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P16294 (FA9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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. Coagulation factor IXa light chain
  2. Coagulation factor IXa heavy chain
Gene names
Name:F9
Synonyms:Cf9
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Propeptide29 – 4618 By similarity
PRO_0000027760
Chain47 – 471425Coagulation factor IX
PRO_0000027761
Chain47 – 192146Coagulation factor IXa light chain
PRO_0000027762
Propeptide193 – 23644Activation peptide By similarity
PRO_0000027763
Chain237 – 471235Coagulation factor IXa heavy chain
PRO_0000027764

Regions

Domain47 – 9246Gla
Domain93 – 12937EGF-like 1; calcium-binding Potential
Domain130 – 17142EGF-like 2
Domain237 – 469233Peptidase S1

Sites

Active site2771Charge relay system By similarity
Active site3251Charge relay system By similarity
Active site4211Charge relay system By similarity
Site192 – 1932Cleavage; by factor XIa By similarity
Site236 – 2372Cleavage; 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 residue2051Phosphoserine By similarity
Glycosylation991O-linked (Glc...) By similarity
Glycosylation2041N-linked (GlcNAc...) Potential
Glycosylation2061O-linked (GalNAc...) By similarity
Glycosylation2231N-linked (GlcNAc...) Potential
Glycosylation2251O-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 ↔ 345 By similarity
Disulfide bond262 ↔ 278 By similarity
Disulfide bond392 ↔ 406 By similarity
Disulfide bond417 ↔ 445 By similarity

Experimental info

Sequence conflict3751Q → H in AAA37629. Ref.2
Sequence conflict4001I → T in AAA37629. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P16294 [UniParc].

Last modified January 9, 2007. Version 3.
Checksum: 05E08E86622397E2

FASTA47152,978
        10         20         30         40         50         60 
MKHLNTVMAE SPALITIFLL GYLLSTECAV FLDRENATKI LTRPKRYNSG KLEEFVRGNL 

        70         80         90        100        110        120 
ERECIEERCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN PCLNGGICKD DISSYECWCQ 

       130        140        150        160        170        180 
VGFEGRNCEL DATCNIKNGR CKQFCKNSPD NKVICSCTEG YQLAEDQKSC EPTVPFPCGR 

       190        200        210        220        230        240 
ASISYSSKKI TRAETVFSNM DYENSTEAVF IQDDITDGAI LNNVTESSES LNDFTRVVGG 

       250        260        270        280        290        300 
ENAKPGQIPW QVILNGEIEA FCGGAIINEK WIVTAAHCLK PGDKIEVVAG EYNIDKKEDT 

       310        320        330        340        350        360 
EQRRNVIRTI PHHQYNATIN KYSHDIALLE LDKPLILNSY VTPICVANRE YTNIFLKFGS 

       370        380        390        400        410        420 
GYVSGWGKVF NKGRQASILQ YLRVPLVDRA TCLRSTTFTI YNNMFCAGYR EGGKDSCEGD 

       430        440        450        460        470 
SGGPHVTEVE GTSFLTGIIS WGEECAMKGK YGIYTKVSRY VNWIKEKTKL T

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver.
[2]"Deduced amino acid sequence of mouse blood-coagulation factor IX."
Wu S.-M., Stafford D.W., Ware J.
Gene 86:275-278(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-471.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 180-463.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK149372 mRNA. Translation: BAE28840.1.
M23109 mRNA. Translation: AAA37629.1.
M26236 mRNA. Translation: AAA37630.1.
IPIIPI00348266.
PIRJQ0419.
RefSeqNP_032005.1. NM_007979.1.
UniGeneMm.391283.

3D structure databases

ProteinModelPortalP16294.
SMRP16294. Positions 47-192, 237-470.
ModBaseSearch...

Protein family/group databases

MEROPSS01.214.

PTM databases

PhosphoSiteP16294.

Proteomic databases

PaxDbP16294.
PRIDEP16294.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033477; ENSMUSP00000033477; ENSMUSG00000031138.
GeneID14071.
KEGGmmu:14071.

Organism-specific databases

CTD2158.
MGIMGI:88384. F9.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00560000076714.
HOGENOMHOG000251821.
HOVERGENHBG013304.
InParanoidP16294.
KOK01321.
OrthoDBEOG4THVTF.

Gene expression databases

ArrayExpressP16294.
BgeeP16294.
CleanExMM_F9.
GenevestigatorP16294.
GermOnlineENSMUSG00000031138. Mus musculus.

Family and domain databases

Gene3D4.10.740.10. 1 hit.
InterProIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00008. EGF. 1 hit.
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]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
SSF57630. VitK_dep_GLA. 1 hit.
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

NextBio285068.
SOURCESearch...

Entry information

Entry nameFA9_MOUSE
AccessionPrimary (citable) accession number: P16294
Secondary accession number(s): Q3UES1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 9, 2007
Last modified: April 3, 2013
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents