SLYB_CALRH
ID SLYB_CALRH Reviewed; 146 AA.
AC Q9I840;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Snaclec rhodocytin subunit beta;
DE AltName: Full=Aggretin beta chain;
DE AltName: Full=Rhodoaggretin subunit beta;
DE Flags: Precursor;
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 NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 24-41.
RC TISSUE=Venom, and Venom gland;
RX PubMed=10512747; DOI=10.1006/bbrc.1999.1457;
RA Chung C.-H., Au L.-C., Huang T.-F.;
RT "Molecular cloning and sequence analysis of aggretin, a collagen-like
RT platelet aggregation inducer.";
RL Biochem. Biophys. Res. Commun. 263:723-727(1999).
RN [2]
RP PROTEIN SEQUENCE OF 24-53, AND FUNCTION.
RX PubMed=11287424; DOI=10.1074/jbc.m101585200;
RA Navdaev A., Clemetson J.M., Polgar J., Kehrel B.E., Glauner M.,
RA Magnenat E., Wells T.N.C., Clemetson K.J.;
RT "Aggretin, a heterodimeric C-type lectin from Calloselasma rhodostoma
RT (malayan pit viper), stimulates platelets by binding to alpha 2beta 1
RT integrin and glycoprotein Ib, activating Syk and phospholipase Cgamma 2,
RT but does not involve the glycoprotein VI/Fc receptor gamma chain collagen
RT receptor.";
RL J. Biol. Chem. 276:20882-20889(2001).
RN [3]
RP PROTEIN SEQUENCE OF 24-43, FUNCTION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=9588185; DOI=10.1006/bbrc.1998.8516;
RA Shin Y., Morita T.;
RT "Rhodocytin, a functional novel platelet agonist belonging to the
RT heterodimeric C-type lectin family, induces platelet aggregation
RT independently of glycoprotein Ib.";
RL Biochem. Biophys. Res. Commun. 245:741-745(1998).
RN [4]
RP PROTEIN SEQUENCE OF 24-42, FUNCTION, AND SUBUNIT.
RX PubMed=11728470; DOI=10.1016/s0014-5793(01)03071-x;
RA Wang R., Kong C., Kolatkar P., Chung M.C.;
RT "A novel dimer of a C-type lectin-like heterodimer from the venom of
RT Calloselasma rhodostoma (Malayan pit viper).";
RL FEBS Lett. 508:447-453(2001).
RN [5]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=7639679; DOI=10.1042/bj3091021;
RA Huang T.-F., Liu C.-Z., Yang S.-H.;
RT "Aggretin, a novel platelet-aggregation inducer from snake (Calloselasma
RT rhodostoma) venom, activates phospholipase C by acting as a glycoprotein
RT Ia/IIa agonist.";
RL Biochem. J. 309:1021-1027(1995).
RN [6]
RP FUNCTION.
RX PubMed=11453648; DOI=10.1006/bbrc.2001.5228;
RA Chung C.-H., Peng H.-C., Huang T.-F.;
RT "Aggretin, a C-type lectin protein, induces platelet aggregation via
RT integrin alpha(2)beta(1) and GPIb in a phosphatidylinositol 3-kinase
RT independent pathway.";
RL Biochem. Biophys. Res. Commun. 285:689-695(2001).
RN [7]
RP FUNCTION.
RX PubMed=11352922; DOI=10.1074/jbc.m103892200;
RA Bergmeier W., Bouvard D., Eble J.A., Mokhtari-Nejad R., Schulte V.,
RA Zirngibl H., Brakebusch C., Fassler R., Nieswandt B.;
RT "Rhodocytin (aggretin) activates platelets lacking alpha(2)beta(1)
RT integrin, glycoprotein VI, and the ligand-binding domain of glycoprotein
RT Ibalpha.";
RL J. Biol. Chem. 276:25121-25126(2001).
RN [8]
RP FUNCTION.
RX PubMed=14630793; DOI=10.1182/blood-2003-07-2483;
RA Chung C.-H., Wu W.-B., Huang T.-F.;
RT "Aggretin, a snake venom-derived endothelial integrin alpha 2 beta 1
RT agonist, induces angiogenesis via expression of vascular endothelial growth
RT factor.";
RL Blood 103:2105-2113(2004).
RN [9]
RP FUNCTION.
RX PubMed=16174766; DOI=10.1182/blood-2005-05-1994;
RA Suzuki-Inoue K., Fuller G.L.J., Garcia A., Eble J.A., Poehlmann S.,
RA Inoue O., Gartner T.K., Hughan S.C., Pearce A.C., Laing G.D.,
RA Theakston R.D.G., Schweighoffer E., Zitzmann N., Morita T.,
RA Tybulewicz V.L.J., Ozaki Y., Watson S.P.;
RT "A novel Syk-dependent mechanism of platelet activation by the C-type
RT lectin receptor CLEC-2.";
RL Blood 107:542-549(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 24-146, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=18597489; DOI=10.1021/bi800528t;
RA Hooley E., Papagrigoriou E., Navdaev A., Pandey A.V., Clemetson J.M.,
RA Clemetson K.J., Emsley J.;
RT "The crystal structure of the platelet activator aggretin reveals a novel
RT (alphabeta)2 dimeric structure.";
RL Biochemistry 47:7831-7837(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 24-146, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=18583525; DOI=10.1110/ps.035568.108;
RA Watson A.A., Eble J.A., O'Callaghan C.A.;
RT "Crystal structure of rhodocytin, a ligand for the platelet-activating
RT receptor CLEC-2.";
RL Protein Sci. 17:1611-1616(2008).
CC -!- FUNCTION: Elicits platelet aggregation by the binding to the C-type
CC lectin domain family 1 member B (CLEC1B/CLEC2). Binding leads to
CC tyrosine phosphorylation in the cytoplasmic tail of CLEC1B, which
CC promotes the binding of spleen tyrosine kinase (Syk), subsequent
CC activation of PLCgamma2, and platelet activation and aggregation.
CC Binding to GPIbalpha (GP1BA) and alpha2/beta-1 (ITGA2/ITGB1) may also
CC induce aggregation, but this is controversial.
CC {ECO:0000269|PubMed:11287424, ECO:0000269|PubMed:11352922,
CC ECO:0000269|PubMed:11453648, ECO:0000269|PubMed:11728470,
CC ECO:0000269|PubMed:14630793, ECO:0000269|PubMed:16174766,
CC ECO:0000269|PubMed:7639679, ECO:0000269|PubMed:9588185}.
CC -!- SUBUNIT: Dimer (non-covalently linked) of heterodimers of subunits
CC alpha and beta (disulfide-linked). {ECO:0000269|PubMed:11728470,
CC ECO:0000269|PubMed:18583525, ECO:0000269|PubMed:18597489,
CC ECO:0000269|PubMed:9588185}.
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 EMBL; AF244901; AAF79953.1; -; mRNA.
DR PIR; JC7105; JC7105.
DR PDB; 2VRP; X-ray; 2.41 A; B=24-146.
DR PDB; 3BX4; X-ray; 1.70 A; B/D=1-146.
DR PDB; 3WWK; X-ray; 2.98 A; B/E/H/K=1-146.
DR PDBsum; 2VRP; -.
DR PDBsum; 3BX4; -.
DR PDBsum; 3WWK; -.
DR AlphaFoldDB; Q9I840; -.
DR SMR; Q9I840; -.
DR DIP; DIP-61335N; -.
DR IntAct; Q9I840; 1.
DR EvolutionaryTrace; Q9I840; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Metal-binding;
KW Platelet aggregation activating toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:10512747,
FT ECO:0000269|PubMed:11287424, ECO:0000269|PubMed:11728470,
FT ECO:0000269|PubMed:9588185"
FT CHAIN 24..146
FT /note="Snaclec rhodocytin subunit beta"
FT /id="PRO_0000355239"
FT DOMAIN 32..143
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 25..36
FT DISULFID 53..142
FT DISULFID 98
FT /note="Interchain (with C-83 in alpha chain)"
FT DISULFID 119..134
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3BX4"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:3BX4"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:3BX4"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3BX4"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:3BX4"
FT TURN 79..84
FT /evidence="ECO:0007829|PDB:3BX4"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:3BX4"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:3BX4"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3BX4"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:3BX4"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:3BX4"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:3BX4"
SQ SEQUENCE 146 AA; 16770 MW; 930839140CFD8908 CRC64;
MGRFIFVSFG LLVVFLSLSG TGADCPSGWS SYEGHCYKPF NEPKNWADAE RFCKLQPKHS
HLVSFQSAEE ADFVVKLTRP RLKANLVWMG LSNIWHGCNW QWSDGARLNY KDWQEQSECL
AFRGVHTEWL NMDCSSTCSF VCKFKA
