SLA_PROFL
ID SLA_PROFL Reviewed; 129 AA.
AC Q7LZ71;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Snaclec coagulation factor IX-binding protein subunit A;
DE Short=IX-bp subunit A;
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 PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
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 [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), METAL-BINDING SITES, AND DISULFIDE
RP BONDS.
RC TISSUE=Venom;
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 [3]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH IX/X-BP SUBUNIT B
RP AND COAGULATION FACTOR IX, FUNCTION, SUBUNIT, METAL-BINDING SITES, AND
RP DISULFIDE BOND.
RC TISSUE=Venom;
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 [4]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS), METAL-BINDING SITES, AND DISULFIDE
RP BONDS.
RC TISSUE=Venom;
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: Anticoagulant protein which binds to the gamma-
CC carboxyglutamic acid-domain regions of factor IX (F9) (but not factor
CC X) in the presence of calcium with a 1 to 1 stoichiometry.
CC {ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:8749314}.
CC -!- SUBUNIT: Heterodimer of subunits A and B; disulfide-linked.
CC {ECO:0000269|PubMed:10339409, ECO:0000269|PubMed:12695512,
CC ECO:0000269|PubMed:16165155, ECO:0000269|PubMed:8749314}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR PIR; JC4329; JC4329.
DR PDB; 1BJ3; X-ray; 2.60 A; A=1-129.
DR PDB; 1J34; X-ray; 1.55 A; A=1-129.
DR PDB; 1J35; X-ray; 1.80 A; A=1-129.
DR PDB; 1X2T; X-ray; 1.72 A; A/C=1-129.
DR PDB; 1X2W; X-ray; 2.29 A; A=1-129.
DR PDBsum; 1BJ3; -.
DR PDBsum; 1J34; -.
DR PDBsum; 1J35; -.
DR PDBsum; 1X2T; -.
DR PDBsum; 1X2W; -.
DR AlphaFoldDB; Q7LZ71; -.
DR SMR; Q7LZ71; -.
DR EvolutionaryTrace; Q7LZ71; -.
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; Toxin.
FT CHAIN 1..129
FT /note="Snaclec coagulation factor IX-binding protein
FT subunit A"
FT /id="PRO_0000346754"
FT DOMAIN 1..129
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT BINDING 41
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:0007744|PDB:1BJ3, ECO:0007744|PDB:1J34,
FT ECO:0007744|PDB:1J35, ECO:0007744|PDB:1X2T"
FT BINDING 43
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:0007744|PDB:1BJ3, ECO:0007744|PDB:1J34,
FT ECO:0007744|PDB:1J35, ECO:0007744|PDB:1X2T"
FT BINDING 47
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:0007744|PDB:1BJ3, ECO:0007744|PDB:1J34,
FT ECO:0007744|PDB:1J35, ECO:0007744|PDB:1X2T"
FT BINDING 128
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:0007744|PDB:1BJ3, ECO:0007744|PDB:1J34,
FT ECO:0007744|PDB:1J35, ECO:0007744|PDB:1X2T"
FT DISULFID 2..13
FT /evidence="ECO:0000269|PubMed:10339409,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:16165155,
FT ECO:0007744|PDB:1BJ3, ECO:0007744|PDB:1J34,
FT ECO:0007744|PDB:1J35, ECO:0007744|PDB:1X2T,
FT ECO:0007744|PDB:1X2W"
FT DISULFID 30..127
FT /evidence="ECO:0000269|PubMed:10339409,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:16165155,
FT ECO:0007744|PDB:1BJ3, ECO:0007744|PDB:1J34,
FT ECO:0007744|PDB:1J35, ECO:0007744|PDB:1X2T,
FT ECO:0007744|PDB:1X2W"
FT DISULFID 79
FT /note="Interchain (with C-98 in subunit B)"
FT /evidence="ECO:0000269|PubMed:12695512"
FT DISULFID 102..119
FT /evidence="ECO:0000269|PubMed:10339409,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:16165155,
FT ECO:0007744|PDB:1BJ3, ECO:0007744|PDB:1J34,
FT ECO:0007744|PDB:1J35, ECO:0007744|PDB:1X2T,
FT ECO:0007744|PDB:1X2W"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:1J34"
FT STRAND 12..21
FT /evidence="ECO:0007829|PDB:1J34"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:1J34"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:1J34"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1J35"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:1J34"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:1J35"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1J34"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:1J34"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1J34"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1J34"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:1J34"
SQ SEQUENCE 129 AA; 14640 MW; 225F3C7D841D8C76 CRC64;
DCPSGWSSYE GHCYKPFKLY KTWDDAERFC TEQAKGGHLV SIESAGEADF VAQLVTENIQ
NTKSYVWIGL RVQGKEKQCS SEWSDGSSVS YENWIEAESK TCLGLEKETG FRKWVNIYCG
QQNPFVCEA
