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O08675 (PAR3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 3

Short name=PAR-3
Alternative name(s):
Coagulation factor II receptor-like 2
Thrombin receptor-like 2
Gene names
Name:F2rl2
Synonyms:Par3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length369 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. May play a role in platelets activation.

Subunit structure

Interacts with INSC/inscuteable and GPSM2. Ref.4

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 3718Removed for receptor activation By similarity
PRO_0000012758
Chain38 – 369332Proteinase-activated receptor 3
PRO_0000012759

Regions

Topological domain38 – 9356Extracellular Potential
Transmembrane94 – 11926Helical; Name=1; Potential
Topological domain120 – 1278Cytoplasmic Potential
Transmembrane128 – 14720Helical; Name=2; Potential
Topological domain148 – 16619Extracellular Potential
Transmembrane167 – 18822Helical; Name=3; Potential
Topological domain189 – 20517Cytoplasmic Potential
Transmembrane206 – 22924Helical; Name=4; Potential
Topological domain230 – 25930Extracellular Potential
Transmembrane260 – 27920Helical; Name=5; Potential
Topological domain280 – 29617Cytoplasmic Potential
Transmembrane297 – 32125Helical; Name=6; Potential
Topological domain322 – 33514Extracellular Potential
Transmembrane336 – 36025Helical; Name=7; Potential
Topological domain361 – 3699Cytoplasmic Potential

Sites

Site37 – 382Cleavage; by thrombin By similarity

Amino acid modifications

Glycosylation241N-linked (GlcNAc...) Potential
Glycosylation811N-linked (GlcNAc...) Potential
Disulfide bond165 ↔ 244 By similarity

Experimental info

Sequence conflict1101A → S in AAC53137. Ref.1
Sequence conflict1101A → S in AAI40986. Ref.3
Sequence conflict1641T → M in AAC53137. Ref.1
Sequence conflict1641T → M in AAI40986. Ref.3
Sequence conflict2101M → L in AAC53137. Ref.1
Sequence conflict2101M → L in AAI40986. Ref.3
Sequence conflict2151M → I in AAC53137. Ref.1
Sequence conflict2151M → I in AAI40986. Ref.3

Secondary structure

... 369
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O08675 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: C8E6B0097F0BF90F

FASTA36941,697
        10         20         30         40         50         60 
MKILILVAAG LLFLPVTVCQ SGINVSDNSA KPTLTIKSFN GGPQNTFEEF PLSDIEGWTG 

        70         80         90        100        110        120 
ATTTIKAECP EDSISTLHVN NATIGYLRSS LSTQVIPAIY ILLFVVGVPA NIVTLWKLSL 

       130        140        150        160        170        180 
RTKSISLVIF HTNLAIADLL FCVTLPFKIA YHLNGNNWVF GEVTCRITTV VFYGNMYCAI 

       190        200        210        220        230        240 
LILTCMGINR YLATAHPFTY QKLPKRSFSM LMCGMVWVMV FLYMLPFVIL KQEYHLVHSE 

       250        260        270        280        290        300 
ITTCHDVVDA CESPSSFRFY YFVSLAFFGF LIPFVIIIFC YTTLIHKLKS KDRIWLGYIK 

       310        320        330        340        350        360 
AVLLILVIFT ICFAPTNIIL VIHHANYYYH NTDSLYFMYL IALCLGSLNS CLDPFLYFVM 


SKVVDQLNP 

« Hide

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].
Strain: C57BL/6.
[2]"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: Wolffian duct.
[3]"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].
Tissue: Brain.
[4]"Asymmetric cell divisions promote stratification and differentiation of mammalian skin."
Lechler T., Fuchs E.
Nature 437:275-280(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INSC AND GPSM2.
Strain: CD-1.
Tissue: Epidermis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U92972 mRNA. Translation: AAC53137.1.
AK135212 mRNA. Translation: BAE22460.1.
BC140985 mRNA. Translation: AAI40986.1.
CCDSCCDS26702.1.
RefSeqNP_034300.3. NM_010170.4.
UniGeneMm.440952.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PUXX-ray2.00C44-56[»]
ProteinModelPortalO08675.
SMRO08675. Positions 85-361.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-261941.

Chemistry

GuidetoPHARMACOLOGY349.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteO08675.

Proteomic databases

PRIDEO08675.

Protocols and materials databases

DNASU14064.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022182; ENSMUSP00000022182; ENSMUSG00000021675.
GeneID14064.
KEGGmmu:14064.
UCSCuc007rmq.1. mouse.

Organism-specific databases

CTD2151.
MGIMGI:1298208. F2rl2.

Phylogenomic databases

eggNOGNOG146611.
GeneTreeENSGT00660000095329.
HOGENOMHOG000116291.
HOVERGENHBG105658.
InParanoidQ3UXV3.
KOK04235.
OMACPEDSIS.
OrthoDBEOG7QC7WD.
TreeFamTF330775.

Enzyme and pathway databases

ReactomeREACT_224553. Hemostasis.

Gene expression databases

BgeeO08675.
CleanExMM_F2RL2.
GenevestigatorO08675.

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.
PROSITEPS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO08675.
NextBio285040.
PROO08675.
SOURCESearch...

Entry information

Entry namePAR3_MOUSE
AccessionPrimary (citable) accession number: O08675
Secondary accession number(s): B9EIT2, Q3UXV3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 124 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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