SLEA_CALRH
ID SLEA_CALRH Reviewed; 133 AA.
AC P81397;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Snaclec rhodocetin subunit alpha;
OS Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Calloselasma.
OX NCBI_TaxID=8717;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=10360956; DOI=10.1021/bi982132z;
RA Wang R., Kini R.M., Chung M.C.M.;
RT "Rhodocetin, a novel platelet aggregation inhibitor from the venom of
RT Calloselasma rhodostoma (Malayan pit viper): synergistic and noncovalent
RT interaction between its subunits.";
RL Biochemistry 38:7584-7593(1999).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, SUBUNIT, DISULFIDE BONDS, VARIANT LYS-70, X-RAY
RP CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF HETEROTETRAMER, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=19369383; DOI=10.1096/fj.08-126763;
RA Eble J.A., Niland S., Bracht T., Mormann M., Peter-Katalinic J.,
RA Pohlentz G., Stetefeld J.;
RT "The alpha2beta1 integrin-specific antagonist rhodocetin is a cruciform,
RT heterotetrameric molecule.";
RL FASEB J. 23:2917-2927(2009).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, AND VARIANT LYS-63.
RX PubMed=11732690; DOI=10.1023/a:1012280720595;
RA Kong C., Chung M.C.;
RT "Purification and characterization of a variant of rhodocetin from
RT Calloselasma rhodostoma (Malayan pit viper) venom.";
RL J. Protein Chem. 20:383-390(2001).
RN [4]
RP PROTEIN SEQUENCE OF 1-21, AND FUNCTION.
RX PubMed=11121411; DOI=10.1074/jbc.m009338200;
RA Eble J.A., Beermann B., Hinz H.J., Schmidt-Hederich A.;
RT "alpha 2beta 1 integrin is not recognized by rhodocytin but is the
RT specific, high affinity target of rhodocetin, an RGD-independent
RT disintegrin and potent inhibitor of cell adhesion to collagen.";
RL J. Biol. Chem. 276:12274-12284(2001).
RN [5]
RP FUNCTION.
RX PubMed=12871211; DOI=10.1042/bj20030373;
RA Eble J.A., Tuckwell D.S.;
RT "The alpha2beta1 integrin inhibitor rhodocetin binds to the A-domain of the
RT integrin alpha2 subunit proximal to the collagen-binding site.";
RL Biochem. J. 376:77-85(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH RHCB, AND DISULFIDE
RP BONDS.
RX PubMed=15576563; DOI=10.1110/ps.04945605;
RA Paaventhan P., Kong C., Joseph J.S., Chung M.C., Kolatkar P.R.;
RT "Structure of rhodocetin reveals noncovalently bound heterodimer
RT interface.";
RL Protein Sci. 14:169-175(2005).
CC -!- FUNCTION: Potent inhibitor of collagen-induced platelet aggregation. It
CC acts by binding to the integrin alpha2A domain and blocks collagen
CC binding to integrin alpha-2/beta-1 (ITGA2/ITGB1). The gamma/delta
CC subunits mainly contribute to this activity.
CC {ECO:0000269|PubMed:10360956, ECO:0000269|PubMed:11121411,
CC ECO:0000269|PubMed:12871211}.
CC -!- SUBUNIT: Heterotetramer of subunit alpha, beta, gamma and delta; only
CC the gamma and the delta subunits are disulfide-linked. Alpha-beta
CC heterodimer and gamma-delta heterodimer associate orthogonally, giving
CC a cruciform conformation (PubMed:19369383). This heterotetramer may
CC covalently dimerizes thanks to the gamma subunit (PubMed:11121411).
CC {ECO:0000269|PubMed:11121411, ECO:0000269|PubMed:15576563,
CC ECO:0000269|PubMed:19369383}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=15955.90; Mass_error=1.44; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10360956};
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR PDB; 1SB2; X-ray; 1.90 A; A=1-133.
DR PDB; 3GPR; X-ray; 3.20 A; A=1-133.
DR PDBsum; 1SB2; -.
DR PDBsum; 3GPR; -.
DR AlphaFoldDB; P81397; -.
DR SMR; P81397; -.
DR EvolutionaryTrace; P81397; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Platelet aggregation inhibiting toxin;
KW Secreted; Toxin.
FT CHAIN 1..133
FT /note="Snaclec rhodocetin subunit alpha"
FT /id="PRO_0000046706"
FT DOMAIN 1..129
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 2..13
FT DISULFID 30..127
FT DISULFID 102..119
FT VARIANT 63
FT /note="I -> K"
FT /evidence="ECO:0000269|PubMed:11732690"
FT VARIANT 70
FT /note="L -> K"
FT /evidence="ECO:0000269|PubMed:19369383"
FT STRAND 10..21
FT /evidence="ECO:0007829|PDB:1SB2"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:1SB2"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1SB2"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:1SB2"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1SB2"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:1SB2"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:3GPR"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1SB2"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1SB2"
FT STRAND 100..111
FT /evidence="ECO:0007829|PDB:1SB2"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1SB2"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3GPR"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:1SB2"
SQ SEQUENCE 133 AA; 15962 MW; 386EAC519DFC674D CRC64;
DCPDGWSSTK SYCYRPFKEK KTWEEAERFC TEQEKEAHLV SMENRLEAVF VDMVMENNFE
NKIYRSWIGL KIENKGQRSN LEWSDGSSIS YENLYEPYME KCFLMDHQSG LPKWHTADCE
EKNVFMCKFQ LPR
