NAS35_BRUMA
ID NAS35_BRUMA Reviewed; 599 AA.
AC A8Q2D1; D5FM35; D5FM36;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Zinc metalloproteinase dpy-31 {ECO:0000250|UniProtKB:P98060};
DE EC=3.4.24.- {ECO:0000269|PubMed:19883650, ECO:0000269|PubMed:26546217};
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:0000312|WormBase:Bm5432};
GN Synonyms=nas-35 {ECO:0000312|EMBL:ACZ64270.1};
GN ORFNames=Bm5432 {ECO:0000312|WormBase:Bm5432};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000312|EMBL:ACZ64270.1};
RN [1] {ECO:0000312|EMBL:ACZ64270.1}
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).
RN [2] {ECO:0000312|Proteomes:UP000006672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K.S., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.-W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [3]
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: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 -!- ACTIVITY REGULATION: Inhibited by marimastat and tripeptide hydroxamic
CC acids. {ECO:0000269|PubMed:26546217}.
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=A8Q2D1-1; Sequence=Displayed;
CC Name=dpy-31b {ECO:0000303|PubMed:19883650};
CC IsoId=A8Q2D1-2; Sequence=VSP_059217;
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DR EMBL; FJ812518; ACZ64270.1; -; Genomic_DNA.
DR EMBL; FJ812518; ACZ64271.1; -; Genomic_DNA.
DR EMBL; LN857013; CRZ25723.1; -; Genomic_DNA.
DR AlphaFoldDB; A8Q2D1; -.
DR SMR; A8Q2D1; -.
DR STRING; 6279.A8Q2D1; -.
DR BindingDB; A8Q2D1; -.
DR ChEMBL; CHEMBL3739250; -.
DR MEROPS; M12.321; -.
DR EnsemblMetazoa; Bm5432a.1; Bm5432a.1; WBGene00225693. [A8Q2D1-1]
DR WBParaSite; Bm5432a.1; Bm5432a.1; WBGene00225693.
DR WormBase; Bm5432; BM29748; WBGene00225693; dpy-31.
DR InParanoid; A8Q2D1; -.
DR OMA; CMDYVEV; -.
DR OrthoDB; 1821862at2759; -.
DR Proteomes; UP000006672; Unassembled WGS sequence.
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; 2.60.120.290; -; 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 Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 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 PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 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; Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..211
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442244"
FT CHAIN 212..599
FT /note="Zinc metalloproteinase dpy-31"
FT /id="PRO_0000442245"
FT DOMAIN 211..410
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 405..445
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 455..571
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT ACT_SITE 307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 254..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 277..298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 413..433
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 435..444
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 455..483
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT VAR_SEQ 575..599
FT /note="VFNIRTVRSMDEFNANLNKHAVADS -> GLFLAWSEWSACNASYGAQHRIR
FT HRRRICVDGACMLV (in isoform dpy-31b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059217"
SQ SEQUENCE 599 AA; 68968 MW; 8DDFCC386FFDC2B0 CRC64;
MALLKPFLSR TFSSFFATIT GGRNLIDSIE ELITTNYWLI FVMIIVCTCS APSNGAFFLN
DPYGYPFVSL QDDSIESVSA TTITTTTIIS TIITTTTATQ RIFQEKAKTF GQSAEEIQKV
KYYLEKIQKF EAKQHPEEIR QQHTTKNSEA IKDDLQIAVE VAKFEKRQKD SITLNPEENG
QYYEGDIVLD AQQAHEIYES MIQHGRRTKR KFIRSELRRW DSHKPIIYSF DGSHTIREQR
VIELALEHWH NITCLNFERR DDEIQENRIV FTDVDGCASN VGRHPLGEPQ FVSLAPECIR
LGVIAHEVAH ALGFWHEQSR PDRDNYVTVR WENIDRDSKG QFLKELPTDV DNGDVPYDYG
SIMHYRSKAF GRYEDLFTLN TNIMDYQKTI GQRDQLSFND IRLMNVIYCS DSCAQKLPCQ
RGGYTDPRRC GRCRCPDGFT GKLCERIMPG FGADCGGRIE LTSSWKRITS PNYPRDFKEG
QECSWLLVAP PGQRVQLRFY GEFEMYCKVR HSLCMDYIEI RNSTDFANTG MRYCCYGTPK
SSIMSATEDM LVLFRSFYRG GKGFQAQVRA LPTTVFNIRT VRSMDEFNAN LNKHAVADS
