SLBA_TRIAB
ID SLBA_TRIAB Reviewed; 156 AA.
AC P81115; A7LAC8; Q9PS19;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Snaclec alboaggregin-B subunit alpha;
DE Short=AL-B subunit alpha;
DE AltName: Full=25-kDa alboaggregin;
DE Flags: Precursor;
OS Trimeresurus albolabris (White-lipped pit viper) (Cryptelytrops
OS albolabris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=8765;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17538847; DOI=10.1080/09537100601078232;
RA Arpijuntarangkoon J., Rojnuckarin P., Muanpasitporn C., Kaeothip S.,
RA Sangvanich P., Intragumtornchai T.;
RT "Molecular cloning and sequence analysis of alboaggregin B.";
RL Platelets 18:266-272(2007).
RN [2]
RP PROTEIN SEQUENCE OF 24-156.
RX PubMed=8645249; DOI=10.1006/bbrc.1996.0302;
RA Usami Y., Suzuki M., Yoshida E., Sakurai Y., Hirano K., Kawasaki T.,
RA Fujimura Y., Titani K.;
RT "Primary structure of alboaggregin-B purified from the venom of
RT Trimeresurus albolabris.";
RL Biochem. Biophys. Res. Commun. 219:727-733(1996).
RN [3]
RP PROTEIN SEQUENCE OF 24-155.
RC TISSUE=Venom;
RX PubMed=9531050;
RA Kowalska M.A., Tan L., Holt J.C., Peng M., Karczewski J., Calvete J.J.,
RA Niewiarowski S.;
RT "Alboaggregins A and B. Structure and interaction with human platelets.";
RL Thromb. Haemost. 79:609-613(1998).
RN [4]
RP PROTEIN SEQUENCE OF 24-63.
RC TISSUE=Venom;
RX PubMed=8466514; DOI=10.1006/bbrc.1993.1371;
RA Yoshida E., Fujimura Y., Miura S., Sugimoto M., Fukui H., Narita N.,
RA Usami Y., Suzuki M., Titani K.;
RT "Alboaggregin-B and botrocetin, two snake venom proteins with highly
RT homologous amino acid sequences but totally distinct functions on von
RT Willebrand factor binding to platelets.";
RL Biochem. Biophys. Res. Commun. 191:1386-1392(1993).
RN [5]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=1747371; DOI=10.1021/bi00113a007;
RA Peng M., Lu W., Kirby E.P.;
RT "Alboaggregin-B: a new platelet agonist that binds to platelet membrane
RT glycoprotein Ib.";
RL Biochemistry 30:11529-11536(1991).
CC -!- FUNCTION: Weakly agglutinates platelets at high doses by binding to
CC GPIbalpha (GP1BA). {ECO:0000269|PubMed:1747371}.
CC -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Monoclonal antibodies to glycoprotein IIb/IIIa, to
CC bovine vWF, and to bovine serum albumin did not show any effect on the
CC binding of AL-B to platelets. {ECO:0000305|PubMed:1747371}.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR EMBL; EF690367; ABS12076.1; -; mRNA.
DR PIR; B56829; B56829.
DR AlphaFoldDB; P81115; -.
DR SMR; P81115; -.
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 Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Platelet aggregation activating toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..156
FT /note="Snaclec alboaggregin-B subunit alpha"
FT /id="PRO_0000046712"
FT DOMAIN 24..151
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 25..36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 53..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 102
FT /note="Interchain (with C-75 in subunit beta)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 125..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 40..42
FT /note="VKE -> IKQ (in Ref. 2; AA sequence and 4; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="K -> R (in Ref. 2; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 54..60
FT /note="SEQANDG -> MDQVKGA (in Ref. 2; AA sequence and 4; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 76..77
FT /note="EL -> QQ (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="N -> H (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="Q -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="S -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="V -> I (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 121..122
FT /note="NP -> LS (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 131..132
FT /note="ES -> GT (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 136..141
FT /note="TWSNVY -> KWFNVA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="I -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..155
FT /note="GS -> RP (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 156 AA; 17893 MW; 613DEC279CEE44C3 CRC64;
MGRFIFVSFG LLVVFLSLSG TGADCPSDWS SFKQYCYQIV KELKTWEDAE KFCSEQANDG
HLVSIESYRE AVFVAELLSE NVKTTKYNVW IGLSVQNKGQ QCSSEWSDGS SVSYENLVKP
NPKKCFVLKK ESEFRTWSNV YCEQKHIFMC KFLGSR
