Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q95KZ0 (PE2R4_PANTR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Prostaglandin E2 receptor EP4 subtype

Short name=PGE receptor EP4 subtype
Short name=PGE2 receptor EP4 subtype
Alternative name(s):
Prostanoid EP4 receptor
Gene names
Name:PTGER4
OrganismPan troglodytes (Chimpanzee) [Reference proteome]
Taxonomic identifier9598 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. Has a relaxing effect on smooth muscle. May play an important role in regulating renal hemodynamics, intestinal epithelial transport, adrenal aldosterone secretion, and uterine function By similarity.

Subunit structure

Interacts with FEM1A By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Post-translational modification

Phosphorylation mediates agonist-mediated desensitization by promoting cytoplasmic retention By similarity.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT-helper cell differentiation

Inferred from electronic annotation. Source: Compara

adenylate cyclase-modulating G-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Compara

negative regulation of cytokine secretion

Inferred from electronic annotation. Source: Compara

negative regulation of eosinophil extravasation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of integrin activation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytokine secretion

Inferred from electronic annotation. Source: Compara

positive regulation of inflammatory response

Inferred from electronic annotation. Source: Compara

regulation of ossification

Inferred from electronic annotation. Source: Compara

regulation of stress fiber assembly

Inferred from electronic annotation. Source: Compara

response to lipopolysaccharide

Inferred from electronic annotation. Source: Compara

   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprostaglandin E receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 490490Prostaglandin E2 receptor EP4 subtype
PRO_0000070066

Regions

Topological domain1 – 1919Extracellular Potential
Transmembrane20 – 4324Helical; Name=1; Potential
Topological domain44 – 5512Cytoplasmic Potential
Transmembrane56 – 7924Helical; Name=2; Potential
Topological domain80 – 9617Extracellular Potential
Transmembrane97 – 11519Helical; Name=3; Potential
Topological domain116 – 13520Cytoplasmic Potential
Transmembrane136 – 16025Helical; Name=4; Potential
Topological domain161 – 18424Extracellular Potential
Transmembrane185 – 21127Helical; Name=5; Potential
Topological domain212 – 26958Cytoplasmic Potential
Transmembrane270 – 29728Helical; Name=6; Potential
Topological domain298 – 31417Extracellular Potential
Transmembrane315 – 33420Helical; Name=7; Potential
Topological domain335 – 490156Cytoplasmic Potential

Amino acid modifications

Modified residue3761Phosphoserine By similarity
Modified residue3791Phosphoserine By similarity
Modified residue3811Phosphoserine By similarity
Modified residue3841Phosphoserine By similarity
Glycosylation71N-linked (GlcNAc...) Potential
Disulfide bond92 ↔ 170 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q95KZ0 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 2074ACAE9CBF87D0

FASTA49053,304
        10         20         30         40         50         60 
MSTPGVNASA SLSPDRLNSP VTIPAVMFIF GVVGNLVAIV VLCKSRKEQK ETTFYTLVCG 

        70         80         90        100        110        120 
LAVTDLLGTL LVSPVTIATY MKGQWPGGQP LCEYSTFILL FFSLSGLSII CAMSVERYLA 

       130        140        150        160        170        180 
INHAYFYSHY VDKRLAGLTL FAVYASNVLF CALPNMGLGS SRLQYPDTWC FIDWTTNVTA 

       190        200        210        220        230        240 
HAAYSYMYAG FSSFLILATV LCNVLVCGAL LRMHRQFMRR TSLGTEQHHA AAAAVTSVAS 

       250        260        270        280        290        300 
RGHPAASPAL PRLSDFRRRR SFRRIAGAEI QMVILLIATS LVVLICSIPL VVRVFVNQLY 

       310        320        330        340        350        360 
QPSLEREVSK NPDLQAIRIA SVNPILDPWI YILLRKTVLS KAIEKIKCLF CRIGGSRRER 

       370        380        390        400        410        420 
SGQHCSDSQR TSSAMSGHSR SFISRELKEI SSTSQTLLPD LSLPDLSENG LGGRNLLPGV 

       430        440        450        460        470        480 
PGMGLAQEDT TSLRTLRISE TSDSSQGQDS ESVLLVDEAG GSGRAGPAPK GSSLQVTFPS 

       490 
ETLNLSEKCI 

« Hide

References

[1]"Pan troglodytes prostaglandin E2 subtype EP4 receptor."
Smock S.L., Castleberry T.A., Lu B., Owen T.A.
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY052641 mRNA. Translation: AAL15039.1.
RefSeqNP_001009078.1. NM_001009078.1.
UniGenePtr.6406.

3D structure databases

ProteinModelPortalQ95KZ0.
ModBaseSearch...

Protein-protein interaction databases

STRING9598.ENSPTRP00000028838.

Protein family/group databases

GPCRDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPTRT00000031222; ENSPTRP00000028838; ENSPTRG00000016819.
GeneID450195.
KEGGptr:450195.

Organism-specific databases

CTD5734.

Phylogenomic databases

eggNOGNOG295140.
GeneTreeENSGT00690000101953.
HOGENOMHOG000251595.
HOVERGENHBG053556.
InParanoidQ95KZ0.
KOK04261.
OMAHCSDSRR.
OrthoDBEOG495ZS1.

Family and domain databases

InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001758. Prost_EP4_rcpt.
IPR008365. Prostanoid_rcpt.
IPR001244. Prostglndn_DP_rcpt.
[Graphical view]
PANTHERPTHR11866. PTHR11866. 1 hit.
PTHR11866:SF6. PTHR11866:SF6. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR00428. PROSTAGLNDNR.
PR01788. PROSTANOIDR.
PR00586. PRSTNOIDEP4R.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20833154.

Entry information

Entry namePE2R4_PANTR
AccessionPrimary (citable) accession number: Q95KZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: December 1, 2001
Last modified: April 3, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

SIMILARITY comments

Index of protein domains and families