VM25A_BITAR
ID VM25A_BITAR Reviewed; 515 AA.
AC P0DM97;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Zinc metalloproteinase-disintegrin BA-5A;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Bitis arietans (African puff adder).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX NCBI_TaxID=8692;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=16786436; DOI=10.1007/s00239-005-0268-z;
RA Juarez P., Wagstaff S.C., Oliver J., Sanz L., Harrison R.A., Calvete J.J.;
RT "Molecular cloning of disintegrin-like transcript BA-5A from a Bitis
RT arietans venom gland cDNA library: a putative intermediate in the evolution
RT of the long-chain disintegrin bitistatin.";
RL J. Mol. Evol. 63:142-152(2006).
CC -!- FUNCTION: Snake venom zinc metalloprotease that possesses hemorrhagic
CC activity and degrades alpha chain of fibrinogen (FGA) (By similarity).
CC May inhibit alpha-2/beta-1 integrin (ITGA2/ITGB1). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: The disintegrin domain belongs to the long disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Contains the typical disintegrin-like domain of the P-III
CC subfamily, but lacks the cysteine-rich domain like in P-II subfamily.
CC This protein may represent an intermediate in the evolutionary pathway
CC along the structural diversification pathway of disintegrin
CC (PubMed:16786436). {ECO:0000305|PubMed:16786436}.
CC -!- CAUTION: This protein has not been detected in the venom.
CC {ECO:0000305|PubMed:16786436}.
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 AlphaFoldDB; P0DM97; -.
DR SMR; P0DM97; -.
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:UniProtKB-KW.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
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; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
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 2: Evidence at transcript level;
KW Cell adhesion impairing toxin; Disulfide bond; Glycoprotein;
KW Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..193
FT /evidence="ECO:0000250"
FT /id="PRO_0000424725"
FT CHAIN 194..515
FT /note="Zinc metalloproteinase-disintegrin BA-5A"
FT /id="PRO_0000424726"
FT DOMAIN 203..399
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 407..493
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 471..473
FT /note="D/ECD-tripeptide"
FT ACT_SITE 340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 314..394
FT /evidence="ECO:0000250"
FT DISULFID 354..378
FT /evidence="ECO:0000250"
FT DISULFID 356..361
FT /evidence="ECO:0000250"
FT DISULFID 410..429
FT /evidence="ECO:0000250"
FT DISULFID 421..439
FT /evidence="ECO:0000250"
FT DISULFID 423..434
FT /evidence="ECO:0000250"
FT DISULFID 433..456
FT /evidence="ECO:0000250"
FT DISULFID 447..453
FT /evidence="ECO:0000250"
FT DISULFID 452..478
FT /evidence="ECO:0000250"
FT DISULFID 465..485
FT /evidence="ECO:0000250"
FT DISULFID 472..497
FT /evidence="ECO:0000250"
SQ SEQUENCE 515 AA; 58718 MW; A26D55B8BFD82D69 CRC64;
MMQVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPQKVT ALPKGAVQQA EQKYEDAMQY
EFEVNGQPVV LHLEKNKDLF SEDYSETHYS PDGKEITTNP PIEDHCYYHG RIQNDAHSTA
SISACNGLKG HFKLRGETYL IEPLKIPDSE AHAVYKYENI EKEDDAPKMC GVTQTNWESD
EPIKEASQLV ATSDQQRYYD HFRYIKYFIV VDHRMVEKYN GNLRTIRRRI YQLVNILNEI
YLPWNIRAPL VGIEFWNQRD LINVTSSAPY TLDLFGKWRA SDLLNRKIHD YTHLLTAIVF
VEQILGMAHI ATMCHSELSV GLVQDYMPSE HVVAAIMVHE MGHNLGISHD EKYCNCGADS
CIMYPQISIP PPVYFSNCSW EQYQNFLTIY KPDCTLIRPS RTDIVSPPVC GNDILEQGEE
CDCGSPEKCQ DPCCDAASCK LHSWIECEFG ECCDQCRFKP AGTECRGIRS ECDLPEYCTG
QSVDCPIDHF HRNGKPCLNN NGAEKGEFQH TGGRY
