SLED_CALRH
ID SLED_CALRH Reviewed; 124 AA.
AC D2YW40;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Snaclec rhodocetin subunit delta;
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}.
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DR PDB; 3GPR; X-ray; 3.20 A; D=1-124.
DR PDB; 5THP; X-ray; 3.01 A; B/E/H/K/N/Q=1-124.
DR PDB; 6ND8; X-ray; 2.90 A; B/E/H/K/N/Q=1-124.
DR PDB; 6ND9; X-ray; 2.90 A; B/E/H/K/N/Q=1-124.
DR PDB; 6NDA; X-ray; 3.15 A; B/E/H/K/N/Q=1-124.
DR PDB; 6NDB; X-ray; 3.20 A; B/E/H/K/N/Q=1-124.
DR PDB; 6NDC; X-ray; 3.35 A; B/E/H/K/N/Q=1-124.
DR PDB; 6NDD; X-ray; 3.05 A; B/E/H/K/N/Q=1-124.
DR PDB; 6NDE; X-ray; 3.50 A; B/E/H/K/N/Q=1-124.
DR PDB; 6NDF; X-ray; 3.05 A; B/E/H/K/N/Q=1-124.
DR PDB; 6NDG; X-ray; 3.15 A; B/E/H/K/N/Q=1-124.
DR PDB; 6NDH; X-ray; 2.90 A; B/E/H/K/N/Q=1-124.
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; D2YW40; -.
DR SMR; D2YW40; -.
DR EvolutionaryTrace; D2YW40; -.
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; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 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..124
FT /note="Snaclec rhodocetin subunit delta"
FT /id="PRO_0000422611"
FT DOMAIN 8..121
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 1..12
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19369383"
FT DISULFID 29..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19369383"
FT DISULFID 74
FT /note="Interchain (with C-80 in subunit gamma of
FT heterotetrameric partner)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19369383"
FT DISULFID 95..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19369383"
FT UNSURE 19
FT /note="Assigned by comparison with orthologs"
FT UNSURE 38
FT /note="Assigned by comparison with orthologs"
FT UNSURE 41
FT /note="Assigned by comparison with orthologs"
FT UNSURE 53
FT /note="Assigned by comparison with orthologs"
FT UNSURE 58
FT /note="Assigned by comparison with orthologs"
FT UNSURE 65
FT /note="Assigned by comparison with orthologs"
FT UNSURE 67
FT /note="Assigned by comparison with orthologs"
FT UNSURE 84
FT /note="Assigned by comparison with orthologs"
FT UNSURE 90
FT /note="Assigned by comparison with orthologs"
FT UNSURE 105
FT /note="Assigned by comparison with orthologs"
FT CONFLICT 70..73
FT /note="PWKE -> AWAA (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="P -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="F -> Y (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="V -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:6ND9"
FT STRAND 11..20
FT /evidence="ECO:0007829|PDB:6ND8"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:6ND8"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:5THP"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:6ND8"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:6ND8"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:6ND8"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6ND8"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:6ND8"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:3GPR"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:6ND8"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:6ND8"
SQ SEQUENCE 124 AA; 14855 MW; 4C34EB2DD3D9DF18 CRC64;
CPLHWSSYNG YCYRVFSELK TWEDAESFCY AQHKGSRLAS IHSREEEAFV GKLASQTLKY
TSMWLGLNNP WKECKWEWSD DAKLDYKVWL RRPYCAVMVV KTDRIFWFNR GCEKTVSFVC
KFYS
