DIDAA_ERIMA
ID DIDAA_ERIMA Reviewed; 69 AA.
AC P81742;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Disintegrin EMF10A;
DE Short=EMF-10A;
DE AltName: Full=Eristocophin I;
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, AND FUNCTION.
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 1-62, AND AMINO-ACID COMPOSITION.
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 EMF10B; disulfide-linked.
CC {ECO:0000269|PubMed:10642516}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Eristocophin I appears to represent degradation product of
CC EMF10A. {ECO:0000305|PubMed:1494485}.
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DR AlphaFoldDB; P81742; -.
DR SMR; P81742; -.
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 Hemostasis impairing toxin; Platelet aggregation inhibiting toxin;
KW Secreted; Toxin.
FT CHAIN 1..69
FT /note="Disintegrin EMF10A"
FT /id="PRO_0000101803"
FT DOMAIN 1..66
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 43..45
FT /note="Cell attachment site"
FT DISULFID 7..30
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:10642516"
FT DISULFID 8
FT /note="Interchain (with C-11 in EMF10B)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:10642516"
FT DISULFID 13
FT /note="Interchain (with C-16 in EMF10B)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:10642516"
FT DISULFID 21..27
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:10642516"
FT DISULFID 26..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:10642516"
FT DISULFID 39..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:10642516"
SQ SEQUENCE 69 AA; 7554 MW; E200B3E89DC18FAD CRC64;
MNSANPCCDP ITCKPKKGEH CVSGPCCRNC KFLNPGTICK KGRGDNLNDY CTGVSSDCPR
NPWKSEEED
