VM32A_GLOBR
ID VM32A_GLOBR Reviewed; 424 AA.
AC P0DM89;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like brevilysin H2a;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
OS Gloydius brevicaudus (Korean slamosa snake) (Agkistrodon halys
OS brevicaudus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=259325;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP GLYCOSYLATION AT ASN-69 AND ASN-185, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC TISSUE=Venom;
RA Terada S., Hattori T.;
RT "Characterization of brevilysin H2, an alpha-fibrinogenolytic
RT metalloproteinase from the venom of Chinese snake (Gloydius blomhoffi
RT brevicaudus).";
RL Fukuoka Univ. Sci. Rep. 43:29-38(2013).
CC -!- FUNCTION: Non-hemorrhagic metalloproteinase that degrades fibrinogen.
CC The alpha chain (FGA) is rapidly degraded, the beta chain (FGB) is
CC degraded very slowly, while the gamma chain is left intact. Shows a
CC prefential cleavage at X-Leu bonds. Cleaves insulin B chain at '29-
CC His-|-Leu-30', '33-Ser-|-His-34', '38-Ala-|-Leu-39' and '40-Tyr-|-Leu-
CC 41' bonds. {ECO:0000269|Ref.1}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Its proteolytic activity is inhibited by EDTA,
CC TPEN, 1,10-phenanthroline, and some thiol compounds, but is enhanced by
CC alkaline earth metal ions (Mg2+, Ca2+, Sr2+, and Ba2+). Its activity is
CC not modulated by urea (4 M). {ECO:0000269|Ref.1}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.5.;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: Glycosylated (Ref.1). {ECO:0000269|Ref.1}.
CC -!- MISCELLANEOUS: Does not show hemorrhagic activity (Ref.1).
CC -!- MISCELLANEOUS: The disintegrin domain belongs to the long disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DM89; -.
DR SMR; P0DM89; -.
DR PRIDE; P0DM89; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW Glycoprotein; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Pyrrolidone carboxylic acid; Secreted; Toxin; Zinc.
FT CHAIN 1..424
FT /note="Zinc metalloproteinase-disintegrin-like brevilysin
FT H2a"
FT /id="PRO_0000424620"
FT DOMAIN 9..207
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 215..301
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 279..281
FT /note="D/ECD-tripeptide"
FT ACT_SITE 146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|Ref.1"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.1"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.1"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..202
FT /evidence="ECO:0000250"
FT DISULFID 164..186
FT /evidence="ECO:0000250"
FT DISULFID 166..169
FT /evidence="ECO:0000250"
FT DISULFID 218..247
FT /evidence="ECO:0000250"
FT DISULFID 229..242
FT /evidence="ECO:0000250"
FT DISULFID 231..237
FT /evidence="ECO:0000250"
FT DISULFID 241..264
FT /evidence="ECO:0000250"
FT DISULFID 255..261
FT /evidence="ECO:0000250"
FT DISULFID 260..286
FT /evidence="ECO:0000250"
FT DISULFID 273..293
FT /evidence="ECO:0000250"
FT DISULFID 280..312
FT /evidence="ECO:0000250"
FT DISULFID 305..317
FT /evidence="ECO:0000250"
FT DISULFID 324..374
FT /evidence="ECO:0000250"
FT DISULFID 339..385
FT /evidence="ECO:0000250"
FT DISULFID 352..362
FT /evidence="ECO:0000250"
FT DISULFID 369..411
FT /evidence="ECO:0000250"
FT DISULFID 405..417
FT /evidence="ECO:0000250"
FT UNSURE 69
FT /note="Assigned by comparison with orthologs"
FT UNSURE 185
FT /note="Assigned by comparison with orthologs"
SQ SEQUENCE 424 AA; 46785 MW; C136D71170D68C44 CRC64;
QQRYLNAKRY VKLAIVADRS MVTKHNGKLK KLRKWIYRIV NTINEVYRSL NILVALVYLE
IWSKEDLINV TSAAKDTLAS FGNWRATDLL KRRSHDAAHL LTNIKFDGTT VGKAYVASMC
QQDSSVGINQ DHSKINLLVA LTMAHELGHN LGMSHDVVNT EKQCNCGTCV MAPTISDQIS
KLFSNCSKND YENFLTLYKP QCILNEPSKT DIVSPPVCGN ELLEVGEECD CGSPETCQNP
CCDAATCKLT SGSQCAKGLC CDQCKFSKSG TECRAAKDDC DIAESCTGQS ADCPTDDLQR
NGKPCQNNAG YCYNGKCPIM LNQCISFYGS NATVAPDICF NYNLKGEGNF YCRKEQATIF
PCAQKDKKCG RLFCVLGPTG KRISCKNTYS EDDPNYGMVD LGTKCEDGKV CNSNRECVDV
NTAY
