ID   VM2AB_ERIMA             Reviewed;          68 AA.
AC   P81743;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Disintegrin EMF10B;
DE            Short=EMF-10B;
DE   AltName: Full=Eristocophin II;
DE   AltName: Full=Platelet aggregation activation inhibitor;
OS   Eristicophis macmahoni (Leaf-nosed viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Eristicophis.
OX   NCBI_TaxID=110227;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND VARIANTS LYS-35 AND 65-PHE--LYS-68 DEL.
RC   TISSUE=Venom;
RX   PubMed=10529205; DOI=10.1021/bi9906930;
RA   Marcinkiewicz C., Calvete J.J., Vijay-Kumar S., Marcinkiewicz M.M.,
RA   Raida M., Schick P., Lobb R.R., Niewiarowski S.;
RT   "Structural and functional characterization of EMF10, a heterodimeric
RT   disintegrin from Eristocophis macmahoni venom that selectively inhibits
RT   alpha 5 beta 1 integrin.";
RL   Biochemistry 38:13302-13309(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 5-65, AMINO-ACID COMPOSITION, AND VARIANT LYS-35.
RC   TISSUE=Venom;
RX   PubMed=1494485; DOI=10.1016/0196-9781(92)90002-k;
RA   Siddiqi A.R., Persson B., Zaidi Z.H., Jornvall H.;
RT   "Characterization of two platelet aggregation inhibitor-like polypeptides
RT   from viper venom.";
RL   Peptides 13:1033-1037(1992).
RN   [3]
RP   DISULFIDE BONDS.
RX   PubMed=10642516; DOI=10.1042/bj3450573;
RA   Calvete J.J., Jurgens M., Marcinkiewicz C., Romero A., Schrader M.,
RA   Niewiarowski S.;
RT   "Disulphide-bond pattern and molecular modelling of the dimeric disintegrin
RT   EMF-10, a potent and selective integrin alpha5beta1 antagonist from
RT   Eristocophis macmahoni venom.";
RL   Biochem. J. 345:573-581(2000).
CC   -!- FUNCTION: Extremely potent and selective inhibitor of integrin alpha-
CC       5/beta-1 (ITGA5/ITGB1). Partially inhibits adhesion of cells expressing
CC       alpha-IIb/beta-3 (ITGA2B/ITGB3), alpha-V/beta-3 (ITGAV/ITGB3), and
CC       alpha-4/beta-1 (ITGA4/ITGB1) to appropriate ligands only at
CC       concentration higher than 500 nM. Weakly inhibits ADP-induced platelet
CC       aggregation. {ECO:0000269|PubMed:10529205}.
CC   -!- SUBUNIT: Heterodimer with EMF10A; disulfide-linked.
CC       {ECO:0000269|PubMed:10642516}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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}.
CC   -!- CAUTION: Eristocophin II appears to represent degradation product of
CC       EMF10B. {ECO:0000305|PubMed:1494485}.
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DR   AlphaFoldDB; P81743; -.
DR   SMR; P81743; -.
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; 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; PS50214; DISINTEGRIN_2; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Hemostasis impairing toxin; Platelet aggregation inhibiting toxin;
KW   Secreted; Toxin.
FT   CHAIN           1..68
FT                   /note="Disintegrin EMF10B"
FT                   /id="PRO_0000101804"
FT   DOMAIN          1..68
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           46..48
FT                   /note="Cell attachment site; atypical (MGD)"
FT   DISULFID        10..33
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:10642516"
FT   DISULFID        11
FT                   /note="Interchain (with C-8 in EMF10A)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:10642516"
FT   DISULFID        16
FT                   /note="Interchain (with C-13 in EMF10A)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:10642516"
FT   DISULFID        24..30
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:10642516"
FT   DISULFID        29..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:10642516"
FT   DISULFID        42..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:10642516"
FT   VARIANT         35
FT                   /note="F -> K"
FT                   /evidence="ECO:0000269|PubMed:10529205,
FT                   ECO:0000269|PubMed:1494485"
FT   VARIANT         65..68
FT                   /note="Missing"
FT   CONFLICT        5..8
FT                   /note="NSGN -> ESAG (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   68 AA;  7427 MW;  E63FEE61BCE74220 CRC64;
     ELLQNSGNPC CDPVTCKPRR GEHCVSGPCC DNCKFLNAGT VCWPAMGDWN DDYCTGISSD
     CPRNPVFK