ID   SLA2_TRIAB              Reviewed;         134 AA.
AC   P81112;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Snaclec alboaggregin-A subunit alpha';
DE   AltName: Full=Alboaggregin-A subunit 2;
DE            Short=AL-A subunit 2;
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   AlphaFoldDB; P81112; -.
DR   SMR; P81112; -.
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; Toxin.
FT   CHAIN           1..134
FT                   /note="Snaclec alboaggregin-A subunit alpha'"
FT                   /id="PRO_0000046709"
FT   DOMAIN          1..134
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..129
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        81
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        104..121
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   134 AA;  15557 MW;  5F9D71FC86DE2435 CRC64;
     DFHCLPGWSA YDQYCYRVFN EPKNWEDAER FCAKQADSGH LVSIETMGEA DFVAQLISEN
     IQSEKHYVWI GLKVQNKEQQ CSSEWSDGSS VTYENLIKLY MRKCGALEQE SGFRKWINLG
     CIQLNPFVCK FPPQ