ID   SLB_PROJR               Reviewed;         146 AA.
AC   D1MGU1;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Snaclec jerdonibitin subunit beta;
DE   AltName: Full=TJ-GPIb-bp subunit beta;
DE   Flags: Precursor;
OS   Protobothrops jerdonii (Jerdon's pitviper) (Trimeresurus jerdonii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=242841;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-45, FUNCTION, AND
RP   SUBUNIT.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=21256857; DOI=10.1016/j.toxicon.2011.01.010;
RA   Chen Z., Wu J., Zhang Y., Yang X., Yu G., Zhu S., Lee W., Lu Q., Zhang Y.;
RT   "A novel platelet glycoprotein Ib-binding protein with human platelet
RT   aggregation-inhibiting activity from Trimeresurus jerdonii venom.";
RL   Toxicon 57:672-679(2011).
CC   -!- FUNCTION: Snaclec that dose-dependently inhibits platelet aggregation
CC       induced by ristocetin or low-dose thrombin, but not by high-dose
CC       thrombin. Binds to GPIbalpha (GP1BA). In vivo, also dose-dependently
CC       induces thrombocytopenia of mice and platelet counts remains at very
CC       low level even after 18 hours intravenous injection.
CC       {ECO:0000269|PubMed:21256857}.
CC   -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
CC       {ECO:0000269|PubMed:21256857}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Does not induce platelet aggregation in either platelet
CC       rich plasma or washed platelets under high-dose conditions. Does not
CC       inhibit platelet aggregation induced by high-dose thrombin. Does not
CC       react with polyclonal anti-GPVI and anti-GPIIb antibodies
CC       (PubMed:21256857). {ECO:0000305|PubMed:21256857}.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   EMBL; GU146050; ACZ34294.1; -; mRNA.
DR   AlphaFoldDB; D1MGU1; -.
DR   SMR; D1MGU1; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0044218; C:other organism cell membrane; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044477; P:envenomation resulting in negative regulation of platelet aggregation in another organism; IDA:UniProtKB.
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 inhibiting toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:21256857"
FT   CHAIN           24..146
FT                   /note="Snaclec jerdonibitin subunit beta"
FT                   /id="PRO_0000422431"
FT   DOMAIN          32..143
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        25..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        53..142
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        98
FT                   /note="Interchain (with C-102 in alpha chain)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        119..134
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   146 AA;  16834 MW;  9B7BC3A2C33AEF18 CRC64;
     MGRFIFVSFG LLVVFLSLSG TGADCPSDWS SYEGHCYRVF QQQMNWADAE KFCTQQRKES
     HLVSFESSEE VDFVVSKTFP ILKENFVWIG LSNVWNGCRL QWSDGTELKY NAWSAESECI
     ASKTTDNQWW SMDCSKTYPF VCKLIV