FA9_BOVIN
ID FA9_BOVIN Reviewed; 462 AA.
AC P00741; F1MFL4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2015, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Coagulation factor IX;
DE EC=3.4.21.22;
DE AltName: Full=Christmas factor;
DE Contains:
DE RecName: Full=Coagulation factor IXa light chain;
DE Contains:
DE RecName: Full=Coagulation factor IXa heavy chain;
DE Flags: Precursor;
GN Name=F9;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP PROTEIN SEQUENCE OF 47-462, GAMMA-CARBOXYGLUTAMATION AT GLU-53; GLU-54;
RP GLU-61; GLU-63; GLU-66; GLU-67; GLU-72; GLU-73; GLU-76; GLU-79; GLU-82 AND
RP GLU-86, AND GLYCOSYLATION AT ASN-204; ASN-214; ASN-219 AND ASN-307.
RX PubMed=291916; DOI=10.1073/pnas.76.10.4990;
RA Katayama K., Ericsson L.H., Enfield D.L., Walsh K.A., Neurath H.,
RA Davie E.W., Titani K.;
RT "Comparison of amino acid sequence of bovine coagulation Factor IX
RT (Christmas factor) with that of other vitamin K-dependent plasma
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:4990-4994(1979).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=6782101; DOI=10.1016/s0021-9258(19)69627-4;
RA van Dieijen G., Tans G., Rosing J., Hemker H.C.;
RT "The role of phospholipid and factor VIIIa in the activation of bovine
RT factor X.";
RL J. Biol. Chem. 256:3433-3442(1981).
RN [4]
RP HYDROXYLATION AT ASP-110.
RX PubMed=6688526; DOI=10.1016/0006-291x(83)90961-0;
RA McMullen B.A., Fujikawa K., Kisiel W.;
RT "The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent
RT blood coagulation zymogens.";
RL Biochem. Biophys. Res. Commun. 115:8-14(1983).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 97-157.
RX PubMed=6287289; DOI=10.1038/299178a0;
RA Choo K.H., Gould K.G., Rees D.J.G., Brownlee G.G.;
RT "Molecular cloning of the gene for human anti-haemophilic factor IX.";
RL Nature 299:178-180(1982).
RN [6]
RP GLYCOSYLATION AT SER-99, AND STRUCTURE OF CARBOHYDRATE ON SER-99.
RX PubMed=3149637; DOI=10.1093/oxfordjournals.jbchem.a122571;
RA Hase S., Kawabata S., Nishimura H., Takeya H., Sueyoshi T., Miyata T.,
RA Iwanaga S., Takao T., Shimonishi Y., Ikenaka T.;
RT "A new trisaccharide sugar chain linked to a serine residue in bovine blood
RT coagulation factors VII and IX.";
RL J. Biochem. 104:867-868(1988).
RN [7]
RP GLYCOSYLATION AT SER-99, AND STRUCTURE OF CARBOHYDRATE ON SER-99.
RX PubMed=2129367; DOI=10.1007/978-1-4615-3806-6_12;
RA Iwanaga S., Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T.;
RT "A new trisaccharide sugar chain linked to a serine residue in the first
RT EGF-like domain of clotting factors VII and IX and protein Z.";
RL Adv. Exp. Med. Biol. 281:121-131(1990).
RN [8]
RP GLYCOSYLATION AT SER-99, AND STRUCTURE OF CARBOHYDRATE ON SER-99.
RX PubMed=2105311; DOI=10.1016/s0021-9258(19)39908-9;
RA Hase S., Nishimura H., Kawabata S., Iwanaga S., Ikenaka T.;
RT "The structure of (xylose)2glucose-O-serine 53 found in the first epidermal
RT growth factor-like domain of bovine blood clotting factor IX.";
RL J. Biol. Chem. 265:1858-1861(1990).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 47-92 IN COMPLEX WITH SNAKE VENOM
RP COAGULATION FACTOR IX-BINDING PROTEIN; CALCIUM AND MAGNESIUM,
RP GAMMA-CARBOXYGLUTAMATION AT GLU-53; GLU-54; GLU-61; GLU-63; GLU-66; GLU-67;
RP GLU-72; GLU-73; GLU-76; GLU-79; GLU-82 AND GLU-86, METAL-BINDING SITES,
RP DISULFIDE BOND, DOMAIN, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Factor IX is a vitamin K-dependent plasma protein that
CC participates in the intrinsic pathway of blood coagulation by
CC converting factor X to its active form in the presence of Ca(2+) ions,
CC phospholipids, and factor VIIIa. {ECO:0000269|PubMed:6782101}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form
CC factor Xa.; EC=3.4.21.22; Evidence={ECO:0000269|PubMed:6782101};
CC -!- SUBUNIT: Heterodimer of a light chain and a heavy chain; disulfide-
CC linked, Interacts with SERPINC1 (By similarity). Interacts with the
CC heterodimeric snake venom coagulation factor IX-binding protein
CC (PubMed:12695512). {ECO:0000250|UniProtKB:P00740,
CC ECO:0000269|PubMed:12695512}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12695512}.
CC -!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level)
CC (PubMed:12695512). {ECO:0000269|PubMed:12695512}.
CC -!- DOMAIN: Calcium binds to the gamma-carboxyglutamic acid (Gla) residues
CC in the Gla domain (PubMed:12695512). Calcium can also bind, with
CC stronger affinity, to another site beyond the Gla domain (By
CC similarity). Under physiological ion concentrations, Ca(2+) is
CC displaced by Mg(2+) from some of the gammaglutamate residues in the N-
CC terminal Gla domain. This leads to a subtle conformation change that
CC may affect the interaction with its binding protein (PubMed:12695512).
CC {ECO:0000250|UniProtKB:P00740, ECO:0000269|PubMed:12695512}.
CC -!- PTM: Activated by factor XIa, which excises the activation peptide. The
CC propeptide can also be removed by snake venom protease.
CC {ECO:0000250|UniProtKB:P00740}.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains.
CC {ECO:0000269|PubMed:6688526}.
CC -!- PTM: Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro.
CC {ECO:0000250|UniProtKB:P00740}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; DAAA02067809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02067810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J00007; AAA30520.1; -; mRNA.
DR PIR; A14757; KFBO.
DR RefSeq; XP_005227591.1; XM_005227534.3.
DR PDB; 1J34; X-ray; 1.55 A; C=47-92.
DR PDB; 1J35; X-ray; 1.80 A; C=47-92.
DR PDBsum; 1J34; -.
DR PDBsum; 1J35; -.
DR AlphaFoldDB; P00741; -.
DR SMR; P00741; -.
DR STRING; 9913.ENSBTAP00000005227; -.
DR MEROPS; S01.214; -.
DR GlyConnect; 97; 5 N-Linked glycans, 1 O-Linked glycan (1 site).
DR iPTMnet; P00741; -.
DR PaxDb; P00741; -.
DR PRIDE; P00741; -.
DR eggNOG; ENOG502QUEV; Eukaryota.
DR InParanoid; P00741; -.
DR OrthoDB; 1314811at2759; -.
DR TreeFam; TF327329; -.
DR SABIO-RK; P00741; -.
DR EvolutionaryTrace; P00741; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007596; P:blood coagulation; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0031638; P:zymogen activation; IDA:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 4.10.740.10; -; 1.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR035694; Coagulation_factor_IX.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR012224; Pept_S1A_FX.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24278:SF31; PTHR24278:SF31; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00001; GLABLOOD.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57630; SSF57630; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation; Calcium; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein;
KW Hemophilia; Hemostasis; Hydrolase; Hydroxylation; Magnesium; Metal-binding;
KW Phosphoprotein; Protease; Reference proteome; Secreted; Serine protease;
KW Signal; Sulfation; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..462
FT /note="Coagulation factor IX"
FT /id="PRO_0000027741"
FT PROPEP 29..46
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT /id="PRO_0000433084"
FT CHAIN 47..192
FT /note="Coagulation factor IXa light chain"
FT /id="PRO_0000027742"
FT PROPEP 193..227
FT /note="Activation peptide"
FT /id="PRO_0000027743"
FT CHAIN 228..462
FT /note="Coagulation factor IXa heavy chain"
FT /id="PRO_0000027744"
FT DOMAIN 47..92
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DOMAIN 93..129
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 130..171
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 228..460
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 268
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT ACT_SITE 316
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT ACT_SITE 412
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J35"
FT BINDING 61
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT BINDING 66
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT BINDING 72
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT SITE 192..193
FT /note="Cleavage; by factor XIa"
FT SITE 227..228
FT /note="Cleavage; by factor XIa"
FT MOD_RES 53
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT MOD_RES 54
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT MOD_RES 61
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT MOD_RES 63
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT MOD_RES 66
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT MOD_RES 67
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT MOD_RES 72
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT MOD_RES 73
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT MOD_RES 76
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT MOD_RES 79
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT MOD_RES 82
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT MOD_RES 86
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT MOD_RES 110
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000269|PubMed:6688526"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 202
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 85
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 99
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:2105311,
FT ECO:0000269|PubMed:2129367, ECO:0000269|PubMed:3149637"
FT /id="CAR_000008"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:291916"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:291916"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:291916"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:291916"
FT DISULFID 64..69
FT /evidence="ECO:0000269|PubMed:12695512,
FT ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"
FT DISULFID 97..108
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 102..117
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 119..128
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 134..145
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 141..155
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 157..170
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 178..336
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 253..269
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 383..397
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 408..436
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CONFLICT 110
FT /note="D -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="L -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1J34"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1J34"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:1J34"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:1J34"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:1J34"
SQ SEQUENCE 462 AA; 52046 MW; 415B2A7BD6EA256A CRC64;
MWCLNMIMAE SPGLVTICLL GYLLSAECTV FLDRENATKI LHRPKRYNSG KLEEFVRGNL
ERECKEEKCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN PCLNGGMCKD DINSYECWCQ
AGFEGTNCEL DATCSIKNGR CKQFCKRDTD NKVVCSCTDG YRLAEDQKSC EPAVPFPCGR
VSVSHISKKL TRAETIFSNT NYENSSEAEI IWDNVTQSNQ SFDEFSRVVG GEDAERGQFP
WQVLLHGEIA AFCGGSIVNE KWVVTAAHCI KPGVKITVVA GEHNTEKPEP TEQKRNVIRA
IPYHSYNASI NKYSHDIALL ELDEPLELNS YVTPICIADR DYTNIFLKFG YGYVSGWGKV
FNRGRSASIL QYLKVPLVDR ATCLRSTKFS IYSHMFCAGY HEGGKDSCQG DSGGPHVTEV
EGTSFLTGII SWGEECAMKG KYGIYTKVSR YVNWIKEKTK LT
