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P16294

- FA9_MOUSE

UniProt

P16294 - FA9_MOUSE

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Protein

Coagulation factor IX

Gene

F9

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 XIaBy similarity
Sitei236 – 2372Cleavage; by factor XIaBy similarity
Active sitei277 – 2771Charge relay systemBy similarity
Active sitei325 – 3251Charge relay systemBy similarity
Active sitei421 – 4211Charge relay systemBy 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

Enzyme and pathway databases

ReactomeiREACT_239392. Intrinsic Pathway.
REACT_240293. Extrinsic Pathway.
REACT_245393. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
REACT_254191. Gamma-carboxylation of protein precursors.
REACT_255710. Removal of aminoterminal propeptides from gamma-carboxylated proteins.

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-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Propeptidei29 – 4618By similarityPRO_0000027760Add
BLAST
Chaini47 – 471425Coagulation factor IXPRO_0000027761Add
BLAST
Chaini47 – 192146Coagulation factor IXa light chainPRO_0000027762Add
BLAST
Propeptidei193 – 23644Activation peptideBy similarityPRO_0000027763Add
BLAST
Chaini237 – 471235Coagulation factor IXa heavy chainPRO_0000027764Add
BLAST

Amino acid modifications

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

BgeeiP16294.
CleanExiMM_F9.
ExpressionAtlasiP16294. baseline and differential.
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 9246GlaPROSITE-ProRule annotationAdd
BLAST
Domaini93 – 12937EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini130 – 17142EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini237 – 469233Peptidase S1PROSITE-ProRule annotationAdd
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.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118890.
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

        10         20         30         40         50
MKHLNTVMAE SPALITIFLL GYLLSTECAV FLDRENATKI LTRPKRYNSG
60 70 80 90 100
KLEEFVRGNL ERECIEERCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN
110 120 130 140 150
PCLNGGICKD DISSYECWCQ VGFEGRNCEL DATCNIKNGR CKQFCKNSPD
160 170 180 190 200
NKVICSCTEG YQLAEDQKSC EPTVPFPCGR ASISYSSKKI TRAETVFSNM
210 220 230 240 250
DYENSTEAVF IQDDITDGAI LNNVTESSES LNDFTRVVGG ENAKPGQIPW
260 270 280 290 300
QVILNGEIEA FCGGAIINEK WIVTAAHCLK PGDKIEVVAG EYNIDKKEDT
310 320 330 340 350
EQRRNVIRTI PHHQYNATIN KYSHDIALLE LDKPLILNSY VTPICVANRE
360 370 380 390 400
YTNIFLKFGS GYVSGWGKVF NKGRQASILQ YLRVPLVDRA TCLRSTTFTI
410 420 430 440 450
YNNMFCAGYR EGGKDSCEGD SGGPHVTEVE GTSFLTGIIS WGEECAMKGK
460 470
YGIYTKVSRY VNWIKEKTKL T
Length:471
Mass (Da):52,978
Last modified:January 9, 2007 - v3
Checksum:i05E08E86622397E2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti375 – 3751Q → H in AAA37629. (PubMed:2323576)Curated
Sequence conflicti400 – 4001I → T in AAA37629. (PubMed:2323576)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 ENSGT00760000118890.
HOGENOMi HOG000251821.
HOVERGENi HBG013304.
InParanoidi P16294.
KOi K01321.
OMAi SAECTVF.
OrthoDBi EOG75B84T.
PhylomeDBi P16294.
TreeFami TF327329.

Enzyme and pathway databases

Reactomei REACT_239392. Intrinsic Pathway.
REACT_240293. Extrinsic Pathway.
REACT_245393. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
REACT_254191. Gamma-carboxylation of protein precursors.
REACT_255710. Removal of aminoterminal propeptides from gamma-carboxylated proteins.

Miscellaneous databases

NextBioi 285068.
PROi P16294.
SOURCEi Search...

Gene expression databases

Bgeei P16294.
CleanExi MM_F9.
ExpressionAtlasi P16294. baseline and differential.
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: November 26, 2014
This is version 165 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