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P16293 (FA9_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coagulation factor IX
EC=3.4.21.22
Alternative name(s):
Christmas factor

Cleaved into the following 2 chains:

  1. Coagulation factor IXa light chain
  2. Coagulation factor IXa heavy chain
Gene names
Name:F9
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length409 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Subunit structure

Heterodimer of a light chain and a heavy chain; disulfide-linked.

Subcellular location

Secreted.

Tissue specificity

Synthesized primarily in the liver and secreted in plasma.

Domain

Calcium binds to the gamma-carboxyglutamic acid (Gla) residues and, with stronger affinity, to another site, beyond the Gla domain.

Post-translational modification

Activated by factor XIa, which excises the activation peptide By similarity.

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 2 EGF-like domains.

Contains 1 Gla (gamma-carboxy-glutamate) domain.

Contains 1 peptidase S1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 409409Coagulation factor IX
PRO_0000027770
Chain1 – 147147Coagulation factor IXa light chain
PRO_0000027771
Propeptide148 – 18235Activation peptide By similarity
PRO_0000027772
Chain183 – 409227Coagulation factor IXa heavy chain
PRO_0000027773

Regions

Domain1 – 4747Gla
Domain48 – 8437EGF-like 1; calcium-binding Potential
Domain85 – 12642EGF-like 2
Domain183 – 409227Peptidase S1

Sites

Active site2231Charge relay system
Active site2711Charge relay system
Active site3671Charge relay system
Site147 – 1482Cleavage; by factor XIa By similarity
Site182 – 1832Cleavage; by factor XIa By similarity

Amino acid modifications

Modified residue714-carboxyglutamate
Modified residue814-carboxyglutamate
Modified residue1614-carboxyglutamate
Modified residue1814-carboxyglutamate
Modified residue2114-carboxyglutamate
Modified residue2214-carboxyglutamate
Modified residue2714-carboxyglutamate
Modified residue2814-carboxyglutamate
Modified residue3114-carboxyglutamate
Modified residue3414-carboxyglutamate
Modified residue3714-carboxyglutamate
Modified residue4114-carboxyglutamate
Modified residue651(3R)-3-hydroxyaspartate
Modified residue691Phosphoserine By similarity
Modified residue1571Sulfotyrosine By similarity
Glycosylation1611O-linked (GalNAc...) By similarity
Glycosylation1711O-linked (GalNAc...) By similarity
Glycosylation1741N-linked (GlcNAc...) Potential
Glycosylation2621N-linked (GlcNAc...) Potential
Disulfide bond19 ↔ 24
Disulfide bond52 ↔ 63
Disulfide bond57 ↔ 72
Disulfide bond74 ↔ 83
Disulfide bond89 ↔ 100
Disulfide bond96 ↔ 110
Disulfide bond112 ↔ 125
Disulfide bond133 ↔ 291
Disulfide bond208 ↔ 224
Disulfide bond338 ↔ 352
Disulfide bond363 ↔ 391

Experimental info

Non-terminal residue11

Secondary structure

1 ..................................................................... 409
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16293 [UniParc].

Last modified February 1, 2005. Version 2.
Checksum: 6AFEAE92E2515488

FASTA40945,516
        10         20         30         40         50         60 
YNSGKLEESF VRGNLERECI EEKCSFEEAR EVFENTEKTN EFWKQYVDGD QCEPNPCLNG 

        70         80         90        100        110        120 
GLCKDDINSY ECWCQVGFEG KNCELDATCN IKNGRCKQFC KTGADSKVLC SCTTGYRLAP 

       130        140        150        160        170        180 
DQKSCKPAVP FPCGRVSVSH SPTTLTRAEI IFSNMDYENS TEVEPILDSL TESNQSSDDF 

       190        200        210        220        230        240 
IRIVGGENAK PGQFPWQVLL NGKIDAFCGG SIINEKWVVT AAHCIEPGVK ITVVAGEYNT 

       250        260        270        280        290        300 
EETEPTEQRR NVIRAIPHHS YNATVNKYSH DIALLELDEP LTLNSYVTPI CIADKEYTNI 

       310        320        330        340        350        360 
FLKFGSGYVS GWGRVFNRGR SATILQYLKV PLVDRATCLR STKVTIYSNM FCAGFHEGGK 

       370        380        390        400 
DSCLGDSGGP HVTEVEGTSF LTGIISWGEE CAVKGKYGIY TKVSRYVNW

« Hide

References

[1]Lollar P.
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-146.
Tissue: Liver.
[2]"Direct sequencing of the activation peptide and the catalytic domain of the factor IX gene in six species."
Sarkar G., Koeberl D.D., Sommer S.S.
Genomics 6:133-143(1990) [PubMed: 2303254] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 139-409.
[3]"Detection of an MboI RFLP at the porcine clotting factor IX locus and verification of sex linkage."
Signer E.N., Armour J.A.L., Jeffreys A.J.
Anim. Genet. 27:130-130(1996) [PubMed: 8856916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 237-245.
Strain: Meishan and Wild boar.
[4]"Degradation of coagulation proteins by an enzyme from Malayan pit viper (Akistrodon rhodostoma) venom."
Lollar P., Parker C.G., Kajenski P.J., Litwiller R.D., Fass D.N.
Biochemistry 26:7627-7636(1987) [PubMed: 3322404] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
[5]"X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B."
Brandstetter H., Bauer M., Huber R., Lollar P., Bode W.
Proc. Natl. Acad. Sci. U.S.A. 92:9796-9800(1995) [PubMed: 7568220] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U51135 mRNA. Translation: AAA96318.1.
M26235 mRNA. Translation: AAA31031.1.
X92427 Genomic DNA. Translation: CAA63155.1.
X92593 Genomic DNA. Translation: CAA63337.1.
PIRI46580.
UniGeneSsc.16252.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PFXX-ray3.00C183-409[»]
L10-147[»]
1X7AX-ray2.90C183-409[»]
L10-147[»]
ProteinModelPortalP16293.
SMRP16293. Positions 1-147, 183-409.
ModBaseSearch...

Protein-protein interaction databases

STRINGP16293.

Protein family/group databases

MEROPSS01.214.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG013304.

Family and domain databases

InterProIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR006209. EGF.
IPR006210. EGF-like.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR000742. EGF_3.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR009003. Pept_cys/ser_Trypsin-like.
IPR012224. Pept_S1A_FX.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
Gene3DG3DSA:4.10.740.10. Coagulation_factor_Gla. 1 hit.
PfamPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001143. Factor_X. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
SSF57630. VitK_dep_GLA. 1 hit.
PROSITEPS00010. 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]
ProtoNetSearch...

Entry information

Entry nameFA9_PIG
AccessionPrimary (citable) accession number: P16293
Secondary accession number(s): Q28994
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 2005
Last modified: November 16, 2011
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents