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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}.
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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
 
 
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