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P19221

- THRB_MOUSE

UniProt

P19221 - THRB_MOUSE

Protein

Prothrombin

Gene

F2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing By similarity.By similarity

    Catalytic activityi

    Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.

    Enzyme regulationi

    Inhibited by SERPINA5.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei200 – 2012Cleavage; by thrombin
    Sitei324 – 3252Cleavage; by factor Xa
    Sitei360 – 3612Cleavage; by factor Xa
    Active sitei403 – 4031Charge relay systemBy similarity
    Active sitei459 – 4591Charge relay systemBy similarity
    Active sitei565 – 5651Charge relay systemBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. peptidase activity Source: MGI
    3. protein binding Source: MGI
    4. serine-type endopeptidase activity Source: MGI
    5. thrombospondin receptor activity Source: Ensembl

    GO - Biological processi

    1. acute-phase response Source: UniProtKB-KW
    2. cytosolic calcium ion homeostasis Source: Ensembl
    3. fibrinolysis Source: Ensembl
    4. negative regulation of astrocyte differentiation Source: Ensembl
    5. negative regulation of proteolysis Source: Ensembl
    6. platelet activation Source: MGI
    7. positive regulation of blood coagulation Source: Ensembl
    8. positive regulation of cell growth Source: MGI
    9. positive regulation of cell proliferation Source: MGI
    10. positive regulation of collagen biosynthetic process Source: Ensembl
    11. positive regulation of phosphatidylinositol 3-kinase signaling Source: MGI
    12. positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway Source: Ensembl
    13. positive regulation of protein phosphorylation Source: Ensembl
    14. positive regulation of reactive oxygen species metabolic process Source: Ensembl
    15. positive regulation of release of sequestered calcium ion into cytosol Source: Ensembl
    16. regulation of cell shape Source: MGI
    17. regulation of gene expression Source: MGI
    18. thrombin receptor signaling pathway Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Acute phase, Blood coagulation, Hemostasis

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_207651. G alpha (q) signalling events.
    REACT_220322. Thrombin signalling through proteinase activated receptors (PARs).
    REACT_225233. Cell surface interactions at the vascular wall.

    Protein family/group databases

    MEROPSiS01.217.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prothrombin (EC:3.4.21.5)
    Alternative name(s):
    Coagulation factor II
    Cleaved into the following 4 chains:
    Gene namesi
    Name:F2
    Synonyms:Cf2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:88380. F2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: Ensembl

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi565 – 5651S → A: Loss of protease activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Propeptidei25 – 4319PRO_0000028165Add
    BLAST
    Chaini44 – 618575ProthrombinPRO_0000028166Add
    BLAST
    Peptidei44 – 200157Activation peptide fragment 1PRO_0000028167Add
    BLAST
    Peptidei201 – 324124Activation peptide fragment 2PRO_0000028168Add
    BLAST
    Chaini325 – 36036Thrombin light chainPRO_0000028169Add
    BLAST
    Chaini361 – 618258Thrombin heavy chainPRO_0000028170Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei50 – 5014-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei51 – 5114-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei58 – 5814-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei60 – 6014-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Disulfide bondi61 ↔ 66By similarity
    Modified residuei63 – 6314-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei64 – 6414-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei69 – 6914-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei70 – 7014-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei73 – 7314-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei76 – 7614-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Disulfide bondi91 ↔ 104By similarity
    Disulfide bondi109 ↔ 187By similarity
    Glycosylationi122 – 1221N-linked (GlcNAc...)1 Publication
    Disulfide bondi130 ↔ 170By similarity
    Glycosylationi144 – 1441N-linked (GlcNAc...)
    Disulfide bondi158 ↔ 182By similarity
    Disulfide bondi215 ↔ 293By similarity
    Disulfide bondi236 ↔ 276By similarity
    Disulfide bondi264 ↔ 288By similarity
    Disulfide bondi333 ↔ 479Interchain (between light and heavy chains)PROSITE-ProRule annotation
    Disulfide bondi388 ↔ 4041 Publication
    Glycosylationi413 – 4131N-linked (GlcNAc...)1 Publication
    Disulfide bondi533 ↔ 5471 Publication
    Glycosylationi553 – 5531N-linked (GlcNAc...)1 Publication
    Disulfide bondi561 ↔ 5911 Publication

    Post-translational modificationi

    The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin.1 Publication

    Keywords - PTMi

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

    Proteomic databases

    MaxQBiP19221.
    PaxDbiP19221.
    PRIDEiP19221.

    PTM databases

    PhosphoSiteiP19221.

    Miscellaneous databases

    PMAP-CutDBP19221.

    Expressioni

    Gene expression databases

    ArrayExpressiP19221.
    BgeeiP19221.
    CleanExiMM_F2.
    GenevestigatoriP19221.

    Interactioni

    Subunit structurei

    Heterodimer (named alpha-thrombin) of a light and a heavy chain; disulfide-linked. Forms a heterodimer with SERPINA5 By similarity.By similarity

    Protein-protein interaction databases

    DIPiDIP-60968N.
    IntActiP19221. 3 interactions.
    MINTiMINT-4137721.
    STRINGi10090.ENSMUSP00000028681.

    Structurei

    Secondary structure

    1
    618
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi323 – 3264
    Turni331 – 3344
    Turni337 – 3393
    Helixi340 – 3423
    Helixi349 – 3546
    Beta strandi375 – 3806
    Turni381 – 3844
    Beta strandi385 – 40016
    Helixi402 – 4043
    Helixi408 – 4103
    Helixi416 – 4183
    Beta strandi419 – 4246
    Beta strandi427 – 4304
    Turni433 – 4353
    Beta strandi437 – 44610
    Turni452 – 4543
    Beta strandi461 – 4677
    Helixi483 – 4897
    Beta strandi495 – 5006
    Beta strandi504 – 5074
    Helixi512 – 5154
    Beta strandi521 – 5277
    Helixi530 – 5356
    Beta strandi545 – 5484
    Beta strandi554 – 5563
    Helixi562 – 5643
    Beta strandi568 – 5725
    Turni574 – 5763
    Beta strandi579 – 5879
    Helixi591 – 5933
    Beta strandi596 – 6027
    Helixi604 – 6063
    Helixi607 – 61711

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OCVX-ray2.20A319-346[»]
    B361-618[»]
    2PUXX-ray2.00A317-360[»]
    B361-618[»]
    2PV9X-ray3.50A317-360[»]
    B361-618[»]
    3EDXX-ray2.40A/C/E317-360[»]
    B/D/F361-618[»]
    3HK3X-ray1.94A317-360[»]
    B361-618[»]
    3HK6X-ray3.20A/C317-360[»]
    B/D361-618[»]
    3HKIX-ray2.20A/D317-360[»]
    B/E361-618[»]
    ProteinModelPortaliP19221.
    SMRiP19221. Positions 44-618.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19221.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini44 – 9047GlaPROSITE-ProRule annotationAdd
    BLAST
    Domaini109 – 18779Kringle 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini215 – 29278Kringle 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini361 – 615255Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni548 – 57023High affinity receptor-binding region which is also known as the TP508 peptideBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
    Contains 2 kringle domains.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Kringle, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    HOGENOMiHOG000251824.
    HOVERGENiHBG108381.
    InParanoidiP19221.
    KOiK01313.
    OMAiGIECQLW.
    PhylomeDBiP19221.
    TreeFamiTF327329.

    Family and domain databases

    Gene3Di2.40.20.10. 2 hits.
    4.10.140.10. 1 hit.
    4.10.740.10. 1 hit.
    InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
    IPR000294. GLA_domain.
    IPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR003966. Prothrombin/thrombin.
    IPR018992. Thrombin_light_chain.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00594. Gla. 1 hit.
    PF00051. Kringle. 2 hits.
    PF09396. Thrombin_light. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001149. Thrombin. 1 hit.
    PRINTSiPR00722. CHYMOTRYPSIN.
    PR00001. GLABLOOD.
    PR01505. PROTHROMBIN.
    SMARTiSM00069. GLA. 1 hit.
    SM00130. KR. 2 hits.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 2 hits.
    SSF57630. SSF57630. 1 hit.
    PROSITEiPS00011. GLA_1. 1 hit.
    PS50998. GLA_2. 1 hit.
    PS00021. KRINGLE_1. 2 hits.
    PS50070. KRINGLE_2. 2 hits.
    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.

    P19221-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHVRGLGLP GCLALAALVS LVHSQHVFLA PQQALSLLQR VRRANSGFLE    50
    ELRKGNLERE CVEEQCSYEE AFEALESPQD TDVFWAKYTV CDSVRKPRET 100
    FMDCLEGRCA MDLGVNYLGT VNVTHTGIQC QLWRSRYPHK PEINSTTHPG 150
    ADLKENFCRN PDSSTTGPWC YTTDPTVRRE ECSVPVCGQE GRTTVVMTPR 200
    SGGSKDNLSP PLGQCLTERG RLYQGNLAVT TLGSPCLPWN SLPAKTLSKY 250
    QDFDPEVKLV ENFCRNPDWD EEGAWCYVAG QPGDFEYCNL NYCEEAVGEE 300
    NYDVDESIAG RTTDAEFHTF FNEKTFGLGE ADCGLRPLFE KKSLKDTTEK 350
    ELLDSYIDGR IVEGWDAEKG IAPWQVMLFR KSPQELLCGA SLISDRWVLT 400
    AAHCILYPPW DKNFTENDLL VRIGKHSRTR YERNVEKISM LEKIYVHPRY 450
    NWRENLDRDI ALLKLKKPVP FSDYIHPVCL PDKQTVTSLL RAGYKGRVTG 500
    WGNLRETWTT NINEIQPSVL QVVNLPIVER PVCKASTRIR ITDNMFCAGF 550
    KVNDTKRGDA CEGDSGGPFV MKSPFNNRWY QMGIVSWGEG CDRKGKYGFY 600
    THVFRLKRWI QKVIDQFG 618
    Length:618
    Mass (Da):70,269
    Last modified:November 1, 1990 - v1
    Checksum:iB89F719AAFD601E0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52308 mRNA. Translation: CAA36548.1.
    BC013662 mRNA. Translation: AAH13662.1.
    M81394 mRNA. Translation: AAA40435.1.
    CCDSiCCDS16434.1.
    PIRiA35827.
    RefSeqiNP_034298.1. NM_010168.2.
    UniGeneiMm.89048.

    Genome annotation databases

    EnsembliENSMUST00000028681; ENSMUSP00000028681; ENSMUSG00000027249.
    GeneIDi14061.
    KEGGimmu:14061.
    UCSCiuc008kwg.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52308 mRNA. Translation: CAA36548.1 .
    BC013662 mRNA. Translation: AAH13662.1 .
    M81394 mRNA. Translation: AAA40435.1 .
    CCDSi CCDS16434.1.
    PIRi A35827.
    RefSeqi NP_034298.1. NM_010168.2.
    UniGenei Mm.89048.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OCV X-ray 2.20 A 319-346 [» ]
    B 361-618 [» ]
    2PUX X-ray 2.00 A 317-360 [» ]
    B 361-618 [» ]
    2PV9 X-ray 3.50 A 317-360 [» ]
    B 361-618 [» ]
    3EDX X-ray 2.40 A/C/E 317-360 [» ]
    B/D/F 361-618 [» ]
    3HK3 X-ray 1.94 A 317-360 [» ]
    B 361-618 [» ]
    3HK6 X-ray 3.20 A/C 317-360 [» ]
    B/D 361-618 [» ]
    3HKI X-ray 2.20 A/D 317-360 [» ]
    B/E 361-618 [» ]
    ProteinModelPortali P19221.
    SMRi P19221. Positions 44-618.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60968N.
    IntActi P19221. 3 interactions.
    MINTi MINT-4137721.
    STRINGi 10090.ENSMUSP00000028681.

    Chemistry

    ChEMBLi CHEMBL1075308.

    Protein family/group databases

    MEROPSi S01.217.

    PTM databases

    PhosphoSitei P19221.

    Proteomic databases

    MaxQBi P19221.
    PaxDbi P19221.
    PRIDEi P19221.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028681 ; ENSMUSP00000028681 ; ENSMUSG00000027249 .
    GeneIDi 14061.
    KEGGi mmu:14061.
    UCSCi uc008kwg.1. mouse.

    Organism-specific databases

    CTDi 2147.
    MGIi MGI:88380. F2.

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000251824.
    HOVERGENi HBG108381.
    InParanoidi P19221.
    KOi K01313.
    OMAi GIECQLW.
    PhylomeDBi P19221.
    TreeFami TF327329.

    Enzyme and pathway databases

    Reactomei REACT_207651. G alpha (q) signalling events.
    REACT_220322. Thrombin signalling through proteinase activated receptors (PARs).
    REACT_225233. Cell surface interactions at the vascular wall.

    Miscellaneous databases

    ChiTaRSi F2. mouse.
    EvolutionaryTracei P19221.
    NextBioi 285028.
    PMAP-CutDB P19221.
    PROi P19221.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19221.
    Bgeei P19221.
    CleanExi MM_F2.
    Genevestigatori P19221.

    Family and domain databases

    Gene3Di 2.40.20.10. 2 hits.
    4.10.140.10. 1 hit.
    4.10.740.10. 1 hit.
    InterProi IPR017857. Coagulation_fac_subgr_Gla_dom.
    IPR000294. GLA_domain.
    IPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR003966. Prothrombin/thrombin.
    IPR018992. Thrombin_light_chain.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00594. Gla. 1 hit.
    PF00051. Kringle. 2 hits.
    PF09396. Thrombin_light. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001149. Thrombin. 1 hit.
    PRINTSi PR00722. CHYMOTRYPSIN.
    PR00001. GLABLOOD.
    PR01505. PROTHROMBIN.
    SMARTi SM00069. GLA. 1 hit.
    SM00130. KR. 2 hits.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 2 hits.
    SSF57630. SSF57630. 1 hit.
    PROSITEi PS00011. GLA_1. 1 hit.
    PS50998. GLA_2. 1 hit.
    PS00021. KRINGLE_1. 2 hits.
    PS50070. KRINGLE_2. 2 hits.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the cDNA coding for mouse prothrombin and localization of the gene on mouse chromosome 2."
      Friezner Degen S.J., Schaffer L.A., Jamison C.S., Grant S.G., Fitzgibbon J.J., Pai J.-A., Chapman V.M., Elliott R.W.
      DNA Cell Biol. 9:487-498(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], GAMMA-CARBOXYGLUTAMATION AT GLU-50; GLU-51; GLU-58; GLU-60; GLU-63; GLU-64; GLU-69; GLU-70; GLU-73 AND GLU-76.
      Strain: C57BL/6.
      Tissue: Liver.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Liver.
    3. "Partial characterization of vertebrate prothrombin cDNAs: amplification and sequence analysis of the B chain of thrombin from nine different species."
      Banfield D.K., Macgillivray R.T.
      Proc. Natl. Acad. Sci. U.S.A. 89:2779-2783(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 384-618.
      Tissue: Liver.
    4. "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
      Bernhard O.K., Kapp E.A., Simpson R.J.
      J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-122; ASN-413 AND ASN-553.
      Strain: C57BL/6.
      Tissue: Plasma.
    5. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 319-618, DISULFIDE BONDS.
    6. "Crystal structures of murine thrombin in complex with the extracellular fragments of murine protease-activated receptors PAR3 and PAR4."
      Bah A., Chen Z.-W., Bush-Pelc L.A., Mathews F.S., Di Cera E.
      Proc. Natl. Acad. Sci. U.S.A. 104:11603-11608(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 317-618 OF MUTANT ALA-565 IN COMPLEXES WITH PAR3/F2RL2 AND PAR4/F2RL3, MUTAGENESIS OF SER-565.

    Entry informationi

    Entry nameiTHRB_MOUSE
    AccessioniPrimary (citable) accession number: P19221
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 158 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Prothrombin is activated on the surface of a phospholipid membrane that binds the amino end of prothrombin and factors Va and Xa in Ca-dependent interactions; factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. The activation process starts slowly because factor V itself has to be activated by the initial, small amounts of thrombin.
    Thrombin can itself cleave the N-terminal fragment (fragment 1) of the prothrombin, prior to its activation by factor Xa.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3