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Protein

Coagulation factor IX

Gene

F9

Organism
Sus scrofa (Pig)
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.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

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, 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

  • Secreted By similarity

GO - Cellular componenti

Complete GO annotation...

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...); alternateBy similarity1
Glycosylationi171O-linked (GalNAc...)By similarity1
Glycosylationi174N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi208 ↔ 2241 Publication
Glycosylationi262N-linked (GlcNAc...)Sequence 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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 18Combined sources4
Turni19 – 23Combined sources5
Helixi26 – 33Combined sources8
Helixi37 – 44Combined sources8
Turni51 – 54Combined sources4
Beta strandi62 – 65Combined sources4
Beta strandi70 – 73Combined sources4
Beta strandi76 – 80Combined sources5
Turni81 – 83Combined sources3
Helixi92 – 94Combined sources3
Beta strandi97 – 99Combined sources3
Beta strandi104 – 106Combined sources3
Beta strandi116 – 118Combined sources3
Beta strandi122 – 127Combined sources6
Beta strandi129 – 131Combined sources3
Turni138 – 143Combined sources6
Beta strandi197 – 201Combined sources5
Beta strandi208 – 214Combined sources7
Beta strandi217 – 220Combined sources4
Helixi222 – 224Combined sources3
Beta strandi232 – 234Combined sources3
Beta strandi252 – 257Combined sources6
Beta strandi263 – 265Combined sources3
Beta strandi273 – 279Combined sources7
Beta strandi285 – 287Combined sources3
Helixi295 – 302Combined sources8
Beta strandi305 – 312Combined sources8
Beta strandi314 – 319Combined sources6
Beta strandi326 – 333Combined sources8
Helixi335 – 339Combined sources5
Beta strandi348 – 354Combined sources7
Beta strandi356 – 359Combined sources4
Turni364 – 368Combined sources5
Beta strandi370 – 377Combined sources8
Beta strandi379 – 387Combined sources9
Beta strandi389 – 392Combined sources4
Beta strandi398 – 401Combined sources4
Helixi403 – 409Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PFXX-ray3.00C183-409[»]
L8-147[»]
1X7AX-ray2.90C183-409[»]
L1-147[»]
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
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, Repeat

Phylogenomic databases

HOVERGENiHBG013304.
InParanoidiP16293.

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: Fragment.

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

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

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PFXX-ray3.00C183-409[»]
L8-147[»]
1X7AX-ray2.90C183-409[»]
L1-147[»]
ProteinModelPortaliP16293.
SMRiP16293.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.214.

Proteomic databases

PeptideAtlasiP16293.
PRIDEiP16293.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG013304.
InParanoidiP16293.

Miscellaneous databases

EvolutionaryTraceiP16293.

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_PIG
AccessioniPrimary (citable) accession number: P16293
Secondary accession number(s): Q28994
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 2005
Last modified: November 2, 2016
This is version 146 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.