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Reviewed, UniProtKB/Swiss-Prot P19540 (FA9_CANFA)

Last modified June 16, 2009. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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- Recommended name:
            Coagulation factor IXa light chain
    2- Recommended name:
            Coagulation factor IXa heavy chain
Gene names
Name: F9
OrganismCanis familiaris (Dog)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

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Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

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

Involvement in disease

Defects in F9 are the cause of hemophilia B (HEMB). Ref.3

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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 By similarity
Propeptide22 – 3918
PRO_0000027745
Chain40 – 452413Coagulation factor IX
PRO_0000027746
Chain40 – 183144Coagulation factor IXa light chain
PRO_0000027747
Propeptide184 – 21734Activation peptide
PRO_0000027748
Chain218 – 452235Coagulation factor IXa heavy chain
PRO_0000027749

Regions

Domain40 – 8546Gla
Domain86 – 12237EGF-like 1; calcium-binding Potential
Domain123 – 16442EGF-like 2
Domain218 – 450233Peptidase S1

Sites

Active site2581Charge relay system
Active site3061Charge relay system
Active site4021Charge relay system
Site183 – 1842Cleavage; by factor XIa By similarity
Site217 – 2182Cleavage; by factor XIa By similarity

Amino acid modifications

Modified residue4614-carboxyglutamate By similarity
Modified residue4714-carboxyglutamate By similarity
Modified residue5414-carboxyglutamate By similarity
Modified residue5614-carboxyglutamate By similarity
Modified residue5914-carboxyglutamate By similarity
Modified residue6014-carboxyglutamate By similarity
Modified residue6514-carboxyglutamate By similarity
Modified residue6614-carboxyglutamate By similarity
Modified residue6914-carboxyglutamate By similarity
Modified residue7214-carboxyglutamate By similarity
Modified residue7514-carboxyglutamate By similarity
Modified residue7914-carboxyglutamate By similarity
Modified residue1031(3R)-3-hydroxyaspartate By similarity
Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Disulfide bond57 ↔ 62 By similarity
Disulfide bond90 ↔ 101 By similarity
Disulfide bond95 ↔ 110 By similarity
Disulfide bond112 ↔ 121 By similarity
Disulfide bond127 ↔ 138 By similarity
Disulfide bond134 ↔ 148 By similarity
Disulfide bond150 ↔ 163 By similarity
Disulfide bond171 ↔ 326 By similarity
Disulfide bond243 ↔ 259 By similarity
Disulfide bond373 ↔ 387 By similarity
Disulfide bond398 ↔ 426 By similarity

Natural variations

Natural variant4181G → E in HEMB. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
P19540-1 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 1F6537C46A6960ED

FASTA45250,828
        10         20         30         40         50         60 
MAEASGLVTV CLLGYLLSAE CAVFLDRENA TKILSRPKRY NSGKLEEFVR GNLERECIEE 

        70         80         90        100        110        120 
KCSFEEAREV FENTEKTTEF WKQYVDGDQC ESNPCLNDGV CKDDINSYEC WCRAGFEGKN 

       130        140        150        160        170        180 
CELDVTCNIK NGRCKQFCKL GPDNKVVCSC TTGYQLAEDQ RSCEPAVPFP CGRVSVPHIS 

       190        200        210        220        230        240 
MTRTRAETLF SNMDYENSTE VEKILDNVTQ PLNDFTRVVG GKDAKPGQFP WQVLLNGKVD 

       250        260        270        280        290        300 
AFCGGSIINE KWVVTAAHCI EPDVKITIVA GEHNTEKREH TEQKRNVIRT ILHHSYNATI 

       310        320        330        340        350        360 
NKYNHDIALL ELDEPLTLNS YVTPICIADR EYSNIFLKFG SGYVSGWGRV FNKGRSASIL 

       370        380        390        400        410        420 
QYLKVPLVDR ATCLRSTKFT IYNNMFCAGF HEGGKDSCQG DSGGPHVTEV EGISFLTGII 

       430        440        450 
SWGEECAMKG KYGIYTKVSR YVNWIKEKTK LT

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References

[1]"Phenotypic correction of factor IX deficiency in skin fibroblasts of hemophilic dogs."
Axelrod J.H., Read M.S., Brinkhous K.M., Verma I.M.
Proc. Natl. Acad. Sci. U.S.A. 87:5173-5177(1990) [PubMed: 2367529] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Molecular cloning of a cDNA encoding canine factor IX."
Evans J.P., Watzke H.H., Ware J.L., Stafford D.W., High K.A.
Blood 74:207-212(1989) [PubMed: 2752110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Canine hemophilia B resulting from a point mutation with unusual consequences."
Evans J.P., Brinkhous K.M., Brayer G.D., Reisner H.M., High K.A.
Proc. Natl. Acad. Sci. U.S.A. 86:10095-10099(1989) [PubMed: 2481310] [Abstract]
Cited for: VARIANT HEMB GLU-418.

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Cross-references

Sequence databases

M21757 mRNA. Translation: AAA75006.1.
M33826 mRNA. Translation: AAA30844.1.
PIRA30351.
RefSeqNP_001003323.1.
UniGeneCfa.3857

3D structure databases

HSSPHSSP built from PDB template 1CFH based on UniProtKB P00740.
SMRP19540. Positions 40-185, 218-452.
ModBaseSearch...

Protein family/group databases

MEROPSS01.214.

Genome annotation databases

EnsemblENSCAFG00000018998. Canis familiaris. [Contig view]
GeneID404015.
KEGGcfa:404015.

Phylogenomic databases

HOVERGENP19540.

Enzyme and pathway databases

BRENDA3.4.21.22. 463.

Family and domain databases

InterProIPR002383. Coagulation_factor_Gla.
IPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_CS.
IPR000742. EGF_3.
IPR001881. EGF_Ca_bd.
IPR018097. EGF_Ca_bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00008. EGF. 2 hits.
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]
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...

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Entry information

Entry nameFA9_CANFA
AccessionPrimary (citable) accession number: P19540
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 16, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents