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Protein

Coagulation factor IX

Gene

F9

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 Ca2+ ions, phospholipids, and factor VIIIa.1 Publication

Catalytic activityi

Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Calcium 1; via carbonyl oxygenCombined sources1 Publication
Metal bindingi48 – 481Calcium 2Combined sources1 Publication
Metal bindingi53 – 531Calcium 1; via 4-carboxyglutamateCombined sources1 Publication
Metal bindingi53 – 531Calcium 2; via 4-carboxyglutamateCombined sources1 Publication
Metal bindingi54 – 541Calcium 2; via 4-carboxyglutamateCombined sources1 Publication
Metal bindingi54 – 541Calcium 3; via 4-carboxyglutamateCombined sources1 Publication
Metal bindingi61 – 611Calcium 4 or magnesium 1; via 4-carboxyglutamateCombined sources1 Publication
Metal bindingi63 – 631Calcium 1; via 4-carboxyglutamateCombined sources1 Publication
Metal bindingi63 – 631Calcium 2; via 4-carboxyglutamateCombined sources1 Publication
Metal bindingi63 – 631Calcium 3; via 4-carboxyglutamateCombined sources1 Publication
Metal bindingi66 – 661Calcium 4 or magnesium 1; via 4-carboxyglutamateCombined sources1 Publication
Metal bindingi67 – 671Calcium 1; via 4-carboxyglutamateCombined sources1 Publication
Metal bindingi72 – 721Calcium 5 or magnesium 2; via 4-carboxyglutamateCombined sources1 Publication
Metal bindingi73 – 731Calcium 2; via 4-carboxyglutamateCombined sources1 Publication
Metal bindingi73 – 731Calcium 3; via 4-carboxyglutamateCombined sources1 Publication
Metal bindingi76 – 761Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi76 – 761Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity
Metal bindingi82 – 821Calcium 6 or magnesium 3; via 4-carboxyglutamateCombined sources1 Publication
Metal bindingi86 – 861Calcium 6 or magnesium 3; via 4-carboxyglutamateCombined sources1 Publication
Metal bindingi93 – 931Calcium 7By similarity
Metal bindingi94 – 941Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi96 – 961Calcium 7By similarity
Metal bindingi110 – 1101Calcium 7By similarity
Metal bindingi111 – 1111Calcium 7; via carbonyl oxygenBy similarity
Active sitei268 – 2681Charge relay systemBy similarity
Metal bindingi282 – 2821Calcium 8By similarity
Metal bindingi284 – 2841Calcium 8; via carbonyl oxygenBy similarity
Metal bindingi289 – 2891Calcium 8By similarity
Metal bindingi292 – 2921Calcium 8By similarity
Active sitei316 – 3161Charge relay systemBy similarity
Active sitei412 – 4121Charge relay systemBy similarity

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • endopeptidase activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • serine-type endopeptidase activity Source: GO_Central

GO - Biological processi

  • blood coagulation Source: UniProtKB
  • proteolysis Source: UniProtKB
  • zymogen activation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-BTA-140834. Extrinsic Pathway of Fibrin Clot Formation.
R-BTA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-BTA-159740. Gamma-carboxylation of protein precursors.
R-BTA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-BTA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
SABIO-RKP00741.

Protein family/group databases

MEROPSiS01.214.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor IX (EC:3.4.21.22)
Alternative name(s):
Christmas factor
Cleaved into the following 2 chains:
Gene namesi
Name:F9
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componentsi: Chromosome X, Unassembled WGS sequence

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Keywords - Diseasei

Hemophilia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 462437Coagulation factor IXPRO_0000027741Add
BLAST
Propeptidei29 – 4618By similarityPRO_0000433084Add
BLAST
Chaini47 – 192146Coagulation factor IXa light chainPRO_0000027742Add
BLAST
Propeptidei193 – 22735Activation peptidePRO_0000027743Add
BLAST
Chaini228 – 462235Coagulation factor IXa heavy chainPRO_0000027744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 5314-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications
Modified residuei54 – 5414-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications
Modified residuei61 – 6114-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications
Modified residuei63 – 6314-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications
Disulfide bondi64 ↔ 69Combined sources1 Publication
Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications
Modified residuei67 – 6714-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications
Modified residuei72 – 7214-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications
Modified residuei73 – 7314-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications
Modified residuei76 – 7614-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications
Modified residuei79 – 7914-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications
Modified residuei82 – 8214-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications
Glycosylationi85 – 851O-linked (GalNAc...)By similarity
Modified residuei86 – 8614-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications
Disulfide bondi97 ↔ 108By similarity
Glycosylationi99 – 991O-linked (Glc...); alternateCAR_000008
Glycosylationi99 – 991O-linked (Xyl...); alternateBy similarity
Disulfide bondi102 ↔ 117By similarity
Modified residuei110 – 1101(3R)-3-hydroxyaspartate1 Publication
Modified residuei114 – 1141PhosphoserineBy similarity
Disulfide bondi119 ↔ 128By similarity
Disulfide bondi134 ↔ 145By similarity
Disulfide bondi141 ↔ 155By similarity
Disulfide bondi157 ↔ 170By similarity
Disulfide bondi178 ↔ 336Interchain (between light and heavy chains)By similarity
Modified residuei202 – 2021SulfotyrosineBy similarity
Glycosylationi204 – 2041N-linked (GlcNAc...)1 Publication
Modified residuei205 – 2051PhosphoserineBy similarity
Glycosylationi214 – 2141N-linked (GlcNAc...)1 Publication
Glycosylationi219 – 2191N-linked (GlcNAc...)1 Publication
Disulfide bondi253 ↔ 269By similarity
Glycosylationi307 – 3071N-linked (GlcNAc...)1 Publication
Disulfide bondi383 ↔ 397By similarity
Disulfide bondi408 ↔ 436By similarity

Post-translational modificationi

Activated by factor XIa, which excises the activation peptide. The propeptide can also be removed by snake venom protease.By similarity
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.1 Publication
Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei192 – 1932Cleavage; by factor XIa
Sitei227 – 2282Cleavage; by factor XIa

Keywords - PTMi

Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

PaxDbiP00741.
PRIDEiP00741.

PTM databases

UniCarbKBiP00741.

Miscellaneous databases

PMAP-CutDBP00741.

Expressioni

Tissue specificityi

Detected in blood plasma (at protein level) (PubMed:12695512).1 Publication

Gene expression databases

ExpressionAtlasiP00741. baseline.

Interactioni

Subunit structurei

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).By similarity1 Publication

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005227.

Structurei

Secondary structure

1
462
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi50 – 523Combined sources
Helixi53 – 553Combined sources
Helixi60 – 645Combined sources
Helixi71 – 788Combined sources
Helixi81 – 9111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J34X-ray1.55C47-92[»]
1J35X-ray1.80C47-92[»]
ProteinModelPortaliP00741.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00741.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 9246GlaPROSITE-ProRule annotationAdd
BLAST
Domaini93 – 12937EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini130 – 17142EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini228 – 460233Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Domaini

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, Ca2+ is displaced by Mg2+ 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).By similarity1 Publication

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Signal

Phylogenomic databases

eggNOGiENOG410IGPV. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP00741.
OMAiMKGKYGI.
OrthoDBiEOG75B84T.
TreeFamiTF327329.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00741-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWCLNMIMAE SPGLVTICLL GYLLSAECTV FLDRENATKI LHRPKRYNSG
60 70 80 90 100
KLEEFVRGNL ERECKEEKCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN
110 120 130 140 150
PCLNGGMCKD DINSYECWCQ AGFEGTNCEL DATCSIKNGR CKQFCKRDTD
160 170 180 190 200
NKVVCSCTDG YRLAEDQKSC EPAVPFPCGR VSVSHISKKL TRAETIFSNT
210 220 230 240 250
NYENSSEAEI IWDNVTQSNQ SFDEFSRVVG GEDAERGQFP WQVLLHGEIA
260 270 280 290 300
AFCGGSIVNE KWVVTAAHCI KPGVKITVVA GEHNTEKPEP TEQKRNVIRA
310 320 330 340 350
IPYHSYNASI NKYSHDIALL ELDEPLELNS YVTPICIADR DYTNIFLKFG
360 370 380 390 400
YGYVSGWGKV FNRGRSASIL QYLKVPLVDR ATCLRSTKFS IYSHMFCAGY
410 420 430 440 450
HEGGKDSCQG DSGGPHVTEV EGTSFLTGII SWGEECAMKG KYGIYTKVSR
460
YVNWIKEKTK LT
Length:462
Mass (Da):52,046
Last modified:May 27, 2015 - v2
Checksum:i415B2A7BD6EA256A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101D → T AA sequence (PubMed:291916).Curated
Sequence conflicti347 – 3471L → S AA sequence (PubMed:291916).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DAAA02067809 Genomic DNA. No translation available.
DAAA02067810 Genomic DNA. No translation available.
J00007 mRNA. Translation: AAA30520.1.
PIRiA14757. KFBO.
RefSeqiXP_005227591.1. XM_005227534.3.
UniGeneiBt.13106.

Genome annotation databases

EnsembliENSBTAT00000005227; ENSBTAP00000005227; ENSBTAG00000004003.
GeneIDi280688.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DAAA02067809 Genomic DNA. No translation available.
DAAA02067810 Genomic DNA. No translation available.
J00007 mRNA. Translation: AAA30520.1.
PIRiA14757. KFBO.
RefSeqiXP_005227591.1. XM_005227534.3.
UniGeneiBt.13106.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J34X-ray1.55C47-92[»]
1J35X-ray1.80C47-92[»]
ProteinModelPortaliP00741.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005227.

Protein family/group databases

MEROPSiS01.214.

PTM databases

UniCarbKBiP00741.

Proteomic databases

PaxDbiP00741.
PRIDEiP00741.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000005227; ENSBTAP00000005227; ENSBTAG00000004003.
GeneIDi280688.

Organism-specific databases

CTDi2158.

Phylogenomic databases

eggNOGiENOG410IGPV. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP00741.
OMAiMKGKYGI.
OrthoDBiEOG75B84T.
TreeFamiTF327329.

Enzyme and pathway databases

ReactomeiR-BTA-140834. Extrinsic Pathway of Fibrin Clot Formation.
R-BTA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-BTA-159740. Gamma-carboxylation of protein precursors.
R-BTA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-BTA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
SABIO-RKP00741.

Miscellaneous databases

EvolutionaryTraceiP00741.
PMAP-CutDBP00741.

Gene expression databases

ExpressionAtlasiP00741. baseline.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Hereford.
  2. "Comparison of amino acid sequence of bovine coagulation Factor IX (Christmas factor) with that of other vitamin K-dependent plasma proteins."
    Katayama K., Ericsson L.H., Enfield D.L., Walsh K.A., Neurath H., Davie E.W., Titani K.
    Proc. Natl. Acad. Sci. U.S.A. 76:4990-4994(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, GLYCOSYLATION AT ASN-204; ASN-214; ASN-219 AND ASN-307.
  3. "The role of phospholipid and factor VIIIa in the activation of bovine factor X."
    van Dieijen G., Tans G., Rosing J., Hemker H.C.
    J. Biol. Chem. 256:3433-3442(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  4. "The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens."
    McMullen B.A., Fujikawa K., Kisiel W.
    Biochem. Biophys. Res. Commun. 115:8-14(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: HYDROXYLATION AT ASP-110.
  5. "Molecular cloning of the gene for human anti-haemophilic factor IX."
    Choo K.H., Gould K.G., Rees D.J.G., Brownlee G.G.
    Nature 299:178-180(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 97-157.
  6. "A new trisaccharide sugar chain linked to a serine residue in bovine blood coagulation factors VII and IX."
    Hase S., Kawabata S., Nishimura H., Takeya H., Sueyoshi T., Miyata T., Iwanaga S., Takao T., Shimonishi Y., Ikenaka T.
    J. Biochem. 104:867-868(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF CARBOHYDRATE ON SER-99.
  7. "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."
    Iwanaga S., Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T.
    Adv. Exp. Med. Biol. 281:121-131(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF CARBOHYDRATE ON SER-99.
  8. "The structure of (xylose)2glucose-O-serine 53 found in the first epidermal growth factor-like domain of bovine blood clotting factor IX."
    Hase S., Nishimura H., Kawabata S., Iwanaga S., Ikenaka T.
    J. Biol. Chem. 265:1858-1861(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF CARBOHYDRATE ON SER-99.
  9. "Crystal structure of Mg2+- and Ca2+-bound Gla domain of factor IX complexed with binding protein."
    Shikamoto Y., Morita T., Fujimoto Z., Mizuno H.
    J. Biol. Chem. 278:24090-24094(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, TISSUE SPECIFICITY.

Entry informationi

Entry nameiFA9_BOVIN
AccessioniPrimary (citable) accession number: P00741
Secondary accession number(s): F1MFL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 27, 2015
Last modified: April 13, 2016
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.