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Coagulation factor IX (EC 3.4.21.22) (Christmas factor) [Cleaved into: Coagulation factor IXa light chain; Coagulation factor IXa heavy chain]

 FA9_BOVIN               Reviewed;         462 AA.
P00741; F1MFL4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
27-MAY-2015, sequence version 2.
05-DEC-2018, entry version 188.
RecName: Full=Coagulation factor IX;
EC=3.4.21.22;
AltName: Full=Christmas factor;
Contains:
RecName: Full=Coagulation factor IXa light chain;
Contains:
RecName: Full=Coagulation factor IXa heavy chain;
Flags: Precursor;
Name=F9;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Hereford;
PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C.,
Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S.,
Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
"A whole-genome assembly of the domestic cow, Bos taurus.";
Genome Biol. 10:R42.01-R42.10(2009).
[2]
PROTEIN SEQUENCE OF 47-462, GAMMA-CARBOXYGLUTAMATION AT GLU-53;
GLU-54; GLU-61; GLU-63; GLU-66; GLU-67; GLU-72; GLU-73; GLU-76;
GLU-79; GLU-82 AND GLU-86, AND GLYCOSYLATION AT ASN-204; ASN-214;
ASN-219 AND ASN-307.
PubMed=291916; DOI=10.1073/pnas.76.10.4990;
Katayama K., Ericsson L.H., Enfield D.L., Walsh K.A., Neurath H.,
Davie E.W., Titani K.;
"Comparison of amino acid sequence of bovine coagulation Factor IX
(Christmas factor) with that of other vitamin K-dependent plasma
proteins.";
Proc. Natl. Acad. Sci. U.S.A. 76:4990-4994(1979).
[3]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=6782101;
van Dieijen G., Tans G., Rosing J., Hemker H.C.;
"The role of phospholipid and factor VIIIa in the activation of bovine
factor X.";
J. Biol. Chem. 256:3433-3442(1981).
[4]
HYDROXYLATION AT ASP-110.
PubMed=6688526; DOI=10.1016/0006-291X(83)90961-0;
McMullen B.A., Fujikawa K., Kisiel W.;
"The occurrence of beta-hydroxyaspartic acid in the vitamin K-
dependent blood coagulation zymogens.";
Biochem. Biophys. Res. Commun. 115:8-14(1983).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 97-157.
PubMed=6287289; DOI=10.1038/299178a0;
Choo K.H., Gould K.G., Rees D.J.G., Brownlee G.G.;
"Molecular cloning of the gene for human anti-haemophilic factor IX.";
Nature 299:178-180(1982).
[6]
GLYCOSYLATION AT SER-99, AND STRUCTURE OF CARBOHYDRATE ON SER-99.
PubMed=3149637;
Hase S., Kawabata S., Nishimura H., Takeya H., Sueyoshi T., Miyata T.,
Iwanaga S., Takao T., Shimonishi Y., Ikenaka T.;
"A new trisaccharide sugar chain linked to a serine residue in bovine
blood coagulation factors VII and IX.";
J. Biochem. 104:867-868(1988).
[7]
GLYCOSYLATION AT SER-99, AND STRUCTURE OF CARBOHYDRATE ON SER-99.
PubMed=2129367;
Iwanaga S., Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T.;
"A new trisaccharide sugar chain linked to a serine residue in the
first EGF-like domain of clotting factors VII and IX and protein Z.";
Adv. Exp. Med. Biol. 281:121-131(1990).
[8]
GLYCOSYLATION AT SER-99, AND STRUCTURE OF CARBOHYDRATE ON SER-99.
PubMed=2105311;
Hase S., Nishimura H., Kawabata S., Iwanaga S., Ikenaka T.;
"The structure of (xylose)2glucose-O-serine 53 found in the first
epidermal growth factor-like domain of bovine blood clotting factor
IX.";
J. Biol. Chem. 265:1858-1861(1990).
[9]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 47-92 IN COMPLEX WITH SNAKE
VENOM COAGULATION FACTOR IX-BINDING PROTEIN; CALCIUM AND MAGNESIUM,
GAMMA-CARBOXYGLUTAMATION AT GLU-53; GLU-54; GLU-61; GLU-63; GLU-66;
GLU-67; GLU-72; GLU-73; GLU-76; GLU-79; GLU-82 AND GLU-86,
METAL-BINDING SITES, DISULFIDE BOND, DOMAIN, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=12695512; DOI=10.1074/jbc.M300650200;
Shikamoto Y., Morita T., Fujimoto Z., Mizuno H.;
"Crystal structure of Mg2+- and Ca2+-bound Gla domain of factor IX
complexed with binding protein.";
J. Biol. Chem. 278:24090-24094(2003).
-!- FUNCTION: Factor IX is a vitamin K-dependent plasma protein that
participates in the intrinsic pathway of blood coagulation by
converting factor X to its active form in the presence of Ca(2+)
ions, phospholipids, and factor VIIIa.
{ECO:0000269|PubMed:6782101}.
-!- CATALYTIC ACTIVITY:
Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form
factor Xa.; EC=3.4.21.22; Evidence={ECO:0000269|PubMed:6782101};
-!- SUBUNIT: Heterodimer of a light chain and a heavy chain;
disulfide-linked, Interacts with SERPINC1 (By similarity).
Interacts with the heterodimeric snake venom coagulation factor
IX-binding protein (PubMed:12695512).
{ECO:0000250|UniProtKB:P00740, ECO:0000269|PubMed:12695512}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12695512}.
-!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level)
(PubMed:12695512). {ECO:0000269|PubMed:12695512}.
-!- DOMAIN: Calcium binds to the gamma-carboxyglutamic acid (Gla)
residues in the Gla domain (PubMed:12695512). Calcium can also
bind, with stronger affinity, to another site beyond the Gla
domain (By similarity). Under physiological ion concentrations,
Ca(2+) is displaced by Mg(2+) from some of the gammaglutamate
residues in the N-terminal Gla domain. This leads to a subtle
conformation change that may affect the interaction with its
binding protein (PubMed:12695512). {ECO:0000250|UniProtKB:P00740,
ECO:0000269|PubMed:12695512}.
-!- PTM: Activated by factor XIa, which excises the activation
peptide. The propeptide can also be removed by snake venom
protease. {ECO:0000250|UniProtKB:P00740}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
aspartate and asparagine is (R) stereospecific within EGF domains.
{ECO:0000269|PubMed:6688526}.
-!- PTM: Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro.
{ECO:0000250|UniProtKB:P00740}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; DAAA02067809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; DAAA02067810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; J00007; AAA30520.1; -; mRNA.
PIR; A14757; KFBO.
RefSeq; XP_005227591.1; XM_005227534.3.
UniGene; Bt.13106; -.
PDB; 1J34; X-ray; 1.55 A; C=47-92.
PDB; 1J35; X-ray; 1.80 A; C=47-92.
PDBsum; 1J34; -.
PDBsum; 1J35; -.
ProteinModelPortal; P00741; -.
SMR; P00741; -.
STRING; 9913.ENSBTAP00000005227; -.
MEROPS; S01.214; -.
GlyConnect; 97; -.
iPTMnet; P00741; -.
UniCarbKB; P00741; -.
PaxDb; P00741; -.
PRIDE; P00741; -.
Ensembl; ENSBTAT00000005227; ENSBTAP00000005227; ENSBTAG00000004003.
VGNC; VGNC:28691; F9.
eggNOG; ENOG410IGPV; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00940000159516; -.
HOGENOM; HOG000251821; -.
HOVERGEN; HBG013304; -.
InParanoid; P00741; -.
OMA; SYECWCQ; -.
OrthoDB; EOG091G0AH5; -.
TreeFam; TF327329; -.
Reactome; R-BTA-140834; Extrinsic Pathway of Fibrin Clot Formation.
Reactome; R-BTA-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-BTA-159740; Gamma-carboxylation of protein precursors.
Reactome; R-BTA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
Reactome; R-BTA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
SABIO-RK; P00741; -.
EvolutionaryTrace; P00741; -.
PMAP-CutDB; P00741; -.
Proteomes; UP000009136; Chromosome X.
Bgee; ENSBTAG00000004003; Expressed in 2 organ(s), highest expression level in liver.
ExpressionAtlas; P00741; baseline and differential.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0007596; P:blood coagulation; ISS:UniProtKB.
GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
GO; GO:0031638; P:zymogen activation; IDA:UniProtKB.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
InterPro; IPR035694; Coagulation_factor_IX.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR012224; Pept_S1A_FX.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR44064:SF4; PTHR44064:SF4; 1.
Pfam; PF00008; EGF; 1.
Pfam; PF00594; Gla; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001143; Factor_X; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
PRINTS; PR00001; GLABLOOD.
SMART; SM00181; EGF; 2.
SMART; SM00179; EGF_CA; 1.
SMART; SM00069; GLA; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57630; SSF57630; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS00011; GLA_1; 1.
PROSITE; PS50998; GLA_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Blood coagulation; Calcium; Complete proteome;
Direct protein sequencing; Disulfide bond; EGF-like domain;
Gamma-carboxyglutamic acid; Glycoprotein; Hemophilia; Hemostasis;
Hydrolase; Hydroxylation; Magnesium; Metal-binding; Phosphoprotein;
Protease; Reference proteome; Secreted; Serine protease; Signal;
Sulfation; Zymogen.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 462 Coagulation factor IX.
/FTId=PRO_0000027741.
PROPEP 29 46 {ECO:0000250|UniProtKB:P00740}.
/FTId=PRO_0000433084.
CHAIN 47 192 Coagulation factor IXa light chain.
/FTId=PRO_0000027742.
PROPEP 193 227 Activation peptide.
/FTId=PRO_0000027743.
CHAIN 228 462 Coagulation factor IXa heavy chain.
/FTId=PRO_0000027744.
DOMAIN 47 92 Gla. {ECO:0000255|PROSITE-
ProRule:PRU00463}.
DOMAIN 93 129 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 130 171 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 228 460 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 268 268 Charge relay system.
{ECO:0000250|UniProtKB:P00740}.
ACT_SITE 316 316 Charge relay system.
{ECO:0000250|UniProtKB:P00740}.
ACT_SITE 412 412 Charge relay system.
{ECO:0000250|UniProtKB:P00740}.
METAL 47 47 Calcium 1; via carbonyl oxygen.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 48 48 Calcium 2. {ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 53 53 Calcium 1; via 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 53 53 Calcium 2; via 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 54 54 Calcium 2; via 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 54 54 Calcium 3; via 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 61 61 Calcium 4 or magnesium 1; via 4-
carboxyglutamate. {ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 63 63 Calcium 1; via 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 63 63 Calcium 2; via 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 63 63 Calcium 3; via 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 66 66 Calcium 4 or magnesium 1; via 4-
carboxyglutamate. {ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 67 67 Calcium 1; via 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 72 72 Calcium 5 or magnesium 2; via 4-
carboxyglutamate. {ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 73 73 Calcium 2; via 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 73 73 Calcium 3; via 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 76 76 Calcium 3; via 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00740}.
METAL 76 76 Calcium 5 or magnesium 2; via 4-
carboxyglutamate.
{ECO:0000250|UniProtKB:P00740}.
METAL 82 82 Calcium 6 or magnesium 3; via 4-
carboxyglutamate. {ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 86 86 Calcium 6 or magnesium 3; via 4-
carboxyglutamate. {ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
METAL 93 93 Calcium 7.
{ECO:0000250|UniProtKB:P00740}.
METAL 94 94 Calcium 7; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P00740}.
METAL 96 96 Calcium 7.
{ECO:0000250|UniProtKB:P00740}.
METAL 110 110 Calcium 7.
{ECO:0000250|UniProtKB:P00740}.
METAL 111 111 Calcium 7; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P00740}.
METAL 282 282 Calcium 8.
{ECO:0000250|UniProtKB:P00740}.
METAL 284 284 Calcium 8; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P00740}.
METAL 289 289 Calcium 8.
{ECO:0000250|UniProtKB:P00740}.
METAL 292 292 Calcium 8.
{ECO:0000250|UniProtKB:P00740}.
SITE 192 193 Cleavage; by factor XIa.
SITE 227 228 Cleavage; by factor XIa.
MOD_RES 53 53 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12695512,
ECO:0000269|PubMed:291916}.
MOD_RES 54 54 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12695512,
ECO:0000269|PubMed:291916}.
MOD_RES 61 61 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12695512,
ECO:0000269|PubMed:291916}.
MOD_RES 63 63 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12695512,
ECO:0000269|PubMed:291916}.
MOD_RES 66 66 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12695512,
ECO:0000269|PubMed:291916}.
MOD_RES 67 67 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12695512,
ECO:0000269|PubMed:291916}.
MOD_RES 72 72 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12695512,
ECO:0000269|PubMed:291916}.
MOD_RES 73 73 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12695512,
ECO:0000269|PubMed:291916}.
MOD_RES 76 76 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12695512,
ECO:0000269|PubMed:291916}.
MOD_RES 79 79 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12695512,
ECO:0000269|PubMed:291916}.
MOD_RES 82 82 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12695512,
ECO:0000269|PubMed:291916}.
MOD_RES 86 86 4-carboxyglutamate.
{ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12695512,
ECO:0000269|PubMed:291916}.
MOD_RES 110 110 (3R)-3-hydroxyaspartate.
{ECO:0000269|PubMed:6688526}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000250|UniProtKB:P00740}.
MOD_RES 202 202 Sulfotyrosine.
{ECO:0000250|UniProtKB:P00740}.
MOD_RES 205 205 Phosphoserine.
{ECO:0000250|UniProtKB:P00740}.
CARBOHYD 85 85 O-linked (GalNAc...) threonine.
{ECO:0000250|UniProtKB:P00740}.
CARBOHYD 99 99 O-linked (Glc...) serine; alternate.
{ECO:0000269|PubMed:2105311,
ECO:0000269|PubMed:2129367,
ECO:0000269|PubMed:3149637}.
/FTId=CAR_000008.
CARBOHYD 99 99 O-linked (Xyl...) serine; alternate.
{ECO:0000250|UniProtKB:P00740,
ECO:0000269|PubMed:2105311,
ECO:0000269|PubMed:2129367,
ECO:0000269|PubMed:3149637}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:291916}.
CARBOHYD 214 214 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:291916}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:291916}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:291916}.
DISULFID 64 69 {ECO:0000244|PDB:1J34,
ECO:0000244|PDB:1J35,
ECO:0000269|PubMed:12695512}.
DISULFID 97 108 {ECO:0000250|UniProtKB:P00740}.
DISULFID 102 117 {ECO:0000250|UniProtKB:P00740}.
DISULFID 119 128 {ECO:0000250|UniProtKB:P00740}.
DISULFID 134 145 {ECO:0000250|UniProtKB:P00740}.
DISULFID 141 155 {ECO:0000250|UniProtKB:P00740}.
DISULFID 157 170 {ECO:0000250|UniProtKB:P00740}.
DISULFID 178 336 Interchain (between light and heavy
chains). {ECO:0000250|UniProtKB:P00740}.
DISULFID 253 269 {ECO:0000250|UniProtKB:P00740}.
DISULFID 383 397 {ECO:0000250|UniProtKB:P00740}.
DISULFID 408 436 {ECO:0000250|UniProtKB:P00740}.
CONFLICT 110 110 D -> T (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 347 347 L -> S (in Ref. 2; AA sequence).
{ECO:0000305}.
STRAND 50 52 {ECO:0000244|PDB:1J34}.
HELIX 53 55 {ECO:0000244|PDB:1J34}.
HELIX 60 64 {ECO:0000244|PDB:1J34}.
HELIX 71 78 {ECO:0000244|PDB:1J34}.
HELIX 81 91 {ECO:0000244|PDB:1J34}.
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


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