NAS36_BRUMA
ID NAS36_BRUMA Reviewed; 581 AA.
AC D5FM38;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Zinc metalloproteinase nas-36 {ECO:0000305};
DE EC=3.4.24.- {ECO:0000269|PubMed:20800010};
DE AltName: Full=Nematode astacin 36 {ECO:0000250|UniProtKB:Q18206};
DE Flags: Precursor;
GN Name=nas-36 {ECO:0000312|WormBase:Bm2394}; Synonyms=Bm1_07340;
GN ORFNames=Bm2394 {ECO:0000312|WormBase:Bm2394};
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:ACZ64273.1};
RN [1] {ECO:0000312|EMBL:ACZ64273.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RX PubMed=20800010; DOI=10.1017/s0031182010001113;
RA Stepek G., McCormack G., Birnie A.J., Page A.P.;
RT "The astacin metalloprotease moulting enzyme NAS-36 is required for normal
RT cuticle ecdysis in free-living and parasitic nematodes.";
RL Parasitology 138:237-248(2011).
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).
CC -!- FUNCTION: Metalloprotease. Involved in molting, a process during larval
CC stages in which a new cuticle is formed and the old cuticle is shed.
CC {ECO:0000269|PubMed:20800010}.
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 1,10-phenanthroline.
CC {ECO:0000269|PubMed:20800010}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJ812520; ACZ64273.1; -; Genomic_DNA.
DR EMBL; LN856752; CDQ04813.2; -; Genomic_DNA.
DR RefSeq; XP_001892937.1; XM_001892902.1.
DR AlphaFoldDB; D5FM38; -.
DR SMR; D5FM38; -.
DR STRING; 6279.D5FM38; -.
DR MEROPS; M12.319; -.
DR EnsemblMetazoa; Bm2394.1; Bm2394.1; WBGene00222655.
DR GeneID; 6096396; -.
DR KEGG; bmy:BM_BM2394; -.
DR WBParaSite; Bm2394.1; Bm2394.1; WBGene00222655.
DR CTD; 6096396; -.
DR WormBase; Bm2394; BM02521; WBGene00222655; nas-36.
DR OrthoDB; 681837at2759; -.
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; 2.20.100.10; -; 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; IPR033957; NAS-36.
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 PANTHER; PTHR10127:SF849; PTHR10127:SF849; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00090; TSP_1; 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 Reference proteome; Secreted; Zinc; Zymogen.
FT PROPEP 1..95
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442250"
FT CHAIN 96..581
FT /note="Zinc metalloproteinase nas-36"
FT /id="PRO_0000442251"
FT DOMAIN 97..290
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 285..325
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 336..449
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 474..523
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT ACT_SITE 187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 137..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 159..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 293..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 315..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 336..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 486..517
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 490..522
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 502..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 581 AA; 65102 MW; 2C0A0A21DC9E2294 CRC64;
MKEIAHSQAY GNRVFSRDSA VDSKKDVSIS AEQPKTISKL TPYLFEGDIF LSTKQAMNIL
DSLASKNKTN KKGQQRMAHD APLYLFRGAN EKGKRFAAEY DAKWFQFPIK YRFDESLDIL
HISQILKALE IWQSNTCIKF ENDQEASGDY IEFFEGDGCY SMVGRFGGRQ GISIGKGCER
TGTIIHEVGH TLGLWHEQSR PDAEEYITVV KEYIIPSYIS EFLTRSEHEI TTFNVPYDLG
SVMHYGSTAF SIDQRSKTLL TKDPFYQMTI GQRDSLSFYN IKLINEAYCK GDCKEKNECK
NGGYLNPSNC QSCLCPSGFG GSKCEMHASS ESNSKCGGTL KAIIDWQYIE SPGYPDGYPT
NVICNWLIET DKEERIEISF EDNFGIFCSS TCVDYIELKI GNDLANTGYR ICCYDKPNDS
LVSAKYQAVI IFRATTGEDT GFKLKFRKTM KPAQTTPSLP KTTTTAPHTT IVGNDIWSEW
GEWSQCSRSC GACGIKSRLR ICKTAQCSGK VQQFLTCNLQ ACPVDIRCTK VKFKNRLCAD
GNTCGKPGEL LSSCSRPSCC PPFENVDGKC QTDQPLLIPL E
