GenomeNet

Database: UniProt
Entry: P00741
LinkDB: P00741
Original site: P00741 
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   10-APR-2019, entry version 191.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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.,
RA   Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S.,
RA   Marcais G., 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;
RP   GLU-54; GLU-61; GLU-63; GLU-66; GLU-67; GLU-72; GLU-73; GLU-76;
RP   GLU-79; GLU-82 AND GLU-86, AND GLYCOSYLATION AT ASN-204; ASN-214;
RP   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;
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-
RT   dependent 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;
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
RT   blood 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;
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
RT   first 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;
RA   Hase S., Nishimura H., Kawabata S., Iwanaga S., Ikenaka T.;
RT   "The structure of (xylose)2glucose-O-serine 53 found in the first
RT   epidermal growth factor-like domain of bovine blood clotting factor
RT   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
RP   VENOM COAGULATION FACTOR IX-BINDING PROTEIN; CALCIUM AND MAGNESIUM,
RP   GAMMA-CARBOXYGLUTAMATION AT GLU-53; GLU-54; GLU-61; GLU-63; GLU-66;
RP   GLU-67; GLU-72; GLU-73; GLU-76; GLU-79; GLU-82 AND GLU-86,
RP   METAL-BINDING SITES, DISULFIDE BOND, DOMAIN, SUBCELLULAR LOCATION, AND
RP   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+)
CC       ions, phospholipids, and factor VIIIa.
CC       {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;
CC       disulfide-linked, Interacts with SERPINC1 (By similarity).
CC       Interacts with the heterodimeric snake venom coagulation factor
CC       IX-binding protein (PubMed:12695512).
CC       {ECO:0000250|UniProtKB:P00740, 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)
CC       residues in the Gla domain (PubMed:12695512). Calcium can also
CC       bind, with stronger affinity, to another site beyond the Gla
CC       domain (By similarity). Under physiological ion concentrations,
CC       Ca(2+) is displaced by Mg(2+) from some of the gammaglutamate
CC       residues in the N-terminal Gla domain. This leads to a subtle
CC       conformation change that may affect the interaction with its
CC       binding protein (PubMed:12695512). {ECO:0000250|UniProtKB:P00740,
CC       ECO:0000269|PubMed:12695512}.
CC   -!- PTM: Activated by factor XIa, which excises the activation
CC       peptide. The propeptide can also be removed by snake venom
CC       protease. {ECO:0000250|UniProtKB:P00740}.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate 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.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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   UniGene; Bt.13106; -.
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   ProteinModelPortal; P00741; -.
DR   SMR; P00741; -.
DR   STRING; 9913.ENSBTAP00000005227; -.
DR   MEROPS; S01.214; -.
DR   GlyConnect; 97; -.
DR   iPTMnet; P00741; -.
DR   UniCarbKB; P00741; -.
DR   PaxDb; P00741; -.
DR   PRIDE; P00741; -.
DR   VGNC; VGNC:28691; F9.
DR   eggNOG; ENOG410IGPV; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000251821; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; P00741; -.
DR   OMA; SYECWCQ; -.
DR   OrthoDB; 1314811at2759; -.
DR   TreeFam; TF327329; -.
DR   Reactome; R-BTA-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-BTA-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-BTA-159740; Gamma-carboxylation of protein precursors.
DR   Reactome; R-BTA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR   Reactome; R-BTA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR   SABIO-RK; P00741; -.
DR   EvolutionaryTrace; P00741; -.
DR   PMAP-CutDB; P00741; -.
DR   Proteomes; UP000009136; Unplaced.
DR   Bgee; ENSBTAG00000004003; Expressed in 2 organ(s), highest expression level in liver.
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:InterPro.
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; 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; IPR013032; EGF-like_CS.
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; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR44064:SF4; PTHR44064:SF4; 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; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hemophilia; Hemostasis;
KW   Hydrolase; Hydroxylation; Magnesium; Metal-binding; Phosphoprotein;
KW   Protease; Reference proteome; Secreted; Serine protease; Signal;
KW   Sulfation; Zymogen.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   CHAIN        26    462       Coagulation factor IX.
FT                                /FTId=PRO_0000027741.
FT   PROPEP       29     46       {ECO:0000250|UniProtKB:P00740}.
FT                                /FTId=PRO_0000433084.
FT   CHAIN        47    192       Coagulation factor IXa light chain.
FT                                /FTId=PRO_0000027742.
FT   PROPEP      193    227       Activation peptide.
FT                                /FTId=PRO_0000027743.
FT   CHAIN       228    462       Coagulation factor IXa heavy chain.
FT                                /FTId=PRO_0000027744.
FT   DOMAIN       47     92       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       93    129       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      130    171       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      228    460       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    268    268       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   ACT_SITE    316    316       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   ACT_SITE    412    412       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        47     47       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        48     48       Calcium 2. {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        53     53       Calcium 1; via 4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        53     53       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        54     54       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        54     54       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        61     61       Calcium 4 or magnesium 1; via 4-
FT                                carboxyglutamate. {ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        63     63       Calcium 1; via 4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        63     63       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        63     63       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        66     66       Calcium 4 or magnesium 1; via 4-
FT                                carboxyglutamate. {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        67     67       Calcium 1; via 4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        72     72       Calcium 5 or magnesium 2; via 4-
FT                                carboxyglutamate. {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        73     73       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        73     73       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        76     76       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        76     76       Calcium 5 or magnesium 2; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        82     82       Calcium 6 or magnesium 3; via 4-
FT                                carboxyglutamate. {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        86     86       Calcium 6 or magnesium 3; via 4-
FT                                carboxyglutamate. {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   METAL        93     93       Calcium 7.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        94     94       Calcium 7; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        96     96       Calcium 7.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       110    110       Calcium 7.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       111    111       Calcium 7; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       282    282       Calcium 8.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       284    284       Calcium 8; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       289    289       Calcium 8.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       292    292       Calcium 8.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   SITE        192    193       Cleavage; by factor XIa.
FT   SITE        227    228       Cleavage; by factor XIa.
FT   MOD_RES      53     53       4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12695512,
FT                                ECO:0000269|PubMed:291916}.
FT   MOD_RES      54     54       4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12695512,
FT                                ECO:0000269|PubMed:291916}.
FT   MOD_RES      61     61       4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12695512,
FT                                ECO:0000269|PubMed:291916}.
FT   MOD_RES      63     63       4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12695512,
FT                                ECO:0000269|PubMed:291916}.
FT   MOD_RES      66     66       4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12695512,
FT                                ECO:0000269|PubMed:291916}.
FT   MOD_RES      67     67       4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12695512,
FT                                ECO:0000269|PubMed:291916}.
FT   MOD_RES      72     72       4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12695512,
FT                                ECO:0000269|PubMed:291916}.
FT   MOD_RES      73     73       4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12695512,
FT                                ECO:0000269|PubMed:291916}.
FT   MOD_RES      76     76       4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12695512,
FT                                ECO:0000269|PubMed:291916}.
FT   MOD_RES      79     79       4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12695512,
FT                                ECO:0000269|PubMed:291916}.
FT   MOD_RES      82     82       4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12695512,
FT                                ECO:0000269|PubMed:291916}.
FT   MOD_RES      86     86       4-carboxyglutamate.
FT                                {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12695512,
FT                                ECO:0000269|PubMed:291916}.
FT   MOD_RES     110    110       (3R)-3-hydroxyaspartate.
FT                                {ECO:0000269|PubMed:6688526}.
FT   MOD_RES     114    114       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     202    202       Sulfotyrosine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     205    205       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD     85     85       O-linked (GalNAc...) threonine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD     99     99       O-linked (Glc...) serine; alternate.
FT                                {ECO:0000269|PubMed:2105311,
FT                                ECO:0000269|PubMed:2129367,
FT                                ECO:0000269|PubMed:3149637}.
FT                                /FTId=CAR_000008.
FT   CARBOHYD     99     99       O-linked (Xyl...) serine; alternate.
FT                                {ECO:0000250|UniProtKB:P00740,
FT                                ECO:0000269|PubMed:2105311,
FT                                ECO:0000269|PubMed:2129367,
FT                                ECO:0000269|PubMed:3149637}.
FT   CARBOHYD    204    204       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:291916}.
FT   CARBOHYD    214    214       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:291916}.
FT   CARBOHYD    219    219       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:291916}.
FT   CARBOHYD    307    307       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:291916}.
FT   DISULFID     64     69       {ECO:0000244|PDB:1J34,
FT                                ECO:0000244|PDB:1J35,
FT                                ECO:0000269|PubMed:12695512}.
FT   DISULFID     97    108       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    102    117       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    119    128       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    134    145       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    141    155       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    157    170       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    178    336       Interchain (between light and heavy
FT                                chains). {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    253    269       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    383    397       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    408    436       {ECO:0000250|UniProtKB:P00740}.
FT   CONFLICT    110    110       D -> T (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    347    347       L -> S (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   STRAND       50     52       {ECO:0000244|PDB:1J34}.
FT   HELIX        53     55       {ECO:0000244|PDB:1J34}.
FT   HELIX        60     64       {ECO:0000244|PDB:1J34}.
FT   HELIX        71     78       {ECO:0000244|PDB:1J34}.
FT   HELIX        81     91       {ECO:0000244|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
//
DBGET integrated database retrieval system