ID   SLBA_TRIST              Reviewed;         156 AA.
AC   Q71RQ7; Q71RQ2; Q71RQ4; Q71RQ6;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Snaclec stejaggregin-B subunit alpha;
DE   Flags: Precursor;
OS   Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera
OS   stejnegeri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX   NCBI_TaxID=39682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Lee W.-H., Liu H., Zhang Y.;
RT   "Cloning and characterization of C-type lectins from Trimeresurus
RT   stejnegeri venom.";
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Interferes with one step of hemostasis (modulation of
CC       platelet aggregation, or coagulation cascade, for example).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heteromultimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   EMBL; AF354918; AAQ15160.1; -; mRNA.
DR   EMBL; AF354919; AAQ15161.1; -; mRNA.
DR   EMBL; AF354920; AAQ15162.1; -; mRNA.
DR   EMBL; AF354921; AAQ15163.1; -; mRNA.
DR   EMBL; AF354922; AAQ15164.1; -; mRNA.
DR   EMBL; AF354923; AAQ15165.1; -; mRNA.
DR   AlphaFoldDB; Q71RQ7; -.
DR   SMR; Q71RQ7; -.
DR   PRIDE; Q71RQ7; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Hemostasis impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..156
FT                   /note="Snaclec stejaggregin-B subunit alpha"
FT                   /id="PRO_0000355305"
FT   DOMAIN          32..151
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..150
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        102
FT                   /note="Interchain (with C-98 in beta chain)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        125..142
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   VARIANT         6
FT                   /note="S -> F (in subunit alpha-2 and subunit alpha-3)"
FT   VARIANT         91
FT                   /note="I -> T (in subunit alpha-3)"
FT   VARIANT         154
FT                   /note="R -> G (in subunit alpha-4)"
SQ   SEQUENCE   156 AA;  17924 MW;  4AAF11F94167D58F CRC64;
     MGRFISVSFG LLVVFLSLSG TGADCPSDWS SFKQYCYQII KQLKTWEDAE RFCMDQVKGA
     HLVSIESYRE AVFVAQQLSE NVKTTKYDVW IGLSVVNKGQ QCSSEWSDGS SVSYENLVKP
     LSKKCFVLKK GTEFRKWFNV ACEQKHLFMC KFLRPR