ID   SL9B1_TRIST             Reviewed;         144 AA.
AC   Q71RR2;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Snaclec coagulation factor IX/factor X-binding protein subunit B1;
DE            Short=IX/X-bp subunit B1;
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: Anticoagulant protein which binds to the gamma-
CC       carboxyglutamic acid-domain regions of factors IX (F9) and factor X
CC       (F10) in the presence of calcium with a 1 to 1 stoichiometry.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of subunits A and B1; disulfide-linked.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Calcium is required for ligand binding. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   EMBL; AF354912; AAQ15154.1; -; mRNA.
DR   EMBL; AF354913; AAQ15155.1; -; mRNA.
DR   AlphaFoldDB; Q71RR2; -.
DR   SMR; Q71RR2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Blood coagulation cascade inhibiting toxin; Calcium; Disulfide bond;
KW   Hemostasis impairing toxin; Metal-binding; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..144
FT                   /note="Snaclec coagulation factor IX/factor X-binding
FT                   protein subunit B1"
FT                   /id="PRO_0000356314"
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 subunit A)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        119..134
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   144 AA;  16709 MW;  2FDC57E5B12BBBA8 CRC64;
     MGRFIFVSFG LLVVFLSLSG TAADCLSGWS SYEGHCYKPF NELKNWADAE NFCTQQQAGG
     HLVSFQSSEE ADFVVKLAFQ TFDHSIFWMG LSNVWNQCNW QWSNAAMLRY KAWAEESYCV
     YFKSTNNKWR SRSCRMMANF VCEF