Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Proteinase-activated receptor 4

Gene

F2rl3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for activated thrombin or trypsin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Blood coagulation, Hemostasis

Enzyme and pathway databases

ReactomeiR-MMU-375276. Peptide ligand-binding receptors.
R-MMU-416476. G alpha (q) signalling events.
R-MMU-456926. Thrombin signalling through proteinase activated receptors (PARs).

Names & Taxonomyi

Protein namesi
Recommended name:
Proteinase-activated receptor 4
Short name:
PAR-4
Alternative name(s):
Coagulation factor II receptor-like 3
Thrombin receptor-like 3
Gene namesi
Name:F2rl3
Synonyms:Par4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1298207. F2rl3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini60 – 9435ExtracellularSequence analysisAdd
BLAST
Transmembranei95 – 11521Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini116 – 1205CytoplasmicSequence analysis
Transmembranei121 – 14121Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini142 – 16221ExtracellularSequence analysisAdd
BLAST
Transmembranei163 – 18321Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini184 – 20320CytoplasmicSequence analysisAdd
BLAST
Transmembranei204 – 22421Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini225 – 25531ExtracellularSequence analysisAdd
BLAST
Transmembranei256 – 27621Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini277 – 29519CytoplasmicSequence analysisAdd
BLAST
Transmembranei296 – 31621Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini317 – 33115ExtracellularSequence analysisAdd
BLAST
Transmembranei332 – 35524Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini356 – 39641CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Propeptidei17 – 5943Removed for receptor activationBy similarityPRO_0000012764Add
BLAST
Chaini60 – 396337Proteinase-activated receptor 4PRO_0000012765Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi68 – 681N-linked (GlcNAc...)Sequence analysis
Disulfide bondi161 ↔ 240PROSITE-ProRule annotation

Post-translational modificationi

A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei59 – 602Cleavage; by thrombinBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO88634.
PaxDbiO88634.
PRIDEiO88634.

PTM databases

PhosphoSiteiO88634.

Expressioni

Tissue specificityi

Highly expressed in the spleen. Slight expression in the heart, lung, skeletal muscle and kidney. No detectable expression in brain, liver or testis. Also detected in platelets.

Gene expression databases

BgeeiO88634.
CleanExiMM_F2RL3.
GenevisibleiO88634. MM.

Interactioni

Protein-protein interaction databases

DIPiDIP-42480N.
IntActiO88634. 1 interaction.
MINTiMINT-2737730.
STRINGi10090.ENSMUSP00000054426.

Structurei

Secondary structure

1
396
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni62 – 654Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PV9X-ray3.50C51-76[»]
ProteinModelPortaliO88634.
SMRiO88634. Positions 51-76, 91-367.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88634.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi374 – 3774Poly-Ser

Sequence similaritiesi

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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFSN. Eukaryota.
ENOG410YD35. LUCA.
GeneTreeiENSGT00760000119001.
HOGENOMiHOG000116291.
HOVERGENiHBG096365.
InParanoidiO88634.
KOiK04236.
OMAiPFVYYYV.
OrthoDBiEOG79PJPM.
TreeFamiTF350010.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR003944. Prot_act_rcpt_4.
IPR003912. Protea_act_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR01428. PROTEASEAR.
PR01430. PROTEASEAR4.
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.

O88634-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCWPLLYPLV LGLSISLAEG IQTPSIYDDV ESTRGSHEGP LGPTVELKEP
60 70 80 90 100
KSSDKPNPRG YPGKFCANDS DTLELPASSQ ALLLGWVPTR LVPALYGLVV
110 120 130 140 150
AVGLPANGLA LWVLATRVPR LPSTILLMNL AVADLLLALV LPPRLAYHLR
160 170 180 190 200
GQRWPFGEAA CRVATAALYG HMYGSVLLLA AVSLDRYLAL VHPLRARALR
210 220 230 240 250
GQRLTTGLCL VAWLSAATLA LPLTLHRQTF RLAGSDRMLC HDALPLTEQT
260 270 280 290 300
SHWRPAFICL AVLGCFVPLL AMGLCYGATL RALAANGQRY SHALRLTALV
310 320 330 340 350
LFSAVASFTP SNVLLVLHYS NPSPEAWGNL YGAYVPSLAL STLNSCVDPF
360 370 380 390
IYYYVSHEFR EKVRAMLCRQ PEASSSSQAS REAGSRGTAI CSSTLL
Length:396
Mass (Da):42,786
Last modified:July 27, 2011 - v2
Checksum:iDC10502E7AAE1B86
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 881P → S in AAC28861 (PubMed:9722561).Curated
Sequence conflicti128 – 1281M → T in AAC28861 (PubMed:9722561).Curated
Sequence conflicti135 – 1351L → S in AAC28861 (PubMed:9722561).Curated
Sequence conflicti141 – 1411L → P in AAC28861 (PubMed:9722561).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF080215 mRNA. Translation: AAC28861.1.
AK036427 mRNA. Translation: BAC29423.1.
AK153720 mRNA. Translation: BAE32155.1.
AK156729 mRNA. Translation: BAE33823.1.
CH466525 Genomic DNA. Translation: EDL10818.1.
CCDSiCCDS22419.1.
RefSeqiNP_032001.2. NM_007975.3.
UniGeneiMm.12948.

Genome annotation databases

EnsembliENSMUST00000058099; ENSMUSP00000054426; ENSMUSG00000050147.
GeneIDi14065.
KEGGimmu:14065.
UCSCiuc009mgr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF080215 mRNA. Translation: AAC28861.1.
AK036427 mRNA. Translation: BAC29423.1.
AK153720 mRNA. Translation: BAE32155.1.
AK156729 mRNA. Translation: BAE33823.1.
CH466525 Genomic DNA. Translation: EDL10818.1.
CCDSiCCDS22419.1.
RefSeqiNP_032001.2. NM_007975.3.
UniGeneiMm.12948.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PV9X-ray3.50C51-76[»]
ProteinModelPortaliO88634.
SMRiO88634. Positions 51-76, 91-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-42480N.
IntActiO88634. 1 interaction.
MINTiMINT-2737730.
STRINGi10090.ENSMUSP00000054426.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiO88634.

Proteomic databases

MaxQBiO88634.
PaxDbiO88634.
PRIDEiO88634.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000058099; ENSMUSP00000054426; ENSMUSG00000050147.
GeneIDi14065.
KEGGimmu:14065.
UCSCiuc009mgr.1. mouse.

Organism-specific databases

CTDi9002.
MGIiMGI:1298207. F2rl3.

Phylogenomic databases

eggNOGiENOG410IFSN. Eukaryota.
ENOG410YD35. LUCA.
GeneTreeiENSGT00760000119001.
HOGENOMiHOG000116291.
HOVERGENiHBG096365.
InParanoidiO88634.
KOiK04236.
OMAiPFVYYYV.
OrthoDBiEOG79PJPM.
TreeFamiTF350010.

Enzyme and pathway databases

ReactomeiR-MMU-375276. Peptide ligand-binding receptors.
R-MMU-416476. G alpha (q) signalling events.
R-MMU-456926. Thrombin signalling through proteinase activated receptors (PARs).

Miscellaneous databases

EvolutionaryTraceiO88634.
PROiO88634.
SOURCEiSearch...

Gene expression databases

BgeeiO88634.
CleanExiMM_F2RL3.
GenevisibleiO88634. MM.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR003944. Prot_act_rcpt_4.
IPR003912. Protea_act_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR01428. PROTEASEAR.
PR01430. PROTEASEAR4.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Gene and locus structure and chromosomal localization of the protease-activated receptor gene family."
    Kahn M.L., Hammes S.R., Botka C., Coughlin S.R.
    J. Biol. Chem. 273:23290-23296(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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 and NOD.
    Tissue: Bone, Spleen and Thymus.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiPAR4_MOUSE
AccessioniPrimary (citable) accession number: O88634
Secondary accession number(s): Q8BZ77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 128 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.