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Snaclec jerdonibitin subunit beta (TJ-GPIb-bp subunit beta)

 SLB_PROJR               Reviewed;         146 AA.
D1MGU1;
29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
19-JAN-2010, sequence version 1.
20-DEC-2017, entry version 28.
RecName: Full=Snaclec jerdonibitin subunit beta;
AltName: Full=TJ-GPIb-bp subunit beta;
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 24-45, 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; GU146050; ACZ34294.1; -; mRNA.
ProteinModelPortal; D1MGU1; -.
SMR; D1MGU1; -.
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 24 146 Snaclec jerdonibitin subunit beta.
/FTId=PRO_0000422431.
DOMAIN 32 143 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DISULFID 25 36 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 53 142 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 98 98 Interchain (with C-102 in alpha chain).
{ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 119 134 {ECO:0000255|PROSITE-ProRule:PRU00040}.
SEQUENCE 146 AA; 16834 MW; 9B7BC3A2C33AEF18 CRC64;
MGRFIFVSFG LLVVFLSLSG TGADCPSDWS SYEGHCYRVF QQQMNWADAE KFCTQQRKES
HLVSFESSEE VDFVVSKTFP ILKENFVWIG LSNVWNGCRL QWSDGTELKY NAWSAESECI
ASKTTDNQWW SMDCSKTYPF VCKLIV


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