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P16294

- FA9_MOUSE

UniProt

P16294 - FA9_MOUSE

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Protein
Coagulation factor IX
Gene
F9, Cf9
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei192 – 1932Cleavage; by factor XIa By similarity
Sitei236 – 2372Cleavage; by factor XIa By similarity
Active sitei277 – 2771Charge relay system By similarity
Active sitei325 – 3251Charge relay system By similarity
Active sitei421 – 4211Charge relay system By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. peptidase activity Source: MGI
  3. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. blood coagulation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

Protein family/group databases

MEROPSiS01.214.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor IX (EC:3.4.21.22)
Alternative name(s):
Christmas factor
Cleaved into the following 2 chains:
Gene namesi
Name:F9
Synonyms:Cf9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:88384. F9.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828 Reviewed prediction
Add
BLAST
Propeptidei29 – 4618 By similarity
PRO_0000027760Add
BLAST
Chaini47 – 471425Coagulation factor IX
PRO_0000027761Add
BLAST
Chaini47 – 192146Coagulation factor IXa light chain
PRO_0000027762Add
BLAST
Propeptidei193 – 23644Activation peptide By similarity
PRO_0000027763Add
BLAST
Chaini237 – 471235Coagulation factor IXa heavy chain
PRO_0000027764Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 5314-carboxyglutamate By similarity
Modified residuei54 – 5414-carboxyglutamate By similarity
Modified residuei61 – 6114-carboxyglutamate By similarity
Modified residuei63 – 6314-carboxyglutamate By similarity
Disulfide bondi64 ↔ 69 By similarity
Modified residuei66 – 6614-carboxyglutamate By similarity
Modified residuei67 – 6714-carboxyglutamate By similarity
Modified residuei72 – 7214-carboxyglutamate By similarity
Modified residuei73 – 7314-carboxyglutamate By similarity
Modified residuei76 – 7614-carboxyglutamate By similarity
Modified residuei79 – 7914-carboxyglutamate By similarity
Modified residuei82 – 8214-carboxyglutamate By similarity
Modified residuei86 – 8614-carboxyglutamate By similarity
Disulfide bondi97 ↔ 108 By similarity
Glycosylationi99 – 991O-linked (Glc...); alternate By similarity
Glycosylationi99 – 991O-linked (Xyl...); alternate By similarity
Disulfide bondi102 ↔ 117 By similarity
Modified residuei110 – 1101(3R)-3-hydroxyaspartate By similarity
Modified residuei114 – 1141Phosphoserine By similarity
Disulfide bondi119 ↔ 128 By similarity
Disulfide bondi134 ↔ 145 By similarity
Disulfide bondi141 ↔ 155 By similarity
Disulfide bondi157 ↔ 170 By similarity
Disulfide bondi178 ↔ 345 By similarity
Modified residuei202 – 2021Sulfotyrosine By similarity
Glycosylationi204 – 2041N-linked (GlcNAc...) Reviewed prediction
Modified residuei205 – 2051Phosphoserine By similarity
Glycosylationi206 – 2061O-linked (GalNAc...) By similarity
Glycosylationi223 – 2231N-linked (GlcNAc...) Reviewed prediction
Glycosylationi225 – 2251O-linked (GalNAc...) By similarity
Disulfide bondi262 ↔ 278 By similarity
Disulfide bondi392 ↔ 406 By similarity
Disulfide bondi417 ↔ 445 By similarity

Post-translational modificationi

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.
Predominantly O-glucosylated at Ser-99 by POGLUT1 By similarity.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

MaxQBiP16294.
PaxDbiP16294.
PRIDEiP16294.

PTM databases

PhosphoSiteiP16294.

Expressioni

Tissue specificityi

Synthesized primarily in the liver and secreted in plasma.

Gene expression databases

ArrayExpressiP16294.
BgeeiP16294.
CleanExiMM_F9.
GenevestigatoriP16294.

Interactioni

Subunit structurei

Heterodimer of a light chain and a heavy chain; disulfide-linked.

Structurei

3D structure databases

ProteinModelPortaliP16294.
SMRiP16294. Positions 47-192, 237-470.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 9246Gla
Add
BLAST
Domaini93 – 12937EGF-like 1; calcium-binding Reviewed prediction
Add
BLAST
Domaini130 – 17142EGF-like 2
Add
BLAST
Domaini237 – 469233Peptidase S1
Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the peptidase S1 family.
Contains 2 EGF-like domains.

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00750000117249.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP16294.
KOiK01321.
OMAiSAECTVF.
OrthoDBiEOG75B84T.
PhylomeDBiP16294.
TreeFamiTF327329.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
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]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16294-1 [UniParc]FASTAAdd to Basket

« Hide

MKHLNTVMAE SPALITIFLL GYLLSTECAV FLDRENATKI LTRPKRYNSG    50
KLEEFVRGNL ERECIEERCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN 100
PCLNGGICKD DISSYECWCQ VGFEGRNCEL DATCNIKNGR CKQFCKNSPD 150
NKVICSCTEG YQLAEDQKSC EPTVPFPCGR ASISYSSKKI TRAETVFSNM 200
DYENSTEAVF IQDDITDGAI LNNVTESSES LNDFTRVVGG ENAKPGQIPW 250
QVILNGEIEA FCGGAIINEK WIVTAAHCLK PGDKIEVVAG EYNIDKKEDT 300
EQRRNVIRTI PHHQYNATIN KYSHDIALLE LDKPLILNSY VTPICVANRE 350
YTNIFLKFGS GYVSGWGKVF NKGRQASILQ YLRVPLVDRA TCLRSTTFTI 400
YNNMFCAGYR EGGKDSCEGD SGGPHVTEVE GTSFLTGIIS WGEECAMKGK 450
YGIYTKVSRY VNWIKEKTKL T 471
Length:471
Mass (Da):52,978
Last modified:January 9, 2007 - v3
Checksum:i05E08E86622397E2
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti375 – 3751Q → H in AAA37629. 1 Publication
Sequence conflicti400 – 4001I → T in AAA37629. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK149372 mRNA. Translation: BAE28840.1.
M23109 mRNA. Translation: AAA37629.1.
M26236 mRNA. Translation: AAA37630.1.
CCDSiCCDS30158.1.
PIRiJQ0419.
RefSeqiNP_032005.1. NM_007979.1.
UniGeneiMm.391283.

Genome annotation databases

EnsembliENSMUST00000033477; ENSMUSP00000033477; ENSMUSG00000031138.
GeneIDi14071.
KEGGimmu:14071.
UCSCiuc009thw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK149372 mRNA. Translation: BAE28840.1 .
M23109 mRNA. Translation: AAA37629.1 .
M26236 mRNA. Translation: AAA37630.1 .
CCDSi CCDS30158.1.
PIRi JQ0419.
RefSeqi NP_032005.1. NM_007979.1.
UniGenei Mm.391283.

3D structure databases

ProteinModelPortali P16294.
SMRi P16294. Positions 47-192, 237-470.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S01.214.

PTM databases

PhosphoSitei P16294.

Proteomic databases

MaxQBi P16294.
PaxDbi P16294.
PRIDEi P16294.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033477 ; ENSMUSP00000033477 ; ENSMUSG00000031138 .
GeneIDi 14071.
KEGGi mmu:14071.
UCSCi uc009thw.1. mouse.

Organism-specific databases

CTDi 2158.
MGIi MGI:88384. F9.

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00750000117249.
HOGENOMi HOG000251821.
HOVERGENi HBG013304.
InParanoidi P16294.
KOi K01321.
OMAi SAECTVF.
OrthoDBi EOG75B84T.
PhylomeDBi P16294.
TreeFami TF327329.

Miscellaneous databases

NextBioi 285068.
PROi P16294.
SOURCEi Search...

Gene expression databases

ArrayExpressi P16294.
Bgeei P16294.
CleanExi MM_F9.
Genevestigatori P16294.

Family and domain databases

Gene3Di 4.10.740.10. 1 hit.
InterProi IPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
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 ]
Pfami PF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PIRSFi PIRSF001143. Factor_X. 1 hit.
PRINTSi PR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTi SM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEi PS00010. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiFA9_MOUSE
AccessioniPrimary (citable) accession number: P16294
Secondary accession number(s): Q3UES1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 9, 2007
Last modified: July 9, 2014
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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