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Reviewed, UniProtKB/Swiss-Prot P16291 (FA9_SHEEP)

Last modified June 16, 2009. Version 73. 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

Names and origin

Protein namesRecommended name:
    Coagulation factor IX
    EC=3.4.21.22
Alternative name(s):
    Christmas factor
Gene names
Name: F9
OrganismOvis aries (Sheep)
Taxonomic identifier9940 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis

Protein attributes

Sequence length274 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript 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.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processBlood coagulation
   Cellular componentSecreted
   LigandCalcium
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processblood coagulation

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›274›274Coagulation factor IX
PRO_0000088686

Regions

Domain49 – ›274›226Peptidase S1

Sites

Active site891Charge relay system
Active site1371Charge relay system
Active site2331Charge relay system

Amino acid modifications

Glycosylation251N-linked (GlcNAc...) Potential
Glycosylation351N-linked (GlcNAc...) Potential
Glycosylation401N-linked (GlcNAc...) Potential
Glycosylation1281N-linked (GlcNAc...) Potential
Disulfide bond74 ↔ 90 By similarity
Disulfide bond204 ↔ 218 By similarity
Disulfide bond229 ↔ 257 By similarity

Experimental info

Non-terminal residue11
Non-terminal residue2741

Sequences

Sequence LengthMass (Da)Tools
P16291-1 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: D3617FC3B1D33E9B

FASTA27430,595
        10         20         30         40         50         60 
RASVLHTSKK LTRAETIFSN MNYENSSEAE IIWDNVTQSN QSFDDFNRVV GGEDAARGQF 

        70         80         90        100        110        120 
PWQVLLHGEI AAFCGGSIVN EKWVVTAAHC IKPGVKITVV AGEHNTEKPE PTEQKRNVIR 

       130        140        150        160        170        180 
AIPYHGYNAS INKYSHDIAL LELDEPLELN SYVTPICIAD REYTNIFLKF GYGYVSGWGR 

       190        200        210        220        230        240 
VFNRGRSASI LQYLKVPLVD RATCLRSTKF TIYNHMFCAG YHEGGKDSCQ GDSGGPHVTE 

       250        260        270 
VEGTSFLTGI ISWGEECAMK GKYGIYTKVS RYEV 

« Hide

References

[1]"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].

Cross-references

Sequence databases

M26233 mRNA. Translation: AAA31520.1.
PIRI47078.
UniGeneOar.369

3D structure databases

HSSPHSSP built from PDB template 1PFX based on UniProtKB P16293.
SMRP16291. Positions 49-272.
ModBaseSearch...

Protein family/group databases

MEROPSS01.214.

Phylogenomic databases

HOVERGENP16291.

Enzyme and pathway databases

BRENDA3.4.21.22. 271.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFA9_SHEEP
AccessionPrimary (citable) accession number: P16291
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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