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Q8K3U6

- FA7_RAT

UniProt

Q8K3U6 - FA7_RAT

Protein

Coagulation factor VII

Gene

F7

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei193 – 1942Cleavage; by factor Xa, factor XIIa, factor IXa, or thrombinBy similarity
    Active sitei234 – 2341Charge relay systemBy similarity
    Active sitei283 – 2831Charge relay systemBy similarity
    Binding sitei379 – 3791SubstrateBy similarity
    Active sitei385 – 3851Charge relay systemBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. endopeptidase activity Source: RGD
    3. receptor binding Source: RGD
    4. serine-type endopeptidase activity Source: InterPro
    5. serine-type peptidase activity Source: RGD

    GO - Biological processi

    1. blood coagulation Source: RGD
    2. circadian rhythm Source: RGD
    3. organ regeneration Source: RGD
    4. positive regulation of blood coagulation Source: RGD
    5. positive regulation of leukocyte chemotaxis Source: Ensembl
    6. positive regulation of platelet-derived growth factor receptor signaling pathway Source: Ensembl
    7. positive regulation of positive chemotaxis Source: Ensembl
    8. positive regulation of protein kinase B signaling Source: Ensembl
    9. response to estrogen Source: RGD
    10. response to growth hormone Source: RGD
    11. response to hormone Source: RGD
    12. response to nutrient levels Source: RGD
    13. response to organic cyclic compound Source: RGD
    14. response to vitamin K Source: RGD

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_196405. BMAL1:CLOCK,NPAS2 activates circadian gene expression.

    Protein family/group databases

    MEROPSiS01.215.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Coagulation factor VII (EC:3.4.21.21)
    Alternative name(s):
    Serum prothrombin conversion accelerator
    Cleaved into the following 2 chains:
    Gene namesi
    Name:F7
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 16

    Organism-specific databases

    RGDi628678. F7.

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular space Source: RGD
    2. vesicle Source: RGD

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Propeptidei25 – 4117Sequence AnalysisPRO_0000027738Add
    BLAST
    Chaini42 – 193152Factor VII light chainBy similarityPRO_0000027739Add
    BLAST
    Chaini194 – 446253Factor VII heavy chainBy similarityPRO_0000027740Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei47 – 4714-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei48 – 4814-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei55 – 5514-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei57 – 5714-carboxyglutamatePROSITE-ProRule annotation
    Disulfide bondi58 ↔ 63By similarity
    Modified residuei60 – 6014-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei61 – 6114-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei67 – 6714-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei70 – 7014-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei76 – 7614-carboxyglutamatePROSITE-ProRule annotation
    Disulfide bondi91 ↔ 102By similarity
    Glycosylationi93 – 931O-linked (Glc...); alternateBy similarity
    Glycosylationi93 – 931O-linked (Xyl...); alternateBy similarity
    Disulfide bondi96 ↔ 111By similarity
    Glycosylationi101 – 1011O-linked (Fuc)By similarity
    Modified residuei104 – 1041(3R)-3-hydroxyaspartateBy similarity
    Disulfide bondi113 ↔ 122By similarity
    Disulfide bondi132 ↔ 143By similarity
    Disulfide bondi139 ↔ 153By similarity
    Disulfide bondi155 ↔ 168By similarity
    Disulfide bondi176 ↔ 303By similarity
    Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi200 ↔ 205By similarity
    Disulfide bondi219 ↔ 235By similarity
    Glycosylationi244 – 2441N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi351 ↔ 370By similarity
    Disulfide bondi381 ↔ 409By similarity

    Post-translational modificationi

    The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.By similarity
    The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity
    Can be either O-glucosylated or O-xylosylated at Ser-93 by POGLUT1.By similarity

    Keywords - PTMi

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

    Proteomic databases

    PaxDbiQ8K3U6.
    PRIDEiQ8K3U6.

    Expressioni

    Tissue specificityi

    Plasma.

    Gene expression databases

    GenevestigatoriQ8K3U6.

    Interactioni

    Subunit structurei

    Heterodimer of a light chain and a heavy chain linked by a disulfide bond.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000038466.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8K3U6.
    SMRiQ8K3U6. Positions 61-183, 194-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 8645GlaPROSITE-ProRule annotationAdd
    BLAST
    Domaini87 – 12337EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini128 – 16942EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini194 – 433240Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    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.
    GeneTreeiENSGT00750000117249.
    HOGENOMiHOG000251821.
    HOVERGENiHBG013304.
    InParanoidiQ8K3U6.
    KOiK01320.
    OMAiGCEQYCS.
    OrthoDBiEOG75B84T.
    PhylomeDBiQ8K3U6.
    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.
    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.

    Q8K3U6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVPQTHGLLL LYFLLQLQGP LGAVVFITQE EAHGVLHRQR RANSLLEELW    50
    SSSLERECNE ERCSFEEARE IFKSPERTKQ FWTIYSDGDQ CASNPCQNGG 100
    TCQDHLKSYV CFCPLDFEGR NCEKNKNEQL ICANENGDCD QYCRDHVGTK 150
    RTCSCHEDYV LQPDEVSCKP KVEYPCGRIP VVEKRNFSRP QGRIVGGYVC 200
    PKGECPWQAV LKFNEALLCG AVLLDTRWIV TAAHCFDKFG KLVNITVVLG 250
    EHDFSEKEGT EQVRLVEQVI MPNKYTRGRT DHDIALVRLH RPVTFTDYVV 300
    PLCLPERAFS ENTLASIRFS RVSGWGQLLD RGATALELMV IEVPRLMTQD 350
    CLEHAKHSAN TPRITENMFC AGYMDGTKDA CKGDSGGPHA THYHGTWYLT 400
    GVVSWGEGCA AIGHIGVYTR VSQYIDWLVK YMDSKLRVGI SRVSLL 446
    Length:446
    Mass (Da):50,399
    Last modified:October 1, 2002 - v1
    Checksum:i292985EBF119C0AA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF532184 mRNA. Translation: AAM95967.1.
    RefSeqiNP_690059.1. NM_152846.1.
    UniGeneiRn.86416.

    Genome annotation databases

    EnsembliENSRNOT00000037806; ENSRNOP00000038466; ENSRNOG00000032737.
    GeneIDi260320.
    KEGGirno:260320.
    UCSCiRGD:628678. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF532184 mRNA. Translation: AAM95967.1 .
    RefSeqi NP_690059.1. NM_152846.1.
    UniGenei Rn.86416.

    3D structure databases

    ProteinModelPortali Q8K3U6.
    SMRi Q8K3U6. Positions 61-183, 194-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000038466.

    Protein family/group databases

    MEROPSi S01.215.

    Proteomic databases

    PaxDbi Q8K3U6.
    PRIDEi Q8K3U6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000037806 ; ENSRNOP00000038466 ; ENSRNOG00000032737 .
    GeneIDi 260320.
    KEGGi rno:260320.
    UCSCi RGD:628678. rat.

    Organism-specific databases

    CTDi 2155.
    RGDi 628678. F7.

    Phylogenomic databases

    eggNOGi COG5640.
    GeneTreei ENSGT00750000117249.
    HOGENOMi HOG000251821.
    HOVERGENi HBG013304.
    InParanoidi Q8K3U6.
    KOi K01320.
    OMAi GCEQYCS.
    OrthoDBi EOG75B84T.
    PhylomeDBi Q8K3U6.
    TreeFami TF327329.

    Enzyme and pathway databases

    Reactomei REACT_196405. BMAL1:CLOCK,NPAS2 activates circadian gene expression.

    Miscellaneous databases

    NextBioi 624347.
    PROi Q8K3U6.

    Gene expression databases

    Genevestigatori Q8K3U6.

    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.
    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

    1. "Nucleotide sequence of the cDNA encoding rat coagulation factor VII."
      Murphy K., Ramaker M.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.

    Entry informationi

    Entry nameiFA7_RAT
    AccessioniPrimary (citable) accession number: Q8K3U6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 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. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3