNEAYKWR KQMRDDLKTE LLNPEKYGRH
     FEGDIILFPE QAKQIYENAL KTGQRRVKRK FIGSDLRRWD PTRPIIYSFD GSHTSREQRI
     IELALEHRHN ITCLNFVRND NANKGNRIVF TDVDGCASNV GRHPLGEEQL VSLAPECIRL
     GVIAHEVAHA LGFWHEQSRP DRDQFVNVRW ENIDKDSKGQ FLKEDPDDVD NAGVPYDYGS
     IMHYRSKAFS RYDDLYTIST FVTDYQKTIG QRDQLSFNDI RLMNKIYCSN VCSRKLPCQR
     GGYTDPRRCD RCRCPDGFTG QFCEQVMPGY GAVCGGRIQV NSGWTRFSSP GYPREFKEGQ
     ECSWLLVAPP GQVVEMQFIG EFEMYCKVRH SLCMDYVEVR NSTDFANTGM RYCCYGTPST
     SIRSATTDLV VLFRSFYRGG RGFEARARAL PANGQWASWT PWTPCTASCG ACGSRMRTRV
     CPHGACPC