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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1 – 11Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi2 – 21Calcium 2By similarity
Metal bindingi7 – 71Calcium 1; via 4-carboxyglutamateBy similarity
Metal bindingi7 – 71Calcium 2; via 4-carboxyglutamateBy similarity
Metal bindingi8 – 81Calcium 2; via 4-carboxyglutamateBy similarity
Metal bindingi8 – 81Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi16 – 161Calcium 4 or magnesium 1; via 4-carboxyglutamateBy similarity
Metal bindingi18 – 181Calcium 1; via 4-carboxyglutamateBy similarity
Metal bindingi18 – 181Calcium 2; via 4-carboxyglutamateBy similarity
Metal bindingi18 – 181Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi21 – 211Calcium 4 or magnesium 1; via 4-carboxyglutamateBy similarity
Metal bindingi22 – 221Calcium 1; via 4-carboxyglutamateBy similarity
Metal bindingi27 – 271Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity
Metal bindingi28 – 281Calcium 2; via 4-carboxyglutamateBy similarity
Metal bindingi28 – 281Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi31 – 311Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi31 – 311Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity
Metal bindingi37 – 371Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity
Metal bindingi41 – 411Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity
Metal bindingi48 – 481Calcium 7By similarity
Metal bindingi49 – 491Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi51 – 511Calcium 7By similarity
Metal bindingi65 – 651Calcium 7By similarity
Metal bindingi66 – 661Calcium 7; via carbonyl oxygenBy similarity
Active sitei223 – 2231Charge relay systemBy similarity
Metal bindingi237 – 2371Calcium 8By similarity
Metal bindingi239 – 2391Calcium 8; via carbonyl oxygenBy similarity
Metal bindingi242 – 2421Calcium 8; via carbonyl oxygenBy similarity
Metal bindingi244 – 2441Calcium 8By similarity
Metal bindingi247 – 2471Calcium 8By similarity
Active sitei271 – 2711Charge relay systemBy similarity
Active sitei367 – 3671Charge relay systemBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409Coagulation factor IXPRO_0000027770Add
BLAST
Chaini1 – 147147Coagulation factor IXa light chainPRO_0000027771Add
BLAST
Propeptidei148 – 18235Activation peptideBy similarityPRO_0000027772Add
BLAST
Chaini183 – 409227Coagulation factor IXa heavy chainPRO_0000027773Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 714-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei8 – 814-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei16 – 1614-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei18 – 1814-carboxyglutamatePROSITE-ProRule annotationBy similarity
Disulfide bondi19 ↔ 241 Publication
Modified residuei21 – 2114-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei22 – 2214-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei27 – 2714-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei28 – 2814-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei31 – 3114-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei34 – 3414-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei37 – 3714-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei41 – 4114-carboxyglutamatePROSITE-ProRule annotationBy similarity
Disulfide bondi52 ↔ 631 Publication
Disulfide bondi57 ↔ 721 Publication
Modified residuei65 – 651(3R)-3-hydroxyaspartateBy similarity
Modified residuei69 – 691PhosphoserineBy similarity
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 residuei157 – 1571SulfotyrosineBy similarity
Modified residuei160 – 1601PhosphoserineBy similarity
Modified residuei161 – 1611Phosphothreonine; alternateBy similarity
Glycosylationi161 – 1611O-linked (GalNAc...); alternateBy similarity
Glycosylationi171 – 1711O-linked (GalNAc...)By similarity
Glycosylationi174 – 1741N-linked (GlcNAc...)Sequence analysis
Disulfide bondi208 ↔ 2241 Publication
Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence analysis
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)LengthDescriptionGraphical viewFeature identifierActions
Sitei147 – 1482Cleavage; by factor XIaBy similarity
Sitei182 – 1832Cleavage; by factor XIaBy similarity

Keywords - PTMi

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

Proteomic databases

PeptideAtlasiP16293.

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
409
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 184Combined sources
Turni19 – 235Combined sources
Helixi26 – 338Combined sources
Helixi37 – 448Combined sources
Turni51 – 544Combined sources
Beta strandi62 – 654Combined sources
Beta strandi70 – 734Combined sources
Beta strandi76 – 805Combined sources
Turni81 – 833Combined sources
Helixi92 – 943Combined sources
Beta strandi97 – 993Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi122 – 1276Combined sources
Beta strandi129 – 1313Combined sources
Turni138 – 1436Combined sources
Beta strandi197 – 2015Combined sources
Beta strandi208 – 2147Combined sources
Beta strandi217 – 2204Combined sources
Helixi222 – 2243Combined sources
Beta strandi232 – 2343Combined sources
Beta strandi252 – 2576Combined sources
Beta strandi263 – 2653Combined sources
Beta strandi273 – 2797Combined sources
Beta strandi285 – 2873Combined sources
Helixi295 – 3028Combined sources
Beta strandi305 – 3128Combined sources
Beta strandi314 – 3196Combined sources
Beta strandi326 – 3338Combined sources
Helixi335 – 3395Combined sources
Beta strandi348 – 3547Combined sources
Beta strandi356 – 3594Combined sources
Turni364 – 3685Combined sources
Beta strandi370 – 3778Combined sources
Beta strandi379 – 3879Combined sources
Beta strandi389 – 3924Combined sources
Beta strandi398 – 4014Combined sources
Helixi403 – 4097Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PFXX-ray3.00C183-409[»]
L8-147[»]
1X7AX-ray2.90C183-409[»]
L1-147[»]
ProteinModelPortaliP16293.
SMRiP16293. Positions 1-147, 183-409.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16293.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 4747GlaPROSITE-ProRule annotationAdd
BLAST
Domaini48 – 8437EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini85 – 12642EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini183 – 409227Peptidase S1PROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1PFXX-ray3.00C183-409[»]
L8-147[»]
1X7AX-ray2.90C183-409[»]
L1-147[»]
ProteinModelPortaliP16293.
SMRiP16293. Positions 1-147, 183-409.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.214.

Proteomic databases

PeptideAtlasiP16293.

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: September 7, 2016
This is version 144 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.