ID   DID2_BITGA              Reviewed;         128 AA.
AC   Q6T6T2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Disintegrin gabonin-2;
DE   AltName: Full=Bitisgabonin-2;
DE   Flags: Precursor;
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 48-115, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
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: The heterodimer bitisgabonin-2 preferentially inhibits the
CC       adhesion of the alpha-4/beta-1 (ITGA4/ITGB1) and alpha-9/beta-1
CC       (ITGA9/ITGB1) integrins to VCAM-1 and acts also as a strong antagonist
CC       of alpha-5/beta-1 (ITGA5/ITGB1). {ECO:0000269|PubMed:17203976}.
CC   -!- SUBUNIT: Heterodimer with bitisgabonin (bitisgabonin-2 is the name of
CC       the heterodimer); disulfide-linked. {ECO:0000269|PubMed:17203976}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17203976}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:17203976}.
CC   -!- SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY430405; AAR24529.1; -; mRNA.
DR   AlphaFoldDB; Q6T6T2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   Pfam; PF00200; Disintegrin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..47
FT                   /evidence="ECO:0000269|PubMed:17203976"
FT                   /id="PRO_0000321882"
FT   CHAIN           48..128
FT                   /note="Disintegrin gabonin-2"
FT                   /id="PRO_0000321883"
FT   DOMAIN          47..112
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           89..91
FT                   /note="Cell attachment site; atypical (MLD)"
FT   DISULFID        53..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        54
FT                   /note="Interchain (with C-265 in bitisgabonin)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        59
FT                   /note="Interchain (with C-270 in bitisgabonin)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        67..73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        72..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        85..104
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ   SEQUENCE   128 AA;  13786 MW;  AB4F50830E469699 CRC64;
     MIQVLLVIIC LAVFPYQGSS IILESGNVND YEIVYPKKVT VLPTGAMNSA HPCCDPVTCK
     PKRGEHCISG PCCRNCKFLN AGTICKKTML DGLNDYCTGV TPDCPRNPNK GESDELEWSA
     AATGSVLM