P30558 (PAR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteinase-activated receptor 1
Short name=PAR-1

Alternative name(s):
Thrombin receptor

Gene names

Name:	F2r
Synonyms:	Cf2r, Par1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	430 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Post-translational modification	A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
Biological process	Blood coagulation
Cellular component	Cell membrane Membrane
Domain	Signal Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	homeostasis of number of cells within a tissue Inferred from mutant phenotype. Source: MGI positive regulation of ERK1 and ERK2 cascade Inferred from direct assay. Source: UniProtKB positive regulation of Rho protein signal transduction Inferred from direct assay. Source: UniProtKB positive regulation of blood coagulation Inferred from mutant phenotype. Source: MGI positive regulation of cell migration Inferred from direct assay. Source: UniProtKB positive regulation of phosphatidylinositol 3-kinase cascade Inferred from direct assay. Source: UniProtKB regulation of interleukin-1 beta production Inferred from mutant phenotype. Source: MGI response to lipopolysaccharide Inferred from mutant phenotype. Source: MGI
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	G-protein alpha-subunit binding Inferred from direct assay. Source: UniProtKB G-protein beta-subunit binding Inferred from direct assay. Source: UniProtKB heterotrimeric G-protein binding Traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Propeptide	22 – 41	20	Removed for receptor activation By similarity		PRO_0000012742
	Chain	42 – 430	389	Proteinase-activated receptor 1		PRO_0000012743
Regions
	Topological domain	42 – 107	66	Extracellular Potential
	Transmembrane	108 – 133	26	Helical; Name=1; Potential
	Topological domain	134 – 142	9	Cytoplasmic Potential
	Transmembrane	143 – 162	20	Helical; Name=2; Potential
	Topological domain	163 – 181	19	Extracellular Potential
	Transmembrane	182 – 203	22	Helical; Name=3; Potential
	Topological domain	204 – 223	20	Cytoplasmic Potential
	Transmembrane	224 – 244	21	Helical; Name=4; Potential
	Topological domain	245 – 273	29	Extracellular Potential
	Transmembrane	274 – 293	20	Helical; Name=5; Potential
	Topological domain	294 – 316	23	Cytoplasmic Potential
	Transmembrane	317 – 339	23	Helical; Name=6; Potential
	Topological domain	340 – 354	15	Extracellular Potential
	Transmembrane	355 – 379	25	Helical; Name=7; Potential
	Topological domain	380 – 430	51	Cytoplasmic Potential
	Compositional bias	60 – 65	6	Asp/Glu-rich (acidic)
	Compositional bias	88 – 91	4	Poly-Pro
Sites
	Site	41 – 42	2	Cleavage; by thrombin By similarity
Amino acid modifications
	Glycosylation	67	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	80	1	N-linked (GlcNAc...) Potential
	Glycosylation	255	1	N-linked (GlcNAc...) Potential
	Disulfide bond	180 ↔ 259		By similarity
Experimental info
	Sequence conflict	162	1	F → S in AAA40438. Ref.1
	Sequence conflict	189	1	G → Y in AAA40438. Ref.1
	Sequence conflict	223	1	R → G in AAA40438. Ref.1
	Sequence conflict	262	1	V → L in AAA40438. Ref.1
	Sequence conflict	365	1	S → T in AAA40438. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P30558 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 395FD64FAE52C9BF	FASTA	430	47,790
	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

References

	« Hide 'large scale' referencesShow '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. 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: 8784787] [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: 16141072] [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: 15489334] [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: 8678993] [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: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-67, MASS SPECTROMETRY.
+	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. U55076, U55075 Genomic DNA. Translation: AAB00198.1.
IPI	IPI00131268.
RefSeq	NP_034299.2. NM_010169.3.
UniGene	Mm.24816.
3D structure databases
ProteinModelPortal	P30558.
SMR	P30558. Positions 108-392.
ModBase	Search...
Protein-protein interaction databases
STRING	P30558.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	P30558.
Proteomic databases
PRIDE	P30558.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000059193; ENSMUSP00000061754; ENSMUSG00000048376.
GeneID	14062.
KEGG	mmu:14062.
NMPDR	fig|10090.3.peg.28270.
UCSC	uc007rmn.1. mouse.
Organism-specific databases
CTD	2149.
MGI	MGI:101802. F2r.
Phylogenomic databases
eggNOG	roNOG04169.
HOGENOM	HBG714985.
HOVERGEN	HBG108233.
InParanoid	P30558.
OMA	IVHYLFL.
OrthoDB	EOG47SSFM.
PhylomeDB	P30558.
Enzyme and pathway databases
Reactome	REACT_89750. Hemostasis.
Gene expression databases
ArrayExpress	P30558.
Bgee	P30558.
CleanEx	MM_F2R.
Genevestigator	P30558.
GermOnline	ENSMUSG00000048376. Mus musculus.
Family and domain databases
InterPro	IPR000276. 7TM_GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_supfam. IPR003912. Protea_act_rcpt. IPR000935. Thrmbn_rcpt. [Graphical view]
KO	K03914.
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR00237. GPCRRHODOPSN. PR01428. PROTEASEAR. PR00908. THROMBINR.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	285032.
SOURCE	Search...

Entry information

Entry name

PAR1_MOUSE

Accession

Primary (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:	November 16, 2011
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program