ID   SLA3_TRIAB              Reviewed;         125 AA.
AC   P81113;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   07-OCT-2020, entry version 76.
DE   RecName: Full=Snaclec alboaggregin-A subunit beta;
DE   AltName: Full=Alboaggregin-A subunit 3;
DE            Short=AL-A subunit 3;
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   PROTEIN SEQUENCE, AND FUNCTION.
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   [2]
RP   PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=11159519; DOI=10.1182/blood.v97.4.929;
RA   Dormann D., Clemetson J.M., Navdaev A., Kehrel B.E., Clemetson K.J.;
RT   "Alboaggregin A activates platelets by a mechanism involving glycoprotein
RT   VI as well as glycoprotein Ib.";
RL   Blood 97:929-936(2001).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom;
RX   PubMed=8823201; DOI=10.1021/bi960704e;
RA   Andrews R.K., Kroll M.H., Ward C.M., Rose J.W., Scarborough R.M.,
RA   Smith A.I., Lopez J.A., Berndt M.C.;
RT   "Binding of a novel 50-kilodalton alboaggregin from Trimeresurus albolabris
RT   and related viper venom proteins to the platelet membrane glycoprotein Ib-
RT   IX-V complex. Effect on platelet aggregation and glycoprotein Ib-mediated
RT   platelet activation.";
RL   Biochemistry 35:12629-12639(1996).
RN   [4]
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=11389045; DOI=10.1182/blood.v97.12.3989;
RA   Asazuma N., Marshall S.J., Berlanga O., Snell D., Poole A.W., Berndt M.C.,
RA   Andrews R.K., Watson S.P.;
RT   "The snake venom toxin alboaggregin-A activates glycoprotein VI.";
RL   Blood 97:3989-3991(2001).
CC   -!- FUNCTION: Potent platelet activator that aggregates platelets via both
CC       GPIbalpha (GP1BA) and GPVI (GP6). Induces a tyrosine phosphorylation
CC       profile in platelets that resembles this produced by collagen,
CC       involving the time dependent tyrosine phosphorylation of Fc receptor
CC       gamma chain (FCGR1A), phospholipase Cgamma2 (PLCG2), and LAT.
CC       {ECO:0000269|PubMed:11159519, ECO:0000269|PubMed:11389045,
CC       ECO:0000269|PubMed:8823201, ECO:0000269|PubMed:9531050}.
CC   -!- SUBUNIT: Heterotetramer of the subunits alpha, alpha', beta and beta';
CC       disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8823201}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:8823201}.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   PRIDE; P81113; -.
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   Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW   Platelet aggregation activating toxin; Secreted; Toxin.
FT   CHAIN           1..125
FT                   /note="Snaclec alboaggregin-A subunit beta"
FT                   /id="PRO_0000046710"
FT   DOMAIN          1..125
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        4..15
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        32..121
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        77
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        98..113
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   125 AA;  14799 MW;  CAFA24C098DF3293 CRC64;
     GFDCPFGWSS YEGYCYKVYN KKMNWEDAES FCREQHKRSH LVSFHSSGEV DFVVSKTFPI
     LRYDFVWMGL SDIWKECTKE WSDGARLDYK AWSGKSYCLV SKTTNNEWLS MDCSRTRYPV
     CKFXG