ID   SL9A_PROFL              Reviewed;         152 AA.
AC   P23806; Q91246; Q98UJ0;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Snaclec coagulation factor IX/factor X-binding protein subunit A;
DE            Short=IX/X-bp subunit A;
DE   Flags: Precursor;
OS   Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=88087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=8645314; DOI=10.1006/bbrc.1996.0414;
RA   Matsuzaki R., Yoshihara E., Yamada M., Shima K., Atoda H., Morita T.;
RT   "cDNA cloning of IX/X-BP, a heterogeneous two-chain anticoagulant protein
RT   from snake venom.";
RL   Biochem. Biophys. Res. Commun. 220:382-387(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-152.
RC   TISSUE=Venom gland;
RX   PubMed=12175618; DOI=10.1016/s0041-0101(01)00289-6;
RA   Tani A., Ogawa T., Nose T., Nikandrov N.N., Deshimaru M., Chijiwa T.,
RA   Chang C.C., Fukumaki Y., Ohno M.;
RT   "Characterization, primary structure and molecular evolution of
RT   anticoagulant protein from Agkistrodon actus venom.";
RL   Toxicon 40:803-813(2002).
RN   [3]
RP   PROTEIN SEQUENCE OF 24-152.
RC   TISSUE=Venom;
RX   PubMed=1831197; DOI=10.1016/s0021-9258(18)98563-7;
RA   Atoda H., Hyuga M., Morita T.;
RT   "The primary structure of coagulation factor IX/factor X-binding protein
RT   isolated from the venom of Trimeresurus flavoviridis. Homology with
RT   asialoglycoprotein receptors, proteoglycan core protein, tetranectin, and
RT   lymphocyte Fc epsilon receptor for immunoglobulin E.";
RL   J. Biol. Chem. 266:14903-14911(1991).
RN   [4]
RP   FUNCTION.
RX   PubMed=2613688; DOI=10.1093/oxfordjournals.jbchem.a122935;
RA   Atoda H., Morita T.;
RT   "A novel blood coagulation factor IX/factor X-binding protein with
RT   anticoagulant activity from the venom of Trimeresurus flavoviridis (Habu
RT   snake): isolation and characterization.";
RL   J. Biochem. 106:808-813(1989).
RN   [5]
RP   FUNCTION.
RX   PubMed=7925387; DOI=10.1111/j.1432-1033.1994.t01-1-00703.x;
RA   Atoda H., Yoshida N., Ishikawa M., Morita T.;
RT   "Binding properties of the coagulation factor IX/factor X-binding protein
RT   isolated from the venom of Trimeresurus flavoviridis.";
RL   Eur. J. Biochem. 224:703-708(1994).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 24-152, METAL-BINDING SITES, AND
RP   DISULFIDE BONDS.
RX   PubMed=9187649; DOI=10.1038/nsb0697-438;
RA   Mizuno H., Fujimoto Z., Koizumi M., Kano H., Atoda H., Morita T.;
RT   "Structure of coagulation factors IX/X-binding protein, a heterodimer of C-
RT   type lectin domains.";
RL   Nat. Struct. Biol. 4:438-441(1997).
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:0000269|PubMed:2613688, ECO:0000269|PubMed:7925387}.
CC   -!- SUBUNIT: Heterodimer of subunits A and B; disulfide-linked.
CC       {ECO:0000269|PubMed:9187649}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Calcium is required for ligand binding.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   EMBL; D83331; BAA11887.1; -; mRNA.
DR   EMBL; AB046491; BAB21452.1; -; mRNA.
DR   PIR; JC4690; JC4690.
DR   PDB; 1IXX; X-ray; 2.50 A; A/C/E=24-152.
DR   PDBsum; 1IXX; -.
DR   AlphaFoldDB; P23806; -.
DR   SMR; P23806; -.
DR   EvolutionaryTrace; P23806; -.
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   1: Evidence at protein level;
KW   3D-structure; Blood coagulation cascade inhibiting toxin; Calcium;
KW   Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW   Metal-binding; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:1831197"
FT   CHAIN           24..152
FT                   /note="Snaclec coagulation factor IX/factor X-binding
FT                   protein subunit A"
FT                   /id="PRO_0000017530"
FT   DOMAIN          24..152
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         66
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         70
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         151
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   DISULFID        25..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:9187649"
FT   DISULFID        53..150
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:9187649"
FT   DISULFID        102
FT                   /note="Interchain (with C-98 in subunit B)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:9187649"
FT   DISULFID        125..142
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:9187649"
FT   STRAND          36..44
FT                   /evidence="ECO:0007829|PDB:1IXX"
FT   HELIX           46..56
FT                   /evidence="ECO:0007829|PDB:1IXX"
FT   HELIX           68..81
FT                   /evidence="ECO:0007829|PDB:1IXX"
FT   STRAND          89..95
FT                   /evidence="ECO:0007829|PDB:1IXX"
FT   HELIX           119..121
FT                   /evidence="ECO:0007829|PDB:1IXX"
FT   STRAND          125..128
FT                   /evidence="ECO:0007829|PDB:1IXX"
FT   HELIX           130..132
FT                   /evidence="ECO:0007829|PDB:1IXX"
FT   STRAND          136..140
FT                   /evidence="ECO:0007829|PDB:1IXX"
FT   STRAND          146..151
FT                   /evidence="ECO:0007829|PDB:1IXX"
SQ   SEQUENCE   152 AA;  17213 MW;  FB3DDD2369009263 CRC64;
     MGRFIFMSFG LLVVAASLRG TGADCLSGWS SYEGHCYKAF EKYKTWEDAE RVCTEQAKGA
     HLVSIESSGE ADFVAQLVTQ NMKRLDFYIW IGLRVQGKVK QCNSEWSDGS SVSYENWIEA
     ESKTCLGLEK ETDFRKWVNI YCGQQNPFVC EA