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P30558 (PAR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteinase-activated receptor 1

Short name=PAR-1
Alternative name(s):
Thrombin receptor
Gene names
Name:F2r
Synonyms:Cf2r, Par1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Cell membrane; Multi-pass membrane protein.

Domain

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

Post-translational modification

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.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Biological processBlood coagulation
Hemostasis
   Cellular componentCell membrane
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSTAT protein import into nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

activation of MAPKK activity

Inferred from sequence or structural similarity. Source: UniProtKB

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

connective tissue replacement involved in inflammatory response wound healing

Inferred from sequence or structural similarity. Source: UniProtKB

death

Inferred from mutant phenotype PubMed 18305483. Source: MGI

establishment of synaptic specificity at neuromuscular junction

Inferred from sequence or structural similarity. Source: UniProtKB

homeostasis of number of cells within a tissue

Inferred from mutant phenotype PubMed 18305483. Source: MGI

inflammatory response

Inferred from mutant phenotype PubMed 18305483. Source: MGI

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of glomerular filtration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of renin secretion into blood stream

Inferred from direct assay PubMed 21859963. Source: UniProtKB

platelet activation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay PubMed 20215560. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of JAK-STAT cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of MAPK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of Rho protein signal transduction

Inferred from direct assay PubMed 20215560. Source: UniProtKB

positive regulation of blood coagulation

Inferred from mutant phenotype PubMed 18305483. Source: MGI

positive regulation of calcium ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay PubMed 20215560. Source: UniProtKB

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of collagen biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration

Inferred from direct assay PubMed 20215560. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-6 secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-8 secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from direct assay PubMed 20215560. Source: UniProtKB

positive regulation of release of sequestered calcium ion into cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of smooth muscle contraction

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of vasoconstriction

Inferred from direct assay PubMed 21859963. Source: UniProtKB

protein kinase C-activating G-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of interleukin-1 beta production

Inferred from mutant phenotype PubMed 18305483. Source: MGI

regulation of sensory perception of pain

Inferred from sequence or structural similarity. Source: UniProtKB

release of sequestered calcium ion into cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

response to lipopolysaccharide

Inferred from mutant phenotype PubMed 18305483. Source: MGI

response to wounding

Inferred from sequence or structural similarity. Source: UniProtKB

thrombin receptor signaling pathway

Inferred from genetic interaction PubMed 18398001. Source: MGI

tyrosine phosphorylation of STAT protein

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcaveola

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

neuromuscular junction

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

platelet dense tubular network

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionG-protein alpha-subunit binding

Inferred from direct assay PubMed 20215560. Source: UniProtKB

G-protein beta-subunit binding

Inferred from direct assay PubMed 20215560. Source: UniProtKB

G-protein coupled receptor activity

Inferred from mutant phenotype PubMed 20215560. Source: UniProtKB

heterotrimeric G-protein binding

Traceable author statement PubMed 20215560. Source: UniProtKB

thrombin receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 By similarity
Propeptide22 – 4120Removed for receptor activation By similarity
PRO_0000012742
Chain42 – 430389Proteinase-activated receptor 1
PRO_0000012743

Regions

Topological domain42 – 10766Extracellular Potential
Transmembrane108 – 13326Helical; Name=1; Potential
Topological domain134 – 1429Cytoplasmic Potential
Transmembrane143 – 16220Helical; Name=2; Potential
Topological domain163 – 18119Extracellular Potential
Transmembrane182 – 20322Helical; Name=3; Potential
Topological domain204 – 22320Cytoplasmic Potential
Transmembrane224 – 24421Helical; Name=4; Potential
Topological domain245 – 27329Extracellular Potential
Transmembrane274 – 29320Helical; Name=5; Potential
Topological domain294 – 31623Cytoplasmic Potential
Transmembrane317 – 33923Helical; Name=6; Potential
Topological domain340 – 35415Extracellular Potential
Transmembrane355 – 37925Helical; Name=7; Potential
Topological domain380 – 43051Cytoplasmic Potential
Compositional bias60 – 656Asp/Glu-rich (acidic)
Compositional bias88 – 914Poly-Pro

Sites

Site41 – 422Cleavage; by thrombin By similarity

Amino acid modifications

Glycosylation671N-linked (GlcNAc...) Ref.6
Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation2551N-linked (GlcNAc...) Potential
Disulfide bond180 ↔ 259 By similarity

Experimental info

Sequence conflict1621F → S in AAA40438. Ref.1
Sequence conflict1891G → Y in AAA40438. Ref.1
Sequence conflict2231R → G in AAA40438. Ref.1
Sequence conflict2621V → L in AAA40438. Ref.1
Sequence conflict3651S → T in AAA40438. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P30558 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 395FD64FAE52C9BF

FASTA43047,790
        10         20         30         40         50         60 
MGPRRLLIVA LGLSLCGPLL SSRVPMSQPE SERTDATVNP RSFFLRNPSE NTFELVPLGD 

        70         80         90        100        110        120 
EEEEEKNESV LLEGRAVYLN ISLPPHTPPP PFISEDASGY LTSPWLTLFM PSVYTIVFIV 

       130        140        150        160        170        180 
SLPLNVLAIA VFVLRMKVKK PAVVYMLHLA MADVLFVSVL PFKISYYFSG TDWQFGSGMC 

       190        200        210        220        230        240 
RFATAAFYGN MYASIMLMTV ISIDRFLAVV YPIQSLSWRT LGRANFTCVV IWVMAIMGVV 

       250        260        270        280        290        300 
PLLLKEQTTR VPGLNITTCH DVLSENLMQG FYSYYFSAFS AIFFLVPLIV STVCYTSIIR 

       310        320        330        340        350        360 
CLSSSAVANR SKKSRALFLS AAVFCIFIVC FGPTNVLLIV HYLFLSDSPG TEAAYFAYLL 

       370        380        390        400        410        420 
CVCVSSVSCC IDPLIYYYAS SECQRHLYSI LCCKESSDPN SCNSTGQLMP SKMDTCSSHL 

       430 
NNSIYKKLLA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_034299.2. NM_010169.3.
UniGeneMm.24816.

3D structure databases

ProteinModelPortalP30558.
SMRP30558. Positions 73-393.
ModBaseSearch...
MobiDBSearch...

Chemistry

GuidetoPHARMACOLOGY347.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP30558.

Proteomic databases

PRIDEP30558.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000059193; ENSMUSP00000061754; ENSMUSG00000048376.
GeneID14062.
KEGGmmu:14062.
UCSCuc007rmn.1. mouse.

Organism-specific databases

CTD2149.
MGIMGI:101802. F2r.

Phylogenomic databases

eggNOGNOG150457.
GeneTreeENSGT00660000095329.
HOGENOMHOG000232200.
HOVERGENHBG108233.
InParanoidP30558.
KOK03914.
OMAVHYLFLS.
OrthoDBEOG7V49ZD.
PhylomeDBP30558.
TreeFamTF330775.

Gene expression databases

BgeeP30558.
CleanExMM_F2R.
GenevestigatorP30558.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR003912. Protea_act_rcpt.
IPR000935. Thrmbn_rcpt.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR01428. PROTEASEAR.
PR00908. THROMBINR.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285032.
PROP30558.
SOURCESearch...

Entry information

Entry namePAR1_MOUSE
AccessionPrimary (citable) accession number: P30558
Secondary accession number(s): P97507, Q3TVP3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries