Reviewed,
UniProtKB/Swiss-Prot P16291 (FA9_SHEEP)
Last modified
June 16, 2009.
Version 73.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Coagulation factor IX EC=3.4.21.22 Alternative name(s): Christmas factor | ||
| Gene names |
| ||
| Organism | Ovis aries (Sheep) | ||
| Taxonomic identifier | 9940 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis |
Protein attributes
| Sequence length | 274 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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 | |
| 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 process | Blood coagulation |
| Cellular component | Secreted |
| Ligand | Calcium |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Disulfide bond Glycoprotein |
| Gene Ontology (GO) | |
| Biological process | blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – ›274 | ›274 | Coagulation factor IX | PRO_0000088686 | |||||||
Regions | |||||||||||
| Domain | 49 – ›274 | ›226 | Peptidase S1 | ||||||||
Sites | |||||||||||
| Active site | 89 | 1 | Charge relay system | ||||||||
| Active site | 137 | 1 | Charge relay system | ||||||||
| Active site | 233 | 1 | Charge relay system | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 25 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 35 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 40 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 128 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 74 ↔ 90 | By similarity | |||||||||
| Disulfide bond | 204 ↔ 218 | By similarity | |||||||||
| Disulfide bond | 229 ↔ 257 | By similarity | |||||||||
Experimental info | |||||||||||
| Non-terminal residue | 1 | 1 | |||||||||
| Non-terminal residue | 274 | 1 | |||||||||
Sequences
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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. | |
| PIR | I47078. |
| UniGene | Oar.369 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1PFX based on UniProtKB P16293. |
| SMR | P16291. Positions 49-272. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S01.214. |
Phylogenomic databases | |
| HOVERGEN | P16291. |
Enzyme and pathway databases | |
| BRENDA | 3.4.21.22. 271. |
Family and domain databases | |
| InterPro | IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view] |
| Pfam | PF00089. Trypsin. 1 hit. [Graphical view] |
| PRINTS | PR00722. CHYMOTRYPSIN. |
| SMART | SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| PROSITE | PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FA9_SHEEP | ||||||||
| Accession | Primary (citable) accession number: P16291 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


