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P30558

- PAR1_MOUSE

UniProt

P30558 - PAR1_MOUSE

Protein

Proteinase-activated receptor 1

Gene

F2r

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei41 – 422Cleavage; by thrombinBy similarity

    GO - Molecular functioni

    1. G-protein alpha-subunit binding Source: UniProtKB
    2. G-protein beta-subunit binding Source: UniProtKB
    3. G-protein coupled receptor activity Source: UniProtKB
    4. heterotrimeric G-protein binding Source: UniProtKB
    5. thrombin receptor activity Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    2. activation of MAPKK activity Source: UniProtKB
    3. connective tissue replacement involved in inflammatory response wound healing Source: UniProtKB
    4. death Source: MGI
    5. establishment of synaptic specificity at neuromuscular junction Source: UniProtKB
    6. homeostasis of number of cells within a tissue Source: MGI
    7. inflammatory response Source: MGI
    8. negative regulation of cell proliferation Source: UniProtKB
    9. negative regulation of glomerular filtration Source: UniProtKB
    10. negative regulation of neuron apoptotic process Source: UniProtKB
    11. negative regulation of renin secretion into blood stream Source: UniProtKB
    12. platelet activation Source: UniProtKB
    13. positive regulation of blood coagulation Source: MGI
    14. positive regulation of calcium ion transport Source: UniProtKB
    15. positive regulation of cell migration Source: UniProtKB
    16. positive regulation of cell proliferation Source: UniProtKB
    17. positive regulation of collagen biosynthetic process Source: UniProtKB
    18. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    19. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
    20. positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: UniProtKB
    21. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    22. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    23. positive regulation of interleukin-6 secretion Source: UniProtKB
    24. positive regulation of interleukin-8 secretion Source: UniProtKB
    25. positive regulation of JAK-STAT cascade Source: UniProtKB
    26. positive regulation of MAPK cascade Source: UniProtKB
    27. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    28. positive regulation of release of sequestered calcium ion into cytosol Source: UniProtKB
    29. positive regulation of Rho protein signal transduction Source: UniProtKB
    30. positive regulation of smooth muscle contraction Source: UniProtKB
    31. positive regulation of transcription, DNA-templated Source: UniProtKB
    32. positive regulation of vasoconstriction Source: UniProtKB
    33. protein kinase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
    34. regulation of interleukin-1 beta production Source: MGI
    35. regulation of sensory perception of pain Source: UniProtKB
    36. release of sequestered calcium ion into cytosol Source: UniProtKB
    37. response to lipopolysaccharide Source: MGI
    38. response to wounding Source: UniProtKB
    39. STAT protein import into nucleus Source: UniProtKB
    40. thrombin receptor signaling pathway Source: MGI
    41. tyrosine phosphorylation of STAT protein Source: UniProtKB

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Enzyme and pathway databases

    ReactomeiREACT_207651. G alpha (q) signalling events.
    REACT_220322. Thrombin signalling through proteinase activated receptors (PARs).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteinase-activated receptor 1
    Short name:
    PAR-1
    Alternative name(s):
    Thrombin receptor
    Gene namesi
    Name:F2r
    Synonyms:Cf2r, Par1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:101802. F2r.

    Subcellular locationi

    GO - Cellular componenti

    1. caveola Source: UniProtKB
    2. integral component of membrane Source: UniProtKB-KW
    3. neuromuscular junction Source: UniProtKB
    4. plasma membrane Source: UniProtKB
    5. platelet dense tubular network Source: UniProtKB
    6. postsynaptic membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121By similarityAdd
    BLAST
    Propeptidei22 – 4120Removed for receptor activationBy similarityPRO_0000012742Add
    BLAST
    Chaini42 – 430389Proteinase-activated receptor 1PRO_0000012743Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi67 – 671N-linked (GlcNAc...)1 Publication
    Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi180 ↔ 259PROSITE-ProRule annotation
    Glycosylationi255 – 2551N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.
    Phosphorylated in the C-terminal tail; probably mediating desensitization prior to the uncoupling and internalization of the receptor.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiP30558.

    PTM databases

    PhosphoSiteiP30558.

    Expressioni

    Gene expression databases

    BgeeiP30558.
    CleanExiMM_F2R.
    GenevestigatoriP30558.

    Structurei

    3D structure databases

    ProteinModelPortaliP30558.
    SMRiP30558. Positions 73-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini42 – 10766ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini134 – 1429CytoplasmicSequence Analysis
    Topological domaini163 – 18119ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini204 – 22320CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini245 – 27329ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini294 – 31623CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini340 – 35415ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini380 – 43051CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei108 – 13326Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei143 – 16220Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei182 – 20322Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei224 – 24421Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei274 – 29320Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei317 – 33923Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei355 – 37925Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi60 – 656Asp/Glu-rich (acidic)
    Compositional biasi88 – 914Poly-Pro

    Domaini

    The cleaved signal peptide may not be degraded and may function as an intracellular angiogenesis inhibitor peptide known as parstatin.By similarity

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG150457.
    GeneTreeiENSGT00660000095329.
    HOGENOMiHOG000232200.
    HOVERGENiHBG108233.
    InParanoidiP30558.
    KOiK03914.
    OMAiVHYLFLS.
    OrthoDBiEOG7V49ZD.
    PhylomeDBiP30558.
    TreeFamiTF330775.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR003912. Protea_act_rcpt.
    IPR000935. Thrmbn_rcpt.
    [Graphical view]
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00237. GPCRRHODOPSN.
    PR01428. PROTEASEAR.
    PR00908. THROMBINR.
    PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P30558-1 [UniParc]FASTAAdd to Basket

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    MGPRRLLIVA LGLSLCGPLL SSRVPMSQPE SERTDATVNP RSFFLRNPSE    50
    NTFELVPLGD EEEEEKNESV LLEGRAVYLN ISLPPHTPPP PFISEDASGY 100
    LTSPWLTLFM PSVYTIVFIV SLPLNVLAIA VFVLRMKVKK PAVVYMLHLA 150
    MADVLFVSVL PFKISYYFSG TDWQFGSGMC RFATAAFYGN MYASIMLMTV 200
    ISIDRFLAVV YPIQSLSWRT LGRANFTCVV IWVMAIMGVV PLLLKEQTTR 250
    VPGLNITTCH DVLSENLMQG FYSYYFSAFS AIFFLVPLIV STVCYTSIIR 300
    CLSSSAVANR SKKSRALFLS AAVFCIFIVC FGPTNVLLIV HYLFLSDSPG 350
    TEAAYFAYLL CVCVSSVSCC IDPLIYYYAS SECQRHLYSI LCCKESSDPN 400
    SCNSTGQLMP SKMDTCSSHL NNSIYKKLLA 430
    Length:430
    Mass (Da):47,790
    Last modified:November 1, 1997 - v2
    Checksum:i395FD64FAE52C9BF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1621F → S in AAA40438. 1 PublicationCurated
    Sequence conflicti189 – 1891G → Y in AAA40438. 1 PublicationCurated
    Sequence conflicti223 – 2231R → G in AAA40438. 1 PublicationCurated
    Sequence conflicti262 – 2621V → L in AAA40438. 1 PublicationCurated
    Sequence conflicti365 – 3651S → T in AAA40438. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L03529 mRNA. Translation: AAA40438.1.
    U36757, U36756 Genomic DNA. Translation: AAB38308.1.
    AK085990 mRNA. Translation: BAC39587.1.
    AK159282 mRNA. Translation: BAE34960.1.
    AK160032 mRNA. Translation: BAE35575.1.
    BC031516 mRNA. Translation: AAH31516.1.
    AH003565 Genomic DNA. Translation: AAB00198.1.
    CCDSiCCDS26701.1.
    RefSeqiNP_034299.2. NM_010169.3.
    UniGeneiMm.24816.

    Genome annotation databases

    EnsembliENSMUST00000059193; ENSMUSP00000061754; ENSMUSG00000048376.
    GeneIDi14062.
    KEGGimmu:14062.
    UCSCiuc007rmn.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L03529 mRNA. Translation: AAA40438.1 .
    U36757 , U36756 Genomic DNA. Translation: AAB38308.1 .
    AK085990 mRNA. Translation: BAC39587.1 .
    AK159282 mRNA. Translation: BAE34960.1 .
    AK160032 mRNA. Translation: BAE35575.1 .
    BC031516 mRNA. Translation: AAH31516.1 .
    AH003565 Genomic DNA. Translation: AAB00198.1 .
    CCDSi CCDS26701.1.
    RefSeqi NP_034299.2. NM_010169.3.
    UniGenei Mm.24816.

    3D structure databases

    ProteinModelPortali P30558.
    SMRi P30558. Positions 73-393.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    GuidetoPHARMACOLOGYi 347.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P30558.

    Proteomic databases

    PRIDEi P30558.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000059193 ; ENSMUSP00000061754 ; ENSMUSG00000048376 .
    GeneIDi 14062.
    KEGGi mmu:14062.
    UCSCi uc007rmn.1. mouse.

    Organism-specific databases

    CTDi 2149.
    MGIi MGI:101802. F2r.

    Phylogenomic databases

    eggNOGi NOG150457.
    GeneTreei ENSGT00660000095329.
    HOGENOMi HOG000232200.
    HOVERGENi HBG108233.
    InParanoidi P30558.
    KOi K03914.
    OMAi VHYLFLS.
    OrthoDBi EOG7V49ZD.
    PhylomeDBi P30558.
    TreeFami TF330775.

    Enzyme and pathway databases

    Reactomei REACT_207651. G alpha (q) signalling events.
    REACT_220322. Thrombin signalling through proteinase activated receptors (PARs).

    Miscellaneous databases

    NextBioi 285032.
    PROi P30558.
    SOURCEi Search...

    Gene expression databases

    Bgeei P30558.
    CleanExi MM_F2R.
    Genevestigatori P30558.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR003912. Protea_act_rcpt.
    IPR000935. Thrmbn_rcpt.
    [Graphical view ]
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00237. GPCRRHODOPSN.
    PR01428. PROTEASEAR.
    PR00908. THROMBINR.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of cDNA for the mouse thrombin receptor."
      Coughlin S.R.
      Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Conserved structure and adjacent location of the thrombin receptor and protease-activated receptor 2 genes define a protease-activated receptor gene cluster."
      Kahn M.L., Ishii K., Kuo W.L., Piper M., Connolly A.J., Shi Y.P., Wu R., Lin C.C., Coughlin S.R.
      Mol. Med. 2:349-357(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Heart.
    4. "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: Mammary gland.
    5. "Structure and localization of the thrombin receptor gene on mouse chromosome 13."
      Xue J., Jenkins N.A., Gilbert D.J., Copeland N.G., Sadler J.E.
      Mamm. Genome 7:625-626(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74.
      Strain: 129/Sv.
    6. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-67.

    Entry informationi

    Entry nameiPAR1_MOUSE
    AccessioniPrimary (citable) accession number: P30558
    Secondary accession number(s): P97507, Q3TVP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 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. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3