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Protein

Coagulation factor IX

Gene

F9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at transcript 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.By similarity

Catalytic activityi

Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi47Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi48Calcium 2By similarity1
Metal bindingi53Calcium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi53Calcium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi54Calcium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi54Calcium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi61Calcium 4 or magnesium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi63Calcium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi63Calcium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi63Calcium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi66Calcium 4 or magnesium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi67Calcium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi72Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi73Calcium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi73Calcium 3; via 4-carboxyglutamateBy similarity1
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-carboxyglutamateBy similarity1
Metal bindingi86Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity1
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 sitei277Charge relay systemBy similarity1
Metal bindingi291Calcium 8By similarity1
Metal bindingi293Calcium 8; via carbonyl oxygenBy similarity1
Metal bindingi298Calcium 8By similarity1
Metal bindingi301Calcium 8By similarity1
Active sitei325Charge relay systemBy similarity1
Active sitei421Charge relay systemBy similarity1

GO - Molecular functioni

GO - Biological processi

  • blood coagulation Source: MGI
  • proteolysis Source: MGI
  • zymogen activation Source: UniProtKB

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processBlood coagulation, Hemostasis
LigandCalcium, Magnesium, Metal-binding

Enzyme and pathway databases

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

Protein family/group databases

MEROPSiS01.214

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor IX (EC:3.4.21.22By similarity)
Alternative name(s):
Christmas factor
Cleaved into the following 2 chains:
Gene namesi
Name:F9
Synonyms:Cf9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:88384 F9

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
PropeptideiPRO_000002776029 – 46By similarityAdd BLAST18
ChainiPRO_000002776147 – 471Coagulation factor IXAdd BLAST425
ChainiPRO_000002776247 – 192Coagulation factor IXa light chainAdd BLAST146
PropeptideiPRO_0000027763193 – 236Activation peptideBy similarityAdd BLAST44
ChainiPRO_0000027764237 – 471Coagulation factor IXa heavy chainAdd BLAST235

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei534-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei544-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei614-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei634-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi64 ↔ 69By similarity
Modified residuei664-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei674-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei734-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei764-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei794-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei824-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Glycosylationi85O-linked (GalNAc...) threonineBy similarity1
Modified residuei864-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi97 ↔ 108By similarity
Glycosylationi99O-linked (Glc...) serine; alternateBy similarity1
Glycosylationi99O-linked (Xyl...) serine; alternateBy similarity1
Disulfide bondi102 ↔ 117By similarity
Modified residuei110(3R)-3-hydroxyaspartateBy similarity1
Modified residuei114PhosphoserineBy similarity1
Disulfide bondi119 ↔ 128By similarity
Disulfide bondi134 ↔ 145By similarity
Disulfide bondi141 ↔ 155By similarity
Disulfide bondi157 ↔ 170By similarity
Disulfide bondi178 ↔ 345Interchain (between light and heavy chains)By similarity
Modified residuei202SulfotyrosineBy similarity1
Glycosylationi204N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei205PhosphoserineBy similarity1
Modified residuei206Phosphothreonine; alternateBy similarity1
Glycosylationi206O-linked (GalNAc...) threonine; alternateBy similarity1
Glycosylationi223N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi225O-linked (GalNAc...) threonineBy similarity1
Glycosylationi235O-linked (GalNAc...) threonineBy similarity1
Disulfide bondi262 ↔ 278By similarity
Disulfide bondi392 ↔ 406By similarity
Disulfide bondi417 ↔ 445By 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.By similarity
Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei192 – 193Cleavage; by factor XIaBy similarity2
Sitei236 – 237Cleavage; by factor XIaBy similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

MaxQBiP16294
PaxDbiP16294
PRIDEiP16294
TopDownProteomicsiP16294

PTM databases

iPTMnetiP16294
PhosphoSitePlusiP16294

Expressioni

Tissue specificityi

Detected in liver.1 Publication

Gene expression databases

BgeeiENSMUSG00000031138 Expressed in 26 organ(s), highest expression level in liver
CleanExiMM_F9
GenevisibleiP16294 MM

Interactioni

Subunit structurei

Heterodimer of a light chain and a heavy chain; disulfide-linked. Interacts with SERPINC1.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033477

Structurei

3D structure databases

ProteinModelPortaliP16294
ModBaseiSearch...
MobiDBiSearch...

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
Domaini237 – 469Peptidase S1PROSITE-ProRule annotationAdd BLAST233

Domaini

Calcium binds to the gamma-carboxyglutamic acid (Gla) residues in the Gla domain. Calcium can also bind, with stronger affinity, to another site beyond the Gla domain. 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.By similarity

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IGPV Eukaryota
COG5640 LUCA
GeneTreeiENSGT00760000118890
HOGENOMiHOG000251821
HOVERGENiHBG013304
InParanoidiP16294
KOiK01321
OMAiSYECWCQ
OrthoDBiEOG091G0AH5
PhylomeDBiP16294
TreeFamiTF327329

Family and domain databases

CDDicd00190 Tryp_SPc, 1 hit
Gene3Di4.10.740.10, 1 hit
InterProiView protein in InterPro
IPR017857 Coagulation_fac-like_Gla_dom
IPR035694 Coagulation_factor_IX
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
IPR035972 GLA-like_dom_SF
IPR000294 GLA_domain
IPR012224 Pept_S1A_FX
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PANTHERiPTHR44064:SF4 PTHR44064:SF4, 1 hit
PfamiView protein in Pfam
PF00008 EGF, 1 hit
PF00594 Gla, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001143 Factor_X, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
PR00001 GLABLOOD
SMARTiView protein in SMART
SM00181 EGF, 2 hits
SM00179 EGF_CA, 1 hit
SM00069 GLA, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF57630 SSF57630, 1 hit
PROSITEiView protein in PROSITE
PS00010 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

Sequencei

Sequence statusi: Complete.

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

P16294-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKHLNTVMAE SPALITIFLL GYLLSTECAV FLDRENATKI LTRPKRYNSG
60 70 80 90 100
KLEEFVRGNL ERECIEERCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN
110 120 130 140 150
PCLNGGICKD DISSYECWCQ VGFEGRNCEL DATCNIKNGR CKQFCKNSPD
160 170 180 190 200
NKVICSCTEG YQLAEDQKSC EPTVPFPCGR ASISYSSKKI TRAETVFSNM
210 220 230 240 250
DYENSTEAVF IQDDITDGAI LNNVTESSES LNDFTRVVGG ENAKPGQIPW
260 270 280 290 300
QVILNGEIEA FCGGAIINEK WIVTAAHCLK PGDKIEVVAG EYNIDKKEDT
310 320 330 340 350
EQRRNVIRTI PHHQYNATIN KYSHDIALLE LDKPLILNSY VTPICVANRE
360 370 380 390 400
YTNIFLKFGS GYVSGWGKVF NKGRQASILQ YLRVPLVDRA TCLRSTTFTI
410 420 430 440 450
YNNMFCAGYR EGGKDSCEGD SGGPHVTEVE GTSFLTGIIS WGEECAMKGK
460 470
YGIYTKVSRY VNWIKEKTKL T
Length:471
Mass (Da):52,978
Last modified:January 9, 2007 - v3
Checksum:i05E08E86622397E2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti375Q → H in AAA37629 (PubMed:2323576).Curated1
Sequence conflicti400I → T in AAA37629 (PubMed:2323576).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK149372 mRNA Translation: BAE28840.1
M23109 mRNA Translation: AAA37629.1
M26236 mRNA Translation: AAA37630.1
CCDSiCCDS30158.1
PIRiJQ0419
RefSeqiNP_001292726.1, NM_001305797.1
NP_032005.1, NM_007979.2
UniGeneiMm.391283

Genome annotation databases

EnsembliENSMUST00000033477; ENSMUSP00000033477; ENSMUSG00000031138
GeneIDi14071
KEGGimmu:14071
UCSCiuc009thw.2 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK149372 mRNA Translation: BAE28840.1
M23109 mRNA Translation: AAA37629.1
M26236 mRNA Translation: AAA37630.1
CCDSiCCDS30158.1
PIRiJQ0419
RefSeqiNP_001292726.1, NM_001305797.1
NP_032005.1, NM_007979.2
UniGeneiMm.391283

3D structure databases

ProteinModelPortaliP16294
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033477

Protein family/group databases

MEROPSiS01.214

PTM databases

iPTMnetiP16294
PhosphoSitePlusiP16294

Proteomic databases

MaxQBiP16294
PaxDbiP16294
PRIDEiP16294
TopDownProteomicsiP16294

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033477; ENSMUSP00000033477; ENSMUSG00000031138
GeneIDi14071
KEGGimmu:14071
UCSCiuc009thw.2 mouse

Organism-specific databases

CTDi2158
MGIiMGI:88384 F9

Phylogenomic databases

eggNOGiENOG410IGPV Eukaryota
COG5640 LUCA
GeneTreeiENSGT00760000118890
HOGENOMiHOG000251821
HOVERGENiHBG013304
InParanoidiP16294
KOiK01321
OMAiSYECWCQ
OrthoDBiEOG091G0AH5
PhylomeDBiP16294
TreeFamiTF327329

Enzyme and pathway databases

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

Miscellaneous databases

PROiPR:P16294
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031138 Expressed in 26 organ(s), highest expression level in liver
CleanExiMM_F9
GenevisibleiP16294 MM

Family and domain databases

CDDicd00190 Tryp_SPc, 1 hit
Gene3Di4.10.740.10, 1 hit
InterProiView protein in InterPro
IPR017857 Coagulation_fac-like_Gla_dom
IPR035694 Coagulation_factor_IX
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
IPR035972 GLA-like_dom_SF
IPR000294 GLA_domain
IPR012224 Pept_S1A_FX
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PANTHERiPTHR44064:SF4 PTHR44064:SF4, 1 hit
PfamiView protein in Pfam
PF00008 EGF, 1 hit
PF00594 Gla, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001143 Factor_X, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
PR00001 GLABLOOD
SMARTiView protein in SMART
SM00181 EGF, 2 hits
SM00179 EGF_CA, 1 hit
SM00069 GLA, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF57630 SSF57630, 1 hit
PROSITEiView protein in PROSITE
PS00010 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
ProtoNetiSearch...

Entry informationi

Entry nameiFA9_MOUSE
AccessioniPrimary (citable) accession number: P16294
Secondary accession number(s): Q3UES1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 9, 2007
Last modified: November 7, 2018
This is version 195 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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