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O00254 (PAR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteinase-activated receptor 3

Short name=PAR-3
Alternative name(s):
Coagulation factor II receptor-like 2
Thrombin receptor-like 2
Gene names
Name:F2RL2
Synonyms:PAR3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. Ref.9

Subunit structure

Interacts with INSC/inscuteable and probably GPSM2. Ref.10

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Highest expression in the megakaryocytes of the bone marrow, lower in mature megakaryocytes, in platelets and in a variety of other tissues such as heart and gut. Ref.8

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.

Sequence caution

The sequence CAD97628.1 differs from that shown. Reason: Frameshift at position 374.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK1P163332EBI-1751853,EBI-389883

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00254-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O00254-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 3817Removed for receptor activation By similarity
PRO_0000012756
Chain39 – 374336Proteinase-activated receptor 3
PRO_0000012757

Regions

Topological domain39 – 9456Extracellular Potential
Transmembrane95 – 12026Helical; Name=1; Potential
Topological domain121 – 1288Cytoplasmic Potential
Transmembrane129 – 14820Helical; Name=2; Potential
Topological domain149 – 16719Extracellular Potential
Transmembrane168 – 18922Helical; Name=3; Potential
Topological domain190 – 20617Cytoplasmic Potential
Transmembrane207 – 23024Helical; Name=4; Potential
Topological domain231 – 26030Extracellular Potential
Transmembrane261 – 28020Helical; Name=5; Potential
Topological domain281 – 29717Cytoplasmic Potential
Transmembrane298 – 32225Helical; Name=6; Potential
Topological domain323 – 33614Extracellular Potential
Transmembrane337 – 36125Helical; Name=7; Potential
Topological domain362 – 37413Cytoplasmic Potential

Sites

Site38 – 392Cleavage; by thrombin By similarity

Amino acid modifications

Glycosylation251N-linked (GlcNAc...) Potential
Glycosylation821N-linked (GlcNAc...) Potential
Glycosylation3311N-linked (GlcNAc...) Potential
Disulfide bond166 ↔ 245 By similarity

Natural variations

Alternative sequence1 – 2222Missing in isoform 2.
VSP_045116
Natural variant151L → S. Ref.4
Corresponds to variant rs2069649 [ dbSNP | Ensembl ].
VAR_012849
Natural variant1771M → V. Ref.4
Corresponds to variant rs2069700 [ dbSNP | Ensembl ].
VAR_012850
Natural variant2501N → D. Ref.4
Corresponds to variant rs2069683 [ dbSNP | Ensembl ].
VAR_012851

Experimental info

Mutagenesis391T → P: No proteolytic cleavage by thrombin. Ref.1
Mutagenesis401F → A: Altered signal upon thrombin cleavage. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: C45C15A695DD1ABB

FASTA37442,508
        10         20         30         40         50         60 
MKALIFAAAG LLLLLPTFCQ SGMENDTNNL AKPTLPIKTF RGAPPNSFEE FPFSALEGWT 

        70         80         90        100        110        120 
GATITVKIKC PEESASHLHV KNATMGYLTS SLSTKLIPAI YLLVFVVGVP ANAVTLWMLF 

       130        140        150        160        170        180 
FRTRSICTTV FYTNLAIADF LFCVTLPFKI AYHLNGNNWV FGEVLCRATT VIFYGNMYCS 

       190        200        210        220        230        240 
ILLLACISIN RYLAIVHPFT YRGLPKHTYA LVTCGLVWAT VFLYMLPFFI LKQEYYLVQP 

       250        260        270        280        290        300 
DITTCHDVHN TCESSSPFQL YYFISLAFFG FLIPFVLIIY CYAAIIRTLN AYDHRWLWYV 

       310        320        330        340        350        360 
KASLLILVIF TICFAPSNII LIIHHANYYY NNTDGLYFIY LIALCLGSLN SCLDPFLYFL 

       370 
MSKTRNHSTA YLTK 

« Hide

Isoform 2 [UniParc].

Checksum: 36F6931ABB5C5393
Show »

FASTA35240,247

References

« Hide 'large scale' references
[1]"Protease-activated receptor 3 is a second thrombin receptor in humans."
Ishihara H., Connolly A.J., Zeng D., Kahn M.L., Zheng Y.-W., Timmons C., Tram T., Coughlin S.R.
Nature 386:502-506(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF THR-39 AND PHE-40.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Thymus.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Retina.
[4]SeattleSNPs variation discovery resource
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-15; VAL-177 AND ASP-250.
[5]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORM 1).
[8]"The human proteinase-activated receptor-3 (PAR-3) gene. Identification within a PAR gene cluster and characterization in vascular endothelial cells and platelets."
Schmidt V.A., Nierman W.C., Maglott D.R., Cupit L.D., Moskowitz K.A., Wainer J.A., Bahou W.F.
J. Biol. Chem. 273:15061-15068(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"Protease-activated receptors 1 and 4 mediate activation of human platelets by thrombin."
Kahn M.L., Nakanishi-Matsui M., Shapiro M.J., Ishihara H., Coughlin S.R.
J. Clin. Invest. 103:879-887(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Two forms of human Inscuteable-related protein that links Par3 to the Pins homologues LGN and AGS3."
Izaki T., Kamakura S., Kohjima M., Sumimoto H.
Biochem. Biophys. Res. Commun. 341:1001-1006(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INSC.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U92971 mRNA. Translation: AAC51218.1.
AK312848 mRNA. Translation: BAG35701.1.
AK298585 mRNA. Translation: BAG60775.1.
BX537386 mRNA. Translation: CAD97628.1. Frameshift.
AF374726 Genomic DNA. Translation: AAK51564.1.
AC026725 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95778.1.
BC093648 mRNA. Translation: AAH93648.1.
BC093650 mRNA. Translation: AAH93650.1.
RefSeqNP_001243495.1. NM_001256566.1.
NP_004092.1. NM_004101.3.
UniGeneHs.42502.

3D structure databases

ProteinModelPortalO00254.
SMRO00254. Positions 69-363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108450. 1 interaction.
IntActO00254. 9 interactions.
MINTMINT-3380783.
STRING9606.ENSP00000296641.

Chemistry

ChEMBLCHEMBL5477.
GuidetoPHARMACOLOGY349.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteO00254.

Proteomic databases

PRIDEO00254.

Protocols and materials databases

DNASU2151.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296641; ENSP00000296641; ENSG00000164220. [O00254-1]
ENST00000504899; ENSP00000426703; ENSG00000164220. [O00254-2]
GeneID2151.
KEGGhsa:2151.
UCSCuc003kem.4. human. [O00254-1]

Organism-specific databases

CTD2151.
GeneCardsGC05M075947.
HGNCHGNC:3539. F2RL2.
MIM601919. gene.
neXtProtNX_O00254.
PharmGKBPA27948.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG146611.
HOGENOMHOG000116291.
HOVERGENHBG105658.
InParanoidO00254.
KOK04235.
OMACRATTVI.
OrthoDBEOG7QC7WD.
PhylomeDBO00254.
TreeFamTF330775.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

BgeeO00254.
CleanExHS_F2RL2.
GenevestigatorO00254.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR003943. Prot_act_rcpt_3.
IPR003912. Protea_act_rcpt.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR01428. PROTEASEAR.
PR01429. PROTEASEAR3.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiF2RL2.
GenomeRNAi2151.
NextBio8693.
PMAP-CutDBO00254.
PROO00254.
SOURCESearch...

Entry information

Entry namePAR3_HUMAN
AccessionPrimary (citable) accession number: O00254
Secondary accession number(s): B2R754 expand/collapse secondary AC list , B4DQ13, Q52M68, Q7Z3W3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries