GENTAUR Molecular Products.

 SLA_PROJR               Reviewed;         156 AA.
 D1MGU0;
 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
 19-JAN-2010, sequence version 1.
 23-MAY-2018, entry version 30.
 RecName: Full=Snaclec jerdonibitin subunit alpha;
 AltName: Full=TJ-GPIb-bp subunit alpha;
 Flags: Precursor;
 Protobothrops jerdonii (Jerdon's pitviper) (Trimeresurus jerdonii).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
 Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae;
 Protobothrops.
 NCBI_TaxID=242841;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-44, FUNCTION, AND
 SUBUNIT.
 TISSUE=Venom, and Venom gland;
 PubMed=21256857; DOI=10.1016/j.toxicon.2011.01.010;
 Chen Z., Wu J., Zhang Y., Yang X., Yu G., Zhu S., Lee W., Lu Q.,
 Zhang Y.;
 "A novel platelet glycoprotein Ib-binding protein with human platelet
 aggregation-inhibiting activity from Trimeresurus jerdonii venom.";
 Toxicon 57:672-679(2011).
 -!- FUNCTION: Snaclec that dose-dependently inhibits platelet
     aggregation induced by ristocetin or low-dose thrombin, but not by
     high-dose thrombin. Binds to GPIbalpha (GP1BA). In vivo, also
     dose-dependently induces thrombocytopenia of mice and platelet
     counts remains at very low level even after 18 hours intravenous
     injection. {ECO:0000269|PubMed:21256857}.
 -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
     {ECO:0000269|PubMed:21256857}.
 -!- SUBCELLULAR LOCATION: Secreted.
 -!- TISSUE SPECIFICITY: Expressed by the venom gland.
 -!- MISCELLANEOUS: Does not induce platelet aggregation in either
     platelet rich plasma or washed platelets under high-dose
     conditions. Does not inhibit platelet aggregation induced by high-
     dose thrombin. Does not react with polyclonal anti-GPVI and anti-
     GPIIb antibodies (PubMed:21256857). {ECO:0000305|PubMed:21256857}.
 -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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 EMBL; GU146049; ACZ34293.1; -; mRNA.
 ProteinModelPortal; D1MGU0; -.
 SMR; D1MGU0; -.
 PRIDE; D1MGU0; -.
 GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
 GO; GO:0044218; C:other organism cell membrane; IDA:UniProtKB.
 GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
 GO; GO:0044477; P:envenomation resulting in negative regulation of platelet aggregation in other organism; IDA:UniProtKB.
 Gene3D; 3.10.100.10; -; 1.
 InterPro; IPR001304; C-type_lectin-like.
 InterPro; IPR016186; C-type_lectin-like/link_sf.
 InterPro; IPR018378; C-type_lectin_CS.
 InterPro; IPR016187; CTDL_fold.
 Pfam; PF00059; Lectin_C; 1.
 SMART; SM00034; CLECT; 1.
 SUPFAM; SSF56436; SSF56436; 1.
 PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
 PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
 1: Evidence at protein level;
 Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
 Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
 SIGNAL        1     23       {ECO:0000269|PubMed:21256857}.
 CHAIN        24    156       Snaclec jerdonibitin subunit alpha.
                              /FTId=PRO_0000422430.
 DOMAIN       32    151       C-type lectin. {ECO:0000255|PROSITE-
                              ProRule:PRU00040}.
 DISULFID     25     36       {ECO:0000255|PROSITE-ProRule:PRU00040}.
 DISULFID     53    150       {ECO:0000255|PROSITE-ProRule:PRU00040}.
 DISULFID    102    102       Interchain (with C-98 in subunit beta).
                              {ECO:0000255|PROSITE-ProRule:PRU00040}.
 DISULFID    125    142       {ECO:0000255|PROSITE-ProRule:PRU00040}.
 SEQUENCE   156 AA;  18146 MW;  80129F2F8EEBC86E CRC64;
 MGRFIFVSFG LLVVFLSLSG TGADCPFDWS SFRQYCYRVF KQLKTWEDAE RFCSEQVKGA
 RLVSIESYRE AVFVAQLLSE NIKATKSHVW IGLSVENKGQ QCSSKWSDGS SVSYENLVKP
 FSKKCFVLKK ESEFHKWFNV YCGQQHLFMC KFLRPR

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