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Protein

Coagulation factor IX

Gene

F9

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 bindingi40Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi41Calcium 2By similarity1
Metal bindingi46Calcium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi46Calcium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi47Calcium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi47Calcium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi54Calcium 4 or magnesium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi56Calcium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi56Calcium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi56Calcium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi59Calcium 4 or magnesium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi60Calcium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi65Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi66Calcium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi66Calcium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi69Calcium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi69Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi69Calcium 5; via 4-carboxyglutamateBy similarity1
Metal bindingi75Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi79Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi86Calcium 7By similarity1
Metal bindingi87Calcium 7; via carbonyl oxygenBy similarity1
Metal bindingi89Calcium 7By similarity1
Metal bindingi103Calcium 7By similarity1
Metal bindingi104Calcium 7; via carbonyl oxygenBy similarity1
Active sitei268Charge relay systemBy similarity1
Metal bindingi282Calcium 8By similarity1
Metal bindingi284Calcium 8; via carbonyl oxygenBy similarity1
Metal bindingi287Calcium 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

GO - Biological processi

  • blood coagulation Source: RGD
  • 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-RNO-140834. Extrinsic Pathway of Fibrin Clot Formation.
R-RNO-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-RNO-159740. Gamma-carboxylation of protein precursors.
R-RNO-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-RNO-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome X

Organism-specific databases

RGDi2589. F9.

Subcellular locationi

  • Secreted By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
PropeptideiPRO_000043311122 – 39By similarityAdd BLAST18
ChainiPRO_000008868540 – 462Coagulation factor IXAdd BLAST423
ChainiPRO_000043311240 – 185Coagulation factor IXa light chainAdd BLAST146
PropeptideiPRO_0000433113186 – 227Activation peptideBy similarityAdd BLAST42
ChainiPRO_0000433114228 – 462Coagulation factor IXa heavy chainAdd BLAST235

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei464-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei474-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei544-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei564-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi57 ↔ 62By similarity
Modified residuei594-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei604-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei654-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei664-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei694-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei754-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Glycosylationi78O-linked (GalNAc...)By similarity1
Modified residuei794-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi90 ↔ 101By similarity
Glycosylationi92O-linked (Glc...); alternateBy similarity1
Glycosylationi92O-linked (Xyl...); alternateBy similarity1
Disulfide bondi95 ↔ 110By similarity
Modified residuei103(3R)-3-hydroxyaspartateBy similarity1
Modified residuei107PhosphoserineBy similarity1
Disulfide bondi112 ↔ 121By similarity
Disulfide bondi127 ↔ 138By similarity
Disulfide bondi134 ↔ 148By similarity
Disulfide bondi150 ↔ 163By similarity
Disulfide bondi171 ↔ 336Interchain (between light and heavy chains)By similarity
Modified residuei195SulfotyrosineBy similarity1
Modified residuei198PhosphoserineBy similarity1
Modified residuei199Phosphothreonine; alternateBy similarity1
Glycosylationi199O-linked (GalNAc...); alternateBy similarity1
Glycosylationi208N-linked (GlcNAc...)Sequence analysis1
Glycosylationi214N-linked (GlcNAc...)Sequence analysis1
Glycosylationi216O-linked (GalNAc...)By similarity1
Glycosylationi226O-linked (GalNAc...)By similarity1
Disulfide bondi253 ↔ 269By similarity
Glycosylationi307N-linked (GlcNAc...)Sequence analysis1
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.By similarity
Predominantly O-glucosylated at Ser-92 by POGLUT1 in vitro.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei185 – 186Cleavage; by factor XIaBy similarity2
Sitei227 – 228Cleavage; by factor XIaBy similarity2

Keywords - PTMi

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

Proteomic databases

PaxDbiP16296.
PeptideAtlasiP16296.
PRIDEiP16296.

Expressioni

Gene expression databases

BgeeiENSRNOG00000003430.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004559.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 86GlaPROSITE-ProRule annotationAdd BLAST47
Domaini86 – 122EGF-like; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini228 – 460Peptidase 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
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.
HOVERGENiHBG013304.
InParanoidiP16296.
KOiK01321.
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.

P16296-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADAPGLIPI FLLGYLLSTE CAVFLDRENA TKILTRPKRY NSGKLEEFVQ
60 70 80 90 100
GNLERECIEE RCSFEEAREV FENTEKTTEF WKQYVDGDQC ESNPCLNGGI
110 120 130 140 150
CKDDINSYEC WCQAGFEGRN CELDATCSIK NGRCKQFCKN SPDNKIICSC
160 170 180 190 200
TEGYQLAEDQ KSCEPAVPFP CGRVSVAYNS KKITRAETVF SNTDYGNSTE
210 220 230 240 250
LILDDITNST ILDNLTENSE PINDFTRVVG GENAKPGQIP WQVILNGEIE
260 270 280 290 300
AFCGGAIINE KWIVTAAHCL KPGDKIEVVA GEHNIDEKED TEQRRNVIRT
310 320 330 340 350
IPHHQYNATI NKYSHDIALL ELDKPLILNS YVTPICVANK EYTNIFLKFG
360 370 380 390 400
SGYVSGWGKV FNKGRQASIL QYLRVPLVDR ATCLRSTKFS IYNNMFCAGY
410 420 430 440 450
REGGKDSCEG DSGGPHVTEV EGTSFLTGII SWGEECAMKG KYGIYTKVSR
460
YVNWIKEKTK LT
Length:462
Mass (Da):51,808
Last modified:May 27, 2015 - v2
Checksum:i6C50A44A8F0945EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06108743 Genomic DNA. No translation available.
AABR06108744 Genomic DNA. No translation available.
AABR06108745 Genomic DNA. No translation available.
AABR06108746 Genomic DNA. No translation available.
CH474019 Genomic DNA. Translation: EDL86171.1.
M26247 mRNA. Translation: AAA41162.1.
PIRiI84621.
RefSeqiNP_113728.1. NM_031540.1.
UniGeneiRn.37599.

Genome annotation databases

EnsembliENSRNOT00000004559; ENSRNOP00000004559; ENSRNOG00000003430.
GeneIDi24946.
KEGGirno:24946.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06108743 Genomic DNA. No translation available.
AABR06108744 Genomic DNA. No translation available.
AABR06108745 Genomic DNA. No translation available.
AABR06108746 Genomic DNA. No translation available.
CH474019 Genomic DNA. Translation: EDL86171.1.
M26247 mRNA. Translation: AAA41162.1.
PIRiI84621.
RefSeqiNP_113728.1. NM_031540.1.
UniGeneiRn.37599.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004559.

Protein family/group databases

MEROPSiS01.214.

Proteomic databases

PaxDbiP16296.
PeptideAtlasiP16296.
PRIDEiP16296.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000004559; ENSRNOP00000004559; ENSRNOG00000003430.
GeneIDi24946.
KEGGirno:24946.

Organism-specific databases

CTDi2158.
RGDi2589. F9.

Phylogenomic databases

eggNOGiENOG410IGPV. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOVERGENiHBG013304.
InParanoidiP16296.
KOiK01321.
OMAiMKGKYGI.
OrthoDBiEOG091G0AH5.
TreeFamiTF327329.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP16296.

Gene expression databases

BgeeiENSRNOG00000003430.

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_RAT
AccessioniPrimary (citable) accession number: P16296
Secondary accession number(s): F1M1M6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: May 27, 2015
Last modified: September 7, 2016
This is version 127 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

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.