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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)DescriptionActionsGraphical viewLength
Metal bindingi47Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi48Calcium 2Combined sources1 Publication1
Metal bindingi53Calcium 1; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi53Calcium 2; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi54Calcium 2; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi54Calcium 3; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi61Calcium 4 or magnesium 1; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi63Calcium 1; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi63Calcium 2; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi63Calcium 3; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi66Calcium 4 or magnesium 1; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi67Calcium 1; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi72Calcium 5 or magnesium 2; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi73Calcium 2; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi73Calcium 3; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi76Calcium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi76Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi82Calcium 6 or magnesium 3; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi86Calcium 6 or magnesium 3; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi93Calcium 7By similarity1
Metal bindingi94Calcium 7; via carbonyl oxygenBy similarity1
Metal bindingi96Calcium 7By similarity1
Metal bindingi110Calcium 7By similarity1
Metal bindingi111Calcium 7; via carbonyl oxygenBy similarity1
Active sitei268Charge relay systemBy similarity1
Metal bindingi282Calcium 8By similarity1
Metal bindingi284Calcium 8; via carbonyl oxygenBy similarity1
Metal bindingi289Calcium 8By similarity1
Metal bindingi292Calcium 8By similarity1
Active sitei316Charge relay systemBy similarity1
Active sitei412Charge relay systemBy similarity1

GO - Molecular functioni

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

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000002774126 – 462Coagulation factor IXAdd BLAST437
PropeptideiPRO_000043308429 – 46By similarityAdd BLAST18
ChainiPRO_000002774247 – 192Coagulation factor IXa light chainAdd BLAST146
PropeptideiPRO_0000027743193 – 227Activation peptideAdd BLAST35
ChainiPRO_0000027744228 – 462Coagulation factor IXa heavy chainAdd BLAST235

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei534-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei544-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei614-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei634-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Disulfide bondi64 ↔ 69Combined sources1 Publication
Modified residuei664-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei674-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei734-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei764-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei794-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei824-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Glycosylationi85O-linked (GalNAc...)By similarity1
Modified residuei864-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Disulfide bondi97 ↔ 108By similarity
GlycosylationiCAR_00000899O-linked (Glc...); alternate1
Glycosylationi99O-linked (Xyl...); alternateBy similarity1
Disulfide bondi102 ↔ 117By similarity
Modified residuei110(3R)-3-hydroxyaspartate1 Publication1
Modified residuei114PhosphoserineBy similarity1
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 residuei202SulfotyrosineBy similarity1
Glycosylationi204N-linked (GlcNAc...)1 Publication1
Modified residuei205PhosphoserineBy similarity1
Glycosylationi214N-linked (GlcNAc...)1 Publication1
Glycosylationi219N-linked (GlcNAc...)1 Publication1
Disulfide bondi253 ↔ 269By similarity
Glycosylationi307N-linked (GlcNAc...)1 Publication1
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)DescriptionActionsGraphical viewLength
Sitei192 – 193Cleavage; by factor XIa2
Sitei227 – 228Cleavage; by factor XIa2

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

BgeeiENSBTAG00000004003.
ExpressionAtlasiP00741. differential.

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

1462
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi50 – 52Combined sources3
Helixi53 – 55Combined sources3
Helixi60 – 64Combined sources5
Helixi71 – 78Combined sources8
Helixi81 – 91Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J34X-ray1.55C47-92[»]
1J35X-ray1.80C47-92[»]
ProteinModelPortaliP00741.
SMRiP00741.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00741.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini47 – 92GlaPROSITE-ProRule annotationAdd BLAST46
Domaini93 – 129EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini130 – 171EGF-like 2PROSITE-ProRule annotationAdd BLAST42
Domaini228 – 460Peptidase S1PROSITE-ProRule annotationAdd BLAST233

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.
OrthoDBiEOG091G0AH5.
TreeFamiTF327329.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti110D → T AA sequence (PubMed:291916).Curated1
Sequence conflicti347L → S AA sequence (PubMed:291916).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J34X-ray1.55C47-92[»]
1J35X-ray1.80C47-92[»]
ProteinModelPortaliP00741.
SMRiP00741.
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.
OrthoDBiEOG091G0AH5.
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

BgeeiENSBTAG00000004003.
ExpressionAtlasiP00741. differential.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
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...

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: November 30, 2016
This is version 171 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.