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Protein

Prothrombin

Gene

F2

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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.UniRule annotation

Catalytic activityi

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

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. serine-type endopeptidase activity Source: Ensembl
  3. thrombospondin receptor activity Source: Ensembl

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protease, Serine proteaseUniRule annotationSAAS annotation

Keywords - Biological processi

Acute phaseUniRule annotation, Blood coagulationUniRule annotation, Hemostasis

Keywords - Ligandi

CalciumSAAS annotation

Enzyme and pathway databases

ReactomeiREACT_229844. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
REACT_232417. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
REACT_232913. Intrinsic Pathway.
REACT_234191. Cell surface interactions at the vascular wall.
REACT_237710. Gamma-carboxylation of protein precursors.
REACT_248858. Platelet Aggregation (Plug Formation).
REACT_250028. Peptide ligand-binding receptors.
REACT_250882. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
REACT_262448. Thrombin signalling through proteinase activated receptors (PARs).
REACT_262871. Common Pathway.
REACT_263374. G alpha (q) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
ProthrombinUniRule annotation (EC:3.4.21.5UniRule annotation)
Alternative name(s):
Coagulation factor IIUniRule annotation
Gene namesi
Name:F2Imported
ORF Names:rCG_27251Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 3

Organism-specific databases

RGDi61996. F2.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Keywords - PTMi

Disulfide bondSAAS annotation

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S1 family.UniRule annotation
Contains Gla (gamma-carboxy-glutamate) domain.SAAS annotation
Contains peptidase S1 domain.SAAS annotation

Keywords - Domaini

KringleSAAS annotation, RepeatSAAS annotation

Phylogenomic databases

GeneTreeiENSGT00760000118890.
KOiK01313.
OMAiGIECQLW.
OrthoDBiEOG767394.
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.

G3V843-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHVRGLGLP GCLALAALAS LVHSQHVFLA PQQALSLLQR VRRANSGFLE
60 70 80 90 100
ELRKGNLERE CVEEQCSYEE AFEALESPQD TDVFWAKYTV CDSVRKPRET
110 120 130 140 150
FMDCLEGRCA MDLGLNYHGN VSVTHTGIEC QLWRSRYPHR PDINSTTHPG
160 170 180 190 200
ADLKENFCRN PDSSTSGPWC YTTDPTVRRE ECSIPVCGQE GRTTVKMTPR
210 220 230 240 250
SRGSKENLSP PLGECLLERG RLYQGNLAVT TLGSPCLAWD SLPTKTLSKY
260 270 280 290 300
QNFDPEVKLV QNFCRNPDRD EEGAWCFVAQ QPGFEYCSLN YCDEAVGEEN
310 320 330 340 350
HDGDESIAGR TTDAEFHTFF DERTFGLGEA DCGLRPLFEK KSLTDKTEKE
360 370 380 390 400
LLDSYIDGRI VEGWDAEKGI APWQVMLFRK SPQELLCGAS LISDRWVLTA
410 420 430 440 450
AHCILYPPWD KNFTENDLLV RIGKHSRTRY ERNVEKISML EKIYIHPRYN
460 470 480 490 500
WRENLDRDIA LLKLKKPVPF SDYIHPVCLP DKQTVTSLLQ AGYKGRVTGW
510 520 530 540 550
GNLRETWTTN INEIQPSVLQ VVNLPIVERP VCKASTRIRI TDNMFCAGFK
560 570 580 590 600
VNDTKRGDAC EGDSGGPFVM KSPYNHRWYQ MGIVSWGEGC DRNGKYGFYT
610
HVFRLKRWMQ KVIDQHR
Length:617
Mass (Da):70,386
Last modified:November 16, 2011 - v1
Checksum:i8C11117828B20AC0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06024739 Genomic DNA. No translation available.
CH473949 Genomic DNA. Translation: EDL79531.1.
RefSeqiNP_075213.2. NM_022924.2.
UniGeneiRn.54498.

Genome annotation databases

EnsembliENSRNOT00000022233; ENSRNOP00000022233; ENSRNOG00000016325.
GeneIDi29251.
KEGGirno:29251.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06024739 Genomic DNA. No translation available.
CH473949 Genomic DNA. Translation: EDL79531.1.
RefSeqiNP_075213.2. NM_022924.2.
UniGeneiRn.54498.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022233; ENSRNOP00000022233; ENSRNOG00000016325.
GeneIDi29251.
KEGGirno:29251.

Organism-specific databases

CTDi2147.
RGDi61996. F2.

Phylogenomic databases

GeneTreeiENSGT00760000118890.
KOiK01313.
OMAiGIECQLW.
OrthoDBiEOG767394.
TreeFamiTF327329.

Enzyme and pathway databases

ReactomeiREACT_229844. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
REACT_232417. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
REACT_232913. Intrinsic Pathway.
REACT_234191. Cell surface interactions at the vascular wall.
REACT_237710. Gamma-carboxylation of protein precursors.
REACT_248858. Platelet Aggregation (Plug Formation).
REACT_250028. Peptide ligand-binding receptors.
REACT_250882. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
REACT_262448. Thrombin signalling through proteinase activated receptors (PARs).
REACT_262871. Common Pathway.
REACT_263374. G alpha (q) signalling events.

Miscellaneous databases

NextBioi608542.
PROiG3V843.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Ensembl
    Submitted (SEP-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiG3V843_RAT
AccessioniPrimary (citable) accession number: G3V843
Entry historyi
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: March 4, 2015
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.