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O19045

- FA10_RABIT

UniProt

O19045 - FA10_RABIT

Protein

Coagulation factor X

Gene

F10

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.

    Catalytic activityi

    Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.

    Enzyme regulationi

    Inhibited by SERPINA5.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei274 – 2741Charge relay system
    Active sitei320 – 3201Charge relay system
    Active sitei417 – 4171Charge relay system

    GO - Molecular functioni

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

    GO - Biological processi

    1. blood coagulation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Keywords - Ligandi

    Calcium

    Protein family/group databases

    MEROPSiS01.216.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Coagulation factor X (EC:3.4.21.6)
    Alternative name(s):
    Stuart factor
    Cleaved into the following 3 chains:
    Gene namesi
    Name:F10
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 4020By similarityPRO_0000027798Add
    BLAST
    Chaini41 – 490450Coagulation factor XPRO_0000027799Add
    BLAST
    Chaini41 – 180140Factor X light chainPRO_0000027800Add
    BLAST
    Chaini184 – 490307Factor X heavy chainPRO_0000027801Add
    BLAST
    Propeptidei184 – 23249Activation peptidePRO_0000027802Add
    BLAST
    Chaini233 – 490258Activated factor Xa heavy chainPRO_0000027803Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei46 – 4614-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei47 – 4714-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei54 – 5414-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei56 – 5614-carboxyglutamatePROSITE-ProRule annotation
    Disulfide bondi57 ↔ 62By similarity
    Modified residuei59 – 5914-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei60 – 6014-carboxyglutamatePROSITE-ProRule annotation
    Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
    Modified residuei65 – 6514-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei69 – 6914-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei72 – 7214-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei75 – 7514-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei79 – 7914-carboxyglutamatePROSITE-ProRule annotation
    Disulfide bondi90 ↔ 101By similarity
    Disulfide bondi95 ↔ 110By similarity
    Modified residuei103 – 1031(3R)-3-hydroxyaspartateBy similarity
    Disulfide bondi112 ↔ 121By similarity
    Disulfide bondi129 ↔ 140By similarity
    Disulfide bondi136 ↔ 149By similarity
    Disulfide bondi151 ↔ 164By similarity
    Disulfide bondi172 ↔ 340Interchain (between light and heavy chains)PROSITE-ProRule annotation
    Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi239 ↔ 244By similarity
    Disulfide bondi259 ↔ 275By similarity
    Disulfide bondi388 ↔ 402By similarity
    Disulfide bondi413 ↔ 441By similarity

    Post-translational modificationi

    The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.By similarity
    N- and O-glycosylated.By similarity
    The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway).By similarity
    The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity

    Keywords - PTMi

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

    Interactioni

    Subunit structurei

    The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds. Forms a heterodimer with SERPINA5 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000025032.

    Structurei

    3D structure databases

    ProteinModelPortaliO19045.
    SMRiO19045. Positions 42-86, 233-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini41 – 8545GlaPROSITE-ProRule annotationAdd
    BLAST
    Domaini86 – 12237EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini125 – 16541EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini233 – 465233Peptidase 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.
    HOGENOMiHOG000251821.
    HOVERGENiHBG013304.

    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. 2 hits.
    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.

    O19045-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANPLHLVLL GAALAGLLLS GSSVFISRRA ANDVLARTRR ANSFLEELKK    50
    GNLERECMEE NCSYEEALEV FEDREKTNEF WNKYVDGDQC ESNPCQNQGT 100
    CKDGLGMYTC SCVEGYEGQD CEPVTRKLCS LDNGGCDQFC KEEENSVLCS 150
    CASGYTLGDN GKSCISTELF PCGKVTLGRW RRSPATNSSE GPPEAPGPEQ 200
    QDDGNLTATE NPFNLLDSPE PPPEDDSSSL VRIVGGQDCR DGECPWQALL 250
    VNEENEGFCG GTILSEYHVL TAAHCLHQAK RFKVRVGDRD TEHEEGNEET 300
    HEVEVVVKHN RFVKETYDFD IAVLRLKTPI TFRRNVAPAC LPQKDWAEST 350
    LMAQKTGIVS GFGRTHEMGR LSTTLKMLEV PYVDRNSCKR SSSFTITQNM 400
    FCAGYDARPE DACQGDSGGP HVTRFRDTYF VTGIVSWGEG CARKGKFGVY 450
    TKVSNFLKWI EKSMRARAVP VAEAAGTPGP TQPTIKGSPS 490
    Length:490
    Mass (Da):53,965
    Last modified:January 1, 1998 - v1
    Checksum:i3A39FA85AF2A6D11
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF003200 mRNA. Translation: AAB62542.1.
    RefSeqiNP_001075485.1. NM_001082016.1.
    UniGeneiOcu.2157.

    Genome annotation databases

    GeneIDi100008647.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF003200 mRNA. Translation: AAB62542.1 .
    RefSeqi NP_001075485.1. NM_001082016.1.
    UniGenei Ocu.2157.

    3D structure databases

    ProteinModelPortali O19045.
    SMRi O19045. Positions 42-86, 233-473.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9986.ENSOCUP00000025032.

    Chemistry

    BindingDBi O19045.
    ChEMBLi CHEMBL5062.

    Protein family/group databases

    MEROPSi S01.216.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100008647.

    Organism-specific databases

    CTDi 2159.

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000251821.
    HOVERGENi HBG013304.

    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. 2 hits.
    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

    1. "Characterization of a full-length cDNA for rabbit factor X."
      Pendurthi U.R., Anderson K.D., James H.L.
      Thromb. Res. 85:503-514(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiFA10_RABIT
    AccessioniPrimary (citable) accession number: O19045
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Calcium also binds, with stronger affinity to another site, beyond the GLA domain.

    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