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Reviewed, UniProtKB/Swiss-Prot Q6SA95 (FA9_FELCA)

Last modified June 16, 2009. Version 47. 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
OrganismFelis silvestris catus (Cat)
Taxonomic identifier9685 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Feliformia › Felidae › Felinae › Felis

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Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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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 By similarity.

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 By similarity.

Subcellular location

Secreted By similarity.

Domain

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

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 By similarity.

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 – 2525 Potential
Propeptide26 – 4621 By similarity
PRO_0000027750
Chain47 – 466420Coagulation factor IX
PRO_0000027751
Chain47 – 192146Coagulation factor IXa light chain
PRO_0000027752
Propeptide193 – 23139Activation peptide By similarity
PRO_0000027753
Chain232 – 466235Coagulation factor IXa heavy chain
PRO_0000027754

Regions

Domain47 – 9246Gla
Domain93 – 12937EGF-like 1; calcium-binding Potential
Domain130 – 17142EGF-like 2
Domain232 – 464233Peptidase S1

Sites

Active site2721Charge relay system By similarity
Active site3201Charge relay system By similarity
Active site4161Charge relay system By similarity
Site192 – 1932Cleavage; by factor XIa By similarity
Site231 – 2322Cleavage; by factor XIa By similarity

Amino acid modifications

Modified residue5314-carboxyglutamate By similarity
Modified residue5414-carboxyglutamate By similarity
Modified residue6114-carboxyglutamate By similarity
Modified residue6314-carboxyglutamate By similarity
Modified residue6614-carboxyglutamate By similarity
Modified residue6714-carboxyglutamate By similarity
Modified residue7214-carboxyglutamate By similarity
Modified residue7314-carboxyglutamate By similarity
Modified residue7614-carboxyglutamate By similarity
Modified residue7914-carboxyglutamate By similarity
Modified residue8214-carboxyglutamate By similarity
Modified residue8614-carboxyglutamate By similarity
Modified residue1101(3R)-3-hydroxyaspartate By similarity
Modified residue1141Phosphoserine By similarity
Modified residue2021Sulfotyrosine By similarity
Modified residue2091Sulfotyrosine Potential
Modified residue2121Phosphoserine By similarity
Glycosylation991O-linked (Glc...) By similarity
Glycosylation2061O-linked (GalNAc...) By similarity
Glycosylation2211N-linked (GlcNAc...) Potential
Disulfide bond64 ↔ 69 By similarity
Disulfide bond97 ↔ 108 By similarity
Disulfide bond102 ↔ 117 By similarity
Disulfide bond119 ↔ 128 By similarity
Disulfide bond134 ↔ 145 By similarity
Disulfide bond141 ↔ 155 By similarity
Disulfide bond157 ↔ 170 By similarity
Disulfide bond178 ↔ 340 By similarity
Disulfide bond257 ↔ 273 By similarity
Disulfide bond387 ↔ 401 By similarity
Disulfide bond412 ↔ 440 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q6SA95-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: D4F788D4CC1A4DCC

FASTA46652,320
        10         20         30         40         50         60 
MRCLNMIMAE PPGLITICLL GYLLGADCTV FLDHEDATKV LSRPKRYNSG KLEEFVQGNL 

        70         80         90        100        110        120 
ERECMEEKCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN PCLNGGICKD DINSYECWCQ 

       130        140        150        160        170        180 
TGFEGKNCEL DVTCNIKNGR CKQFCKLDAD NKVVCSCTTG YQLAEDQKSC EPAVPFPCGR 

       190        200        210        220        230        240 
VSVPHISTTH TRAETLFLNM DYENSTTDYE NSAEAEKNVD NVTQPLNDLT RIVGGKTAKP 

       250        260        270        280        290        300 
GQFPWQVLLK GKIDAFCGGS IINEKWVVTA AHCINPDVEI TVVAGEHNTE ETEHTEQKRN 

       310        320        330        340        350        360 
VIRTILHHSY NASVNKYSHD IALLELDEPL TLNSYVTPIC VADREYTNTF LKFGYGYVSG 

       370        380        390        400        410        420 
WGKVFNKGRP ATILQYLKVP LVDRATCLRS TKFTIYNNMF CAGFHEGGKD SCQGDSGGPH 

       430        440        450        460 
VTEVEGINFL TGIISWGEEC AMKGKYGIYT KVSRYVNWIK EKTKLT

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References

[1]"Feline factor IX gene."
Boudreaux M.K., Goree S.M.
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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Cross-references

Sequence databases

AY461386 expand/collapse EMBL AC list , AY461381, AY461382, AY461383, AY461384, AY461385 Genomic DNA. Translation: AAR26346.1.
RefSeqNP_001009377.1.

3D structure databases

HSSPHSSP built from PDB template 1APO based on UniProtKB P00743.
SMRQ6SA95. Positions 47-192, 232-466.
ModBaseSearch...

Genome annotation databases

GeneID493973.

Phylogenomic databases

HOVERGENQ6SA95.

Enzyme and pathway databases

BRENDA3.4.21.22. 273949.

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.
IPR001438. EGF_2.
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.
PR00010. EGFBLOOD.
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_FELCA
AccessionPrimary (citable) accession number: Q6SA95
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 5, 2004
Last modified: June 16, 2009
This is version 47 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