SLEC_CALRH
ID SLEC_CALRH Reviewed; 135 AA.
AC D2YW39;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Snaclec rhodocetin subunit gamma;
DE Flags: Fragment;
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, SUBUNIT, DISULFIDE BONDS, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF HETEROTETRAMER.
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 [2]
RP 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 [3]
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).
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:11121411, 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:19369383}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PDB; 3GPR; X-ray; 3.20 A; C=2-135.
DR PDB; 5THP; X-ray; 3.01 A; A/D/G/J/M/P=1-135.
DR PDB; 6ND8; X-ray; 2.90 A; A/D/G/J/M/P=1-135.
DR PDB; 6ND9; X-ray; 2.90 A; A/D/G/J/M/P=1-135.
DR PDB; 6NDA; X-ray; 3.15 A; A/D/G/J/M/P=1-135.
DR PDB; 6NDB; X-ray; 3.20 A; A/D/G/J/M/P=1-135.
DR PDB; 6NDC; X-ray; 3.35 A; A/D/G/J/M/P=1-135.
DR PDB; 6NDD; X-ray; 3.05 A; A/D/G/J/M/P=1-135.
DR PDB; 6NDE; X-ray; 3.50 A; A/D/G/J/M/P=1-135.
DR PDB; 6NDF; X-ray; 3.05 A; A/D/G/J/M/P=1-135.
DR PDB; 6NDG; X-ray; 3.15 A; A/D/G/J/M/P=1-135.
DR PDB; 6NDH; X-ray; 2.90 A; A/D/G/J/M/P=1-135.
DR PDBsum; 3GPR; -.
DR PDBsum; 5THP; -.
DR PDBsum; 6ND8; -.
DR PDBsum; 6ND9; -.
DR PDBsum; 6NDA; -.
DR PDBsum; 6NDB; -.
DR PDBsum; 6NDC; -.
DR PDBsum; 6NDD; -.
DR PDBsum; 6NDE; -.
DR PDBsum; 6NDF; -.
DR PDBsum; 6NDG; -.
DR PDBsum; 6NDH; -.
DR AlphaFoldDB; D2YW39; -.
DR SMR; D2YW39; -.
DR EvolutionaryTrace; D2YW39; -.
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 2..135
FT /note="Snaclec rhodocetin subunit gamma"
FT /id="PRO_0000422610"
FT DOMAIN 11..130
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 4..15
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19369383"
FT DISULFID 32..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19369383"
FT DISULFID 81
FT /note="Interchain (with C-74 in subunit delta of
FT heterotetrameric partner)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19369383"
FT DISULFID 104..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19369383"
FT DISULFID 135
FT /note="Interchain (with C-135 in subunit gamma of octameric
FT partner)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19369383"
FT UNSURE 41
FT /note="Assigned by comparison with orthologs"
FT UNSURE 44
FT /note="Assigned by comparison with orthologs"
FT UNSURE 56
FT /note="Assigned by comparison with orthologs"
FT UNSURE 61
FT /note="Assigned by comparison with orthologs"
FT UNSURE 66
FT /note="Assigned by comparison with orthologs"
FT UNSURE 70
FT /note="Assigned by comparison with orthologs"
FT UNSURE 72
FT /note="Assigned by comparison with orthologs"
FT UNSURE 91
FT /note="Assigned by comparison with orthologs"
FT UNSURE 92
FT /note="Assigned by comparison with orthologs"
FT UNSURE 107
FT /note="Assigned by comparison with orthologs"
FT CONFLICT 1
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="P -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6ND8"
FT STRAND 14..23
FT /evidence="ECO:0007829|PDB:6ND8"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:6ND8"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3GPR"
FT HELIX 47..60
FT /evidence="ECO:0007829|PDB:6ND8"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:6ND8"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:6ND8"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:5THP"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:3GPR"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:6ND8"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6ND8"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:6ND8"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6ND8"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:6ND8"
SQ SEQUENCE 135 AA; 15725 MW; E267D54347BE802F CRC64;
DFNCLPGWSA YDQHCYQAFN EPKTWDEAER FCTEQAKRGH LVSIGSDGEA DFVAQLVTNN
IKRPELYVWI GLRDRRKEQQ CSSEWSMSAS IIYVNWNTGE SQMCQGLARW TGFRKWDYSD
CQAKNPFVCK FPSEC
