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Protein

Coagulation factor IX

Gene

F9

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: -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.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 bindingi1Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi2Calcium 2By similarity1
Metal bindingi7Calcium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi7Calcium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi8Calcium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi8Calcium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi16Calcium 4 or magnesium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi18Calcium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi18Calcium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi18Calcium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi21Calcium 4 or magnesium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi22Calcium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi27Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi28Calcium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi28Calcium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi31Calcium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi31Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi37Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi41Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi48Calcium 7By similarity1
Metal bindingi49Calcium 7; via carbonyl oxygenBy similarity1
Metal bindingi51Calcium 7By similarity1
Metal bindingi65Calcium 7By similarity1
Metal bindingi66Calcium 7; via carbonyl oxygenBy similarity1
Active sitei223Charge relay systemBy similarity1
Metal bindingi237Calcium 8By similarity1
Metal bindingi239Calcium 8; via carbonyl oxygenBy similarity1
Metal bindingi242Calcium 8; via carbonyl oxygenBy similarity1
Metal bindingi244Calcium 8By similarity1
Metal bindingi247Calcium 8By similarity1
Active sitei271Charge relay systemBy similarity1
Active sitei367Charge relay systemBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

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
ChainiPRO_00000277701 – 409Coagulation factor IXAdd BLAST409
ChainiPRO_00000277711 – 147Coagulation factor IXa light chainAdd BLAST147
PropeptideiPRO_0000027772148 – 182Activation peptideBy similarityAdd BLAST35
ChainiPRO_0000027773183 – 409Coagulation factor IXa heavy chainAdd BLAST227

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei74-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei84-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei164-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei184-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi19 ↔ 241 Publication
Modified residuei214-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei224-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei274-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei284-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei314-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei344-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei374-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei414-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi52 ↔ 631 Publication
Disulfide bondi57 ↔ 721 Publication
Modified residuei65(3R)-3-hydroxyaspartateBy similarity1
Modified residuei69PhosphoserineBy similarity1
Disulfide bondi74 ↔ 831 Publication
Disulfide bondi89 ↔ 1001 Publication
Disulfide bondi96 ↔ 1101 Publication
Disulfide bondi112 ↔ 1251 Publication
Disulfide bondi133 ↔ 291Interchain (between light and heavy chains)1 Publication
Modified residuei157SulfotyrosineBy similarity1
Modified residuei160PhosphoserineBy similarity1
Modified residuei161Phosphothreonine; alternateBy similarity1
Glycosylationi161O-linked (GalNAc...) threonine; alternateBy similarity1
Glycosylationi171O-linked (GalNAc...) threonineBy similarity1
Glycosylationi174N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi208 ↔ 2241 Publication
Glycosylationi262N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi338 ↔ 3521 Publication
Disulfide bondi363 ↔ 3911 Publication

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei147 – 148Cleavage; by factor XIaBy similarity2
Sitei182 – 183Cleavage; by factor XIaBy similarity2

Keywords - PTMi

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

Proteomic databases

PeptideAtlasiP16293
PRIDEiP16293

Interactioni

Subunit structurei

Heterodimer of a light chain and a heavy chain; disulfide-linked. Interacts with SERPINC1.1 Publication

Structurei

Secondary structure

1409
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP16293
SMRiP16293
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16293

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 47GlaPROSITE-ProRule annotationAdd BLAST47
Domaini48 – 84EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini85 – 126EGF-like 2PROSITE-ProRule annotationAdd BLAST42
Domaini183 – 409Peptidase S1PROSITE-ProRule annotationAdd BLAST227

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

Phylogenomic databases

HOVERGENiHBG013304
InParanoidiP16293

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

Sequence (1+)i

Sequence statusi: Fragment.

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

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.iShow all

P16293-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
YNSGKLEESF VRGNLERECI EEKCSFEEAR EVFENTEKTN EFWKQYVDGD
60 70 80 90 100
QCEPNPCLNG GLCKDDINSY ECWCQVGFEG KNCELDATCN IKNGRCKQFC
110 120 130 140 150
KTGADSKVLC SCTTGYRLAP DQKSCKPAVP FPCGRVSVSH SPTTLTRAEI
160 170 180 190 200
IFSNMDYENS TEVEPILDSL TESNQSSDDF IRIVGGENAK PGQFPWQVLL
210 220 230 240 250
NGKIDAFCGG SIINEKWVVT AAHCIEPGVK ITVVAGEYNT EETEPTEQRR
260 270 280 290 300
NVIRAIPHHS YNATVNKYSH DIALLELDEP LTLNSYVTPI CIADKEYTNI
310 320 330 340 350
FLKFGSGYVS GWGRVFNRGR SATILQYLKV PLVDRATCLR STKVTIYSNM
360 370 380 390 400
FCAGFHEGGK DSCLGDSGGP HVTEVEGTSF LTGIISWGEE CAVKGKYGIY

TKVSRYVNW
Length:409
Mass (Da):45,516
Last modified:February 1, 2005 - v2
Checksum:i6AFEAE92E2515488
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A287BHR3A0A287BHR3_PIG
Coagulation factor IX
F9
419Annotation score:
F1RQ75F1RQ75_PIG
Coagulation factor IX
F9
462Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51135 mRNA Translation: AAA96318.1
M26235 mRNA Translation: AAA31031.1
X92427 Genomic DNA Translation: CAA63155.1
X92593 Genomic DNA Translation: CAA63337.1
PIRiI46580
UniGeneiSsc.16252

Similar proteinsi

Entry informationi

Entry nameiFA9_PIG
AccessioniPrimary (citable) accession number: P16293
Secondary accession number(s): Q28994
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 2005
Last modified: March 28, 2018
This is version 154 of the entry and version 2 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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