SL9B_PROFL
ID SL9B_PROFL Reviewed; 146 AA.
AC P23807; Q91247;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Snaclec coagulation factor IX/factor X-binding protein subunit B;
DE Short=IX/X-bp subunit B;
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 PROTEIN SEQUENCE OF 24-146.
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 [3]
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 [4]
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 [5]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=8749314; DOI=10.1093/jb/118.5.965;
RA Atoda H., Ishikawa M., Yoshihara E., Sekiya F., Morita T.;
RT "Blood coagulation factor IX-binding protein from the venom of Trimeresurus
RT flavoviridis: purification and characterization.";
RL J. Biochem. 118:965-973(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 24-146 IN DIMER WITH IX/X-BP,
RP METAL-BINDING SITES, DISULFIDE BONDS, AND SUBUNIT.
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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 24-146 IN DIMER WITH IX-BP,
RP METAL-BINDING SITES, DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=10339409; DOI=10.1006/jmbi.1999.2756;
RA Mizuno H., Fujimoto Z., Koizumi M., Kano H., Atoda H., Morita T.;
RT "Crystal structure of coagulation factor IX-binding protein from habu snake
RT venom at 2.6 A: implication of central loop swapping based on deletion in
RT the linker region.";
RL J. Mol. Biol. 289:103-112(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 24-146 IN COMPLEX WITH IX-BPAND
RP COAGULATION FACTOR IX, METAL-BINDING SITES, DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=12695512; DOI=10.1074/jbc.m300650200;
RA Shikamoto Y., Morita T., Fujimoto Z., Mizuno H.;
RT "Crystal structure of Mg2+- and Ca2+-bound Gla domain of factor IX
RT complexed with binding protein.";
RL J. Biol. Chem. 278:24090-24094(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 24-146 IN DIMER WITH IX-BP,
RP METAL-BINDING SITES, AND DISULFIDE BONDS.
RX PubMed=16165155; DOI=10.1016/j.jmb.2005.08.018;
RA Suzuki N., Fujimoto Z., Morita T., Fukamizu A., Mizuno H.;
RT "pH-dependent structural changes at Ca(2+)-binding sites of coagulation
RT factor IX-binding protein.";
RL J. Mol. Biol. 353:80-87(2005).
CC -!- FUNCTION: When linked to subunit A of IX/X-bp, anticoagulant protein
CC which binds to the gamma-carboxyglutamic acid-domain regions of factors
CC IX (F9) and factor X (10) in the presence of calcium with a 1 to 1
CC stoichiometry.
CC -!- FUNCTION: When linked to subunit A of IX-bp, anticoagulant protein
CC which binds to the gamma-carboxyglutamic acid-domain regions of factor
CC IX (but not to factor X) in the presence of calcium with a 1 to 1
CC stoichiometry. {ECO:0000269|PubMed:12695512,
CC ECO:0000269|PubMed:2613688, ECO:0000269|PubMed:7925387,
CC ECO:0000269|PubMed:8749314}.
CC -!- SUBUNIT: Heterodimer with subunit A of IX/X-bp or IX-bp; disulfide-
CC linked. {ECO:0000269|PubMed:10339409, ECO:0000269|PubMed:12695512,
CC ECO:0000269|PubMed:16165155, 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; D83332; BAA11888.1; -; mRNA.
DR PIR; JC4691; JC4691.
DR PDB; 1BJ3; X-ray; 2.60 A; B=24-146.
DR PDB; 1IXX; X-ray; 2.50 A; B/D/F=24-146.
DR PDB; 1J34; X-ray; 1.55 A; B=24-146.
DR PDB; 1J35; X-ray; 1.80 A; B=24-146.
DR PDB; 1X2T; X-ray; 1.72 A; B/D=24-146.
DR PDB; 1X2W; X-ray; 2.29 A; B=24-146.
DR PDBsum; 1BJ3; -.
DR PDBsum; 1IXX; -.
DR PDBsum; 1J34; -.
DR PDBsum; 1J35; -.
DR PDBsum; 1X2T; -.
DR PDBsum; 1X2W; -.
DR AlphaFoldDB; P23807; -.
DR SMR; P23807; -.
DR EvolutionaryTrace; P23807; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
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..146
FT /note="Snaclec coagulation factor IX/factor X-binding
FT protein subunit B"
FT /id="PRO_0000017531"
FT DOMAIN 24..146
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 /evidence="ECO:0000269|PubMed:10339409,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:16165155,
FT ECO:0000269|PubMed:9187649, ECO:0007744|PDB:1BJ3,
FT ECO:0007744|PDB:1IXX, ECO:0007744|PDB:1J34,
FT ECO:0007744|PDB:1J35, ECO:0007744|PDB:1X2T"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10339409,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:16165155,
FT ECO:0000269|PubMed:9187649, ECO:0007744|PDB:1BJ3,
FT ECO:0007744|PDB:1IXX, ECO:0007744|PDB:1J34,
FT ECO:0007744|PDB:1J35, ECO:0007744|PDB:1X2T"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10339409,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:16165155,
FT ECO:0000269|PubMed:9187649, ECO:0007744|PDB:1BJ3,
FT ECO:0007744|PDB:1IXX, ECO:0007744|PDB:1J34,
FT ECO:0007744|PDB:1J35, ECO:0007744|PDB:1X2T"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10339409,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:16165155,
FT ECO:0000269|PubMed:9187649, ECO:0007744|PDB:1BJ3,
FT ECO:0007744|PDB:1IXX, ECO:0007744|PDB:1J34,
FT ECO:0007744|PDB:1J35, ECO:0007744|PDB:1X2T"
FT DISULFID 25..36
FT /evidence="ECO:0000269|PubMed:10339409,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:16165155,
FT ECO:0000269|PubMed:9187649, ECO:0007744|PDB:1BJ3,
FT ECO:0007744|PDB:1IXX, ECO:0007744|PDB:1J34,
FT ECO:0007744|PDB:1J35, ECO:0007744|PDB:1X2T,
FT ECO:0007744|PDB:1X2W"
FT DISULFID 53..142
FT /evidence="ECO:0000269|PubMed:10339409,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:16165155,
FT ECO:0000269|PubMed:9187649, ECO:0007744|PDB:1BJ3,
FT ECO:0007744|PDB:1IXX, ECO:0007744|PDB:1J34,
FT ECO:0007744|PDB:1J35, ECO:0007744|PDB:1X2T,
FT ECO:0007744|PDB:1X2W"
FT DISULFID 98
FT /note="Interchain (with C-102 in subunit A of IX/X-bp or
FT with C-79 in subunit A of IX-bp)"
FT /evidence="ECO:0000269|PubMed:10339409,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:16165155,
FT ECO:0000269|PubMed:9187649"
FT DISULFID 119..134
FT /evidence="ECO:0000269|PubMed:10339409,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:16165155,
FT ECO:0000269|PubMed:9187649, ECO:0007744|PDB:1BJ3,
FT ECO:0007744|PDB:1IXX, ECO:0007744|PDB:1J34,
FT ECO:0007744|PDB:1J35, ECO:0007744|PDB:1X2T,
FT ECO:0007744|PDB:1X2W"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1J34"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:1J34"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:1J34"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:1J34"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1J34"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:1X2T"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1J34"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1IXX"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1J34"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:1J34"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:1J34"
SQ SEQUENCE 146 AA; 16922 MW; 8E1961C59F96757C CRC64;
MGRFIFMSFG FLVVFLSLSG TAADCPSDWS SYEGHCYKPF SEPKNWADAE NFCTQQHAGG
HLVSFQSSEE ADFVVKLAFQ TFGHSIFWMG LSNVWNQCNW QWSNAAMLRY KAWAEESYCV
YFKSTNNKWR SRACRMMAQF VCEFQA
