ID   SLA1_TRIAB              Reviewed;         131 AA.
AC   P81111;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   26-FEB-2020, entry version 77.
DE   RecName: Full=Snaclec alboaggregin-A subunit alpha;
DE   AltName: Full=50-kDa alboaggregin;
DE   AltName: Full=Alboaggregin-A subunit 1;
DE            Short=AL-A subunit 1;
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   PROTEIN SEQUENCE OF 1-18, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   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   [3]
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   [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}.
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   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..131
FT                   /note="Snaclec alboaggregin-A subunit alpha"
FT                   /id="PRO_0000046708"
FT   DOMAIN          1..131
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        2..13
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        30..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        79
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        102..119
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   131 AA;  15428 MW;  B3569F5BF91F6624 CRC64;
     DCPSDWSSYD QYCYRVFKRI QTWEDAERFC SEQANDGHLV SIESAGEADF VTQLVSENIR
     SEKHYVWIGL RVQGKGQQCS SEWSDGSSVH YDNLQENKTR KCYGLEKRAE FRTWSNVYCG
     HEYPFVCKFX R