ID   SL9B_BOTJA              Reviewed;          30 AA.
AC   Q9PS06;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Snaclec coagulation factor IX/factor X-binding protein subunit B;
DE            Short=IX/X-bp subunit B;
DE   Flags: Fragment;
OS   Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8724;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=8334120; DOI=10.1021/bi00078a012;
RA   Sekiya F., Atoda H., Morita T.;
RT   "Isolation and characterization of an anticoagulant protein homologous to
RT   botrocetin from the venom of Bothrops jararaca.";
RL   Biochemistry 32:6892-6897(1993).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, DEVELOPMENTAL STAGE, AND
RP   GLYCOSYLATION.
RC   TISSUE=Venom;
RX   PubMed=20146532; DOI=10.1021/pr901027r;
RA   Zelanis A., Tashima A.K., Rocha M.M., Furtado M.F., Camargo A.C., Ho P.L.,
RA   Serrano S.M.;
RT   "Analysis of the ontogenetic variation in the venom proteome/peptidome of
RT   Bothrops jararaca reveals different strategies to deal with prey.";
RL   J. Proteome Res. 9:2278-2291(2010).
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 B; disulfide-linked.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- DEVELOPMENTAL STAGE: This protein seems to be found in newborn
CC       B.jararaca venom but not in adult snake venom.
CC       {ECO:0000269|PubMed:20146532}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:20146532}.
CC   -!- MISCELLANEOUS: Calcium is required for ligand binding. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   PIR; A53088; A53088.
DR   AlphaFoldDB; Q9PS06; -.
DR   SMR; Q9PS06; -.
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; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   SUPFAM; SSF56436; SSF56436; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade inhibiting toxin; Calcium;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hemostasis impairing toxin; Metal-binding; Secreted; Toxin.
FT   CHAIN           1..>30
FT                   /note="Snaclec coagulation factor IX/factor X-binding
FT                   protein subunit B"
FT                   /id="PRO_0000355257"
FT   DOMAIN          9..>30
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        2..13
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   UNSURE          23
FT                   /note="Assigned by comparison with orthologs"
FT   NON_TER         30
SQ   SEQUENCE   30 AA;  3582 MW;  D7A2DFFE41F2B6FC CRC64;
     DCPSDWSPYE GHCYRVFTEP QNWADAEKFC