Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P19221

- THRB_MOUSE

UniProt

P19221 - THRB_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Prothrombin

Gene

F2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. serine-type endopeptidase activity Source: MGI
  4. 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
Complete GO annotation...

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.
REACT_235286. Peptide ligand-binding receptors.
REACT_235886. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
REACT_239392. Intrinsic Pathway.
REACT_245393. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
REACT_249309. Platelet Aggregation (Plug Formation).
REACT_254191. Gamma-carboxylation of protein precursors.
REACT_255710. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
REACT_259461. Common Pathway.

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. blood microparticle Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

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

BgeeiP19221.
CleanExiMM_F2.
ExpressionAtlasiP19221. baseline and differential.
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 – 3264Combined sources
Turni331 – 3344Combined sources
Turni337 – 3393Combined sources
Helixi340 – 3423Combined sources
Helixi349 – 3546Combined sources
Beta strandi375 – 3806Combined sources
Turni381 – 3844Combined sources
Beta strandi385 – 40016Combined sources
Helixi402 – 4043Combined sources
Helixi408 – 4103Combined sources
Helixi416 – 4183Combined sources
Beta strandi419 – 4246Combined sources
Beta strandi427 – 4304Combined sources
Turni433 – 4353Combined sources
Beta strandi437 – 44610Combined sources
Turni452 – 4543Combined sources
Beta strandi461 – 4677Combined sources
Helixi483 – 4897Combined sources
Beta strandi495 – 5006Combined sources
Beta strandi504 – 5074Combined sources
Helixi512 – 5154Combined sources
Beta strandi521 – 5277Combined sources
Helixi530 – 5356Combined sources
Beta strandi545 – 5484Combined sources
Beta strandi554 – 5563Combined sources
Helixi562 – 5643Combined sources
Beta strandi568 – 5725Combined sources
Turni574 – 5763Combined sources
Beta strandi579 – 5879Combined sources
Helixi591 – 5933Combined sources
Beta strandi596 – 6027Combined sources
Helixi604 – 6063Combined sources
Helixi607 – 61711Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 81-618.
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

        10         20         30         40         50
MSHVRGLGLP GCLALAALVS LVHSQHVFLA PQQALSLLQR VRRANSGFLE
60 70 80 90 100
ELRKGNLERE CVEEQCSYEE AFEALESPQD TDVFWAKYTV CDSVRKPRET
110 120 130 140 150
FMDCLEGRCA MDLGVNYLGT VNVTHTGIQC QLWRSRYPHK PEINSTTHPG
160 170 180 190 200
ADLKENFCRN PDSSTTGPWC YTTDPTVRRE ECSVPVCGQE GRTTVVMTPR
210 220 230 240 250
SGGSKDNLSP PLGQCLTERG RLYQGNLAVT TLGSPCLPWN SLPAKTLSKY
260 270 280 290 300
QDFDPEVKLV ENFCRNPDWD EEGAWCYVAG QPGDFEYCNL NYCEEAVGEE
310 320 330 340 350
NYDVDESIAG RTTDAEFHTF FNEKTFGLGE ADCGLRPLFE KKSLKDTTEK
360 370 380 390 400
ELLDSYIDGR IVEGWDAEKG IAPWQVMLFR KSPQELLCGA SLISDRWVLT
410 420 430 440 450
AAHCILYPPW DKNFTENDLL VRIGKHSRTR YERNVEKISM LEKIYVHPRY
460 470 480 490 500
NWRENLDRDI ALLKLKKPVP FSDYIHPVCL PDKQTVTSLL RAGYKGRVTG
510 520 530 540 550
WGNLRETWTT NINEIQPSVL QVVNLPIVER PVCKASTRIR ITDNMFCAGF
560 570 580 590 600
KVNDTKRGDA CEGDSGGPFV MKSPFNNRWY QMGIVSWGEG CDRKGKYGFY
610
THVFRLKRWI QKVIDQFG
Length:618
Mass (Da):70,269
Last modified:November 1, 1990 - v1
Checksum:iB89F719AAFD601E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 81-618.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

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

Chemistry

BindingDBi P19221.
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.
REACT_235286. Peptide ligand-binding receptors.
REACT_235886. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
REACT_239392. Intrinsic Pathway.
REACT_245393. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
REACT_249309. Platelet Aggregation (Plug Formation).
REACT_254191. Gamma-carboxylation of protein precursors.
REACT_255710. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
REACT_259461. Common Pathway.

Miscellaneous databases

EvolutionaryTracei P19221.
NextBioi 285028.
PMAP-CutDB P19221.
PROi P19221.
SOURCEi Search...

Gene expression databases

Bgeei P19221.
CleanExi MM_F2.
ExpressionAtlasi P19221. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 160 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