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Reviewed, UniProtKB/Swiss-Prot Q95ND7 (FA9_PANTR)

Last modified February 9, 2010. Version 76. 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
OrganismPan troglodytes (Chimpanzee)
Taxonomic identifier9598 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pan

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Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 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.

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 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 – 2828 Potential
Propeptide29 – 4618 By similarity
PRO_0000027765
Chain47 – 461415Coagulation factor IX
PRO_0000027766
Chain47 – 191145Coagulation factor IXa light chain
PRO_0000027767
Propeptide192 – 22635Activation peptide
PRO_0000027768
Chain227 – 461235Coagulation factor IXa heavy chain
PRO_0000027769

Regions

Domain47 – 9246Gla
Domain93 – 12937EGF-like 1; calcium-binding Potential
Domain130 – 17142EGF-like 2
Domain227 – 459233Peptidase S1

Sites

Active site2671Charge relay system By similarity
Active site3151Charge relay system By similarity
Active site4111Charge relay system By similarity
Site191 – 1922Cleavage; by factor XIa
Site226 – 2272Cleavage; by factor XIa

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 residue2011Sulfotyrosine By similarity
Modified residue2041Phosphoserine By similarity
Glycosylation991O-linked (Glc...) By similarity
Glycosylation1071O-linked (Fuc...) By similarity
Glycosylation2051O-linked (GalNAc...) By similarity
Glycosylation2131N-linked (GlcNAc...) Potential
Glycosylation2151O-linked (GalNAc...) By similarity
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 ↔ 335 By similarity
Disulfide bond252 ↔ 268 By similarity
Disulfide bond382 ↔ 396 By similarity
Disulfide bond407 ↔ 435 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q95ND7-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 30C2F857C0F77F45

FASTA46151,764
        10         20         30         40         50         60 
MQRVNMIMAE SPGLITICLL GYLLSAECTV FLDHENANKI LNRPKRYNSG KLEEFVQGNL 

        70         80         90        100        110        120 
ERECMEEKCS FEEAREVFEN TERTTEFWKQ YVDGDQCESN PCLNGGSCKD DINSYECWCP 

       130        140        150        160        170        180 
FGFEGKNCEL DVTCNIKNGR CEQFCKNSAD NKVVCSCTEG YRLAENQKSC EPAVPFPCGR 

       190        200        210        220        230        240 
VSVSQTSKLT RAETVFPDVD YVNSTEAETI LDNITQSTQS FNDFTRVVGG EDAKPGQFPW 

       250        260        270        280        290        300 
QVVLNGKVDA FCGGSIVNEK WIVTAAHCVD TGVKITVVAG EHNIEETEHT EQKRNVIRII 

       310        320        330        340        350        360 
PHHNYNAAIN KYNHDIALLE LDEPLVLNSY VTPICIADKE YTNIFLKFGS GYVSGWGRVF 

       370        380        390        400        410        420 
HKGRSALVLQ YLRVPLVDRA TCLRSTKFTI YNNMFCAGFH EGGRDSCQGD SGGPHVTEVE 

       430        440        450        460 
GTSFLTGIIS WGEECAMKGK YGIYTKVSRY VNWIKEKTKL T

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References

[1]"Comparison of DNA and protein polymorphisms between humans and chimpanzees."
Satta Y.
Genes Genet. Syst. 76:159-168(2001) [PubMed: 11569499] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Isolate 504.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB062470 Genomic DNA. Translation: BAB58885.1.
RefSeqNP_001129063.1.

3D structure databases

SMRQ95ND7. Positions 47-191, 135-458, 227-461.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ95ND7.

Protein family/group databases

MEROPSS01.214.

Genome annotation databases

EnsemblENSPTRT00000041650; ENSPTRP00000047240; ENSPTRG00000022330; Pan troglodytes. [Genome view]
GeneID465887.
KEGGptr:465887.

Organism-specific databases

CTD465887.

Phylogenomic databases

HOVERGENQ95ND7.
InParanoidQ95ND7.

Enzyme and pathway databases

BRENDA3.4.21.22. 264977.

Family and domain databases

InterProIPR002383. Coagulation_factor_Gla_dom.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
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.
IPR009003. Ser/Cys_Pept_Trypsin-like.
[Graphical view]
PfamPF00594. 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...

Other Resources

PMAP-CutDBQ95ND7.

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Entry information

Entry nameFA9_PANTR
AccessionPrimary (citable) accession number: Q95ND7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: December 1, 2001
Last modified: February 9, 2010
This is version 76 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