DIDA_AGKCO
ID DIDA_AGKCO Reviewed; 111 AA.
AC Q805F7;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Disintegrin acostatin-alpha;
DE Contains:
DE RecName: Full=Disintegrin acostatin-alpha, processed form;
DE Flags: Precursor;
OS Agkistrodon contortrix contortrix (Southern copperhead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX NCBI_TaxID=8713 {ECO:0000312|EMBL:BAC55944.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-109, PYROGLUTAMATE
RP FORMATION AT GLN-48 IN PROCESSED FORM, FUNCTION, AND SUBUNIT.
RC TISSUE=Venom {ECO:0000269|PubMed:12450389}, and Venom gland;
RX PubMed=12450389; DOI=10.1021/bi025876s;
RA Okuda D., Koike H., Morita T.;
RT "A new gene structure of the disintegrin family: a subunit of dimeric
RT disintegrin has a short coding region.";
RL Biochemistry 41:14248-14254(2002).
RN [2]
RP CRYSTALLIZATION.
RC TISSUE=Venom;
RX PubMed=11752794; DOI=10.1107/s090744490101736x;
RA Fujii Y., Okuda D., Fujimoto Z., Morita T., Mizuno H.;
RT "Crystallization and preliminary crystallographic studies of dimeric
RT disintegrins from the venom of two Agkistrodon snakes.";
RL Acta Crystallogr. D 58:145-147(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 48-109, DISULFIDE BONDS, AND
RP PYROGLUTAMATE FORMATION AT GLN-48.
RX PubMed=18391413; DOI=10.1107/s0907444908002370;
RA Moiseeva N., Bau R., Swenson S.D., Markland F.S. Jr., Choe J.Y., Liu Z.J.,
RA Allaire M.;
RT "Structure of acostatin, a dimeric disintegrin from Southern copperhead
RT (Agkistrodon contortrix contortrix), at 1.7 A resolution.";
RL Acta Crystallogr. D 64:466-470(2008).
CC -!- FUNCTION: Inhibits fibrinogen interaction with platelets. Acts by
CC binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) on the platelet surface and
CC inhibits ADP-induced platelet aggregation in human platelet-rich
CC plasma. {ECO:0000269|PubMed:12450389}.
CC -!- SUBUNIT: Heterodimer with subunit beta; disulfide-linked.
CC {ECO:0000269|PubMed:12450389, ECO:0000269|PubMed:18391413}.
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}.
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DR EMBL; AB078903; BAC55944.1; -; mRNA.
DR PDB; 3C05; X-ray; 1.70 A; A/C=49-109.
DR PDBsum; 3C05; -.
DR AlphaFoldDB; Q805F7; -.
DR SMR; Q805F7; -.
DR IntAct; Q805F7; 1.
DR EvolutionaryTrace; Q805F7; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; TAS:UniProtKB.
DR GO; GO:0030195; P:negative regulation of blood coagulation; IDA:UniProtKB.
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 3D-structure; Cell adhesion impairing toxin; Direct protein sequencing;
KW Disulfide bond; Hemostasis impairing toxin;
KW Platelet aggregation inhibiting toxin; Pyrrolidone carboxylic acid;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..46
FT /evidence="ECO:0000269|PubMed:12450389"
FT /id="PRO_0000007236"
FT CHAIN 47..109
FT /note="Disintegrin acostatin-alpha"
FT /id="PRO_0000007237"
FT CHAIN 48..109
FT /note="Disintegrin acostatin-alpha, processed form"
FT /id="PRO_0000413008"
FT PROPEP 110..111
FT /id="PRO_0000007238"
FT DOMAIN 47..111
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 89..91
FT /note="Cell attachment site"
FT MOD_RES 48
FT /note="Pyrrolidone carboxylic acid; in Disintegrin
FT acostatin-alpha, processed form"
FT /evidence="ECO:0000269|PubMed:12450389,
FT ECO:0000269|PubMed:18391413"
FT DISULFID 53..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:18391413"
FT DISULFID 54
FT /note="Interchain (with C-431 in subunit beta)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:18391413"
FT DISULFID 59
FT /note="Interchain (with C-426 in subunit beta)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:18391413"
FT DISULFID 67..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:18391413"
FT DISULFID 72..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:18391413"
FT DISULFID 85..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:18391413"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:3C05"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:3C05"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3C05"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:3C05"
SQ SEQUENCE 111 AA; 12093 MW; 5D120A539592659C CRC64;
MIQVLLVTLC LAVFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAIQPK NPCCDAATCK
LTPGSQCAEG LCCDQCKFIK AGKICRRARG DNPDYRCTGQ SGDCPRKHFY A
