DIDA_AGKPL
ID DIDA_AGKPL Reviewed; 111 AA.
AC C9E1S2;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Disintegrin subunit alpha;
DE Flags: Precursor;
OS Agkistrodon piscivorus leucostoma (Western cottonmouth) (Acontias
OS leucostoma).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX NCBI_TaxID=459671;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=18502463; DOI=10.1016/j.toxicon.2008.03.028;
RA Jia Y., Cantu B.A., Sanchez E.E., Perez J.C.;
RT "Complementary DNA sequencing and identification of mRNAs from the venomous
RT gland of Agkistrodon piscivorus leucostoma.";
RL Toxicon 51:1457-1466(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=19799929; DOI=10.1016/j.toxicon.2009.09.016;
RA Jia Y., Perez J.C.;
RT "Molecular cloning and characterization of cDNAs encoding
RT metalloproteinases from snake venom glands.";
RL Toxicon 55:462-469(2010).
CC -!- FUNCTION: Acts by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) on the
CC platelet surface and inhibits both ADP-induced platelet aggregation and
CC platelet aggregate dissociation in human platelet-rich plasma.
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with subunit beta; disulfide-linked.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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; EV854797; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GQ451443; ACV83937.1; -; mRNA.
DR AlphaFoldDB; C9E1S2; -.
DR SMR; C9E1S2; -.
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 2: Evidence at transcript level;
KW Cell adhesion impairing toxin; Disulfide bond; Secreted; Signal; Toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..44
FT /evidence="ECO:0000250"
FT /id="PRO_0000407743"
FT CHAIN 45..109
FT /note="Disintegrin subunit alpha"
FT /id="PRO_0000407744"
FT PROPEP 110..111
FT /evidence="ECO:0000250"
FT /id="PRO_0000407745"
FT DOMAIN 45..111
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 89..91
FT /note="Cell attachment site"
FT DISULFID 53..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 54
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 59
FT /note="Interchain"
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"
FT CONFLICT 65
FT /note="A -> S (in Ref. 1; EV854797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 111 AA; 12103 MW; 47358809BCE06F80 CRC64;
MIQVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKIT PLPKGAVQPK NPCCDAATCK
LTPGAQCAEG LCCDQCKFIK AGKICRRARG DNPDYRCTGQ SGDCPRKHFY A