VM2BI_BITGA
ID VM2BI_BITGA Reviewed; 325 AA.
AC Q6T271;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase-4;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin bitisgabonin;
DE AltName: Full=Bitisgabonin-1;
DE AltName: Full=Bitisgabonin-2;
DE Flags: Precursor; Fragment;
OS Bitis gabonica (Gaboon adder) (Gaboon viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX NCBI_TaxID=8694;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Venom gland;
RX PubMed=15276202; DOI=10.1016/j.gene.2004.03.024;
RA Francischetti I.M.B., My-Pham V., Harrison J., Garfield M.K.,
RA Ribeiro J.M.C.;
RT "Bitis gabonica (Gaboon viper) snake venom gland: toward a catalog for the
RT full-length transcripts (cDNA) and proteins.";
RL Gene 337:55-69(2004).
RN [2]
RP PROTEIN SEQUENCE OF 258-325, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND PYROGLUTAMATE
RP FORMATION AT GLN-258.
RC TISSUE=Venom;
RX PubMed=17203976; DOI=10.1021/pr060494k;
RA Calvete J.J., Marcinkiewicz C., Sanz L.;
RT "Snake venomics of Bitis gabonica gabonica. Protein family composition,
RT subunit organization of venom toxins, and characterization of dimeric
RT disintegrins bitisgabonin-1 and bitisgabonin-2.";
RL J. Proteome Res. 6:326-336(2007).
CC -!- FUNCTION: [Snake venom metalloproteinase-4]: Impairs hemostasis in the
CC envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin bitisgabonin]: In dimer with gabonin-1
CC (bitisgabonin-1), is a potent inhibitor of the adhesion of the RGD-
CC dependent integrin alpha-5/beta-1 (ITGA5/ITGB1) to immobilized
CC fibronectin. {ECO:0000269|PubMed:17203976}.
CC -!- FUNCTION: [Disintegrin bitisgabonin]: In dimer with gabonin-2
CC (bitisgabonin-2), preferentially inhibits the adhesion of the alpha-
CC 4/beta-1 (ITGA4/ITGB1) and alpha-9/beta-1 (ITGA9/ITGB1) integrins to
CC VCAM-1 and acts also as a strong antagonist of alpha-5/beta-1
CC (ITGA5/ITGB1). {ECO:0000269|PubMed:17203976}.
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: Heterodimer of bitisgabonin and gabonin-1 (bitisgabonin-1) or
CC gabonin-2 (bitisgabonin-2); disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17203976}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:17203976}.
CC -!- MISCELLANEOUS: The disintegrin belongs to the dimeric disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIe sub-subfamily. {ECO:0000305}.
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DR EMBL; AY442287; AAR19273.1; -; mRNA.
DR AlphaFoldDB; Q6T271; -.
DR SMR; Q6T271; -.
DR MEROPS; M12.164; -.
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; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF00200; Disintegrin; 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 1: Evidence at protein level;
KW Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Pyrrolidone carboxylic acid; Secreted; Toxin; Zinc; Zymogen.
FT PROPEP <1..39
FT /evidence="ECO:0000250"
FT /id="PRO_0000336067"
FT CHAIN 40..242
FT /note="Snake venom metalloproteinase-4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000336068"
FT PROPEP 243..257
FT /evidence="ECO:0000250"
FT /id="PRO_0000336069"
FT CHAIN 258..325
FT /note="Disintegrin bitisgabonin"
FT /id="PRO_0000336070"
FT DOMAIN 46..242
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 250..322
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 300..302
FT /note="Cell attachment site"
FT ACT_SITE 183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 40
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT MOD_RES 258
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:17203976"
FT DISULFID 197..221
FT /evidence="ECO:0000250"
FT DISULFID 199..204
FT /evidence="ECO:0000250"
FT DISULFID 264..287
FT /evidence="ECO:0000250"
FT DISULFID 265
FT /note="Interchain (with C-54 in gabonin-1/2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 270
FT /note="Interchain (with C-59 in gabonin-1/2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 278..284
FT /evidence="ECO:0000250"
FT DISULFID 283..308
FT /evidence="ECO:0000250"
FT DISULFID 296..315
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 325 AA; 36670 MW; B42472E292F4B9B0 CRC64;
KYENVEKGDE APKKCGVTHT NLESDEPIEK ASQLFGTSEQ QRFDPRHIEL VIVADHGMVM
KHNGDLTAVR TWLHQIGNNL NVMFADLNIR ITMAGLEMWS EKDLIDIQSA ASETLRLFGE
WRERYLLNRR MHDNAQLLTT VNLDGDTVGL AYVGGMCDPK NSVGIVQDHS RIAREVAATM
AHELGHNLGM AHDGNQCNCG ANGCVMSEEI IERTSYQFSD CSKEEYRTFL DNHNPQRILN
EPLRTDTVST PVYGNVLQNS PHPCCDPVTC KPKAWEHCIS GPCCRDCKFL RPGTVCRVAR
GDWNDDFCTG RSSECESNPW NFWNH
