P43115 · PE2R3_HUMAN
- ProteinProstaglandin E2 receptor EP3 subtype
- GenePTGER3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids390 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor for prostaglandin E2 (PGE2) (PubMed:7883006, PubMed:7981210, PubMed:8117308, PubMed:8135729, PubMed:8307176).
The activity of this receptor can couple to both the inhibition of adenylate cyclase mediated by G(i) proteins, and to an elevation of intracellular calcium (PubMed:7883006, PubMed:7981210, PubMed:8117308, PubMed:8135729).
Required for normal development of fever in response to pyrinogens, including IL1B, prostaglandin E2 and bacterial lipopolysaccharide (LPS). Required for normal potentiation of platelet aggregation by prostaglandin E2, and thus plays a role in the regulation of blood coagulation. Required for increased HCO3- secretion in the duodenum in response to mucosal acidification, and thereby contributes to the protection of the mucosa against acid-induced ulceration. Not required for normal kidney function, normal urine volume and osmolality (By similarity).
The activity of this receptor can couple to both the inhibition of adenylate cyclase mediated by G(i) proteins, and to an elevation of intracellular calcium (PubMed:7883006, PubMed:7981210, PubMed:8117308, PubMed:8135729).
Required for normal development of fever in response to pyrinogens, including IL1B, prostaglandin E2 and bacterial lipopolysaccharide (LPS). Required for normal potentiation of platelet aggregation by prostaglandin E2, and thus plays a role in the regulation of blood coagulation. Required for increased HCO3- secretion in the duodenum in response to mucosal acidification, and thereby contributes to the protection of the mucosa against acid-induced ulceration. Not required for normal kidney function, normal urine volume and osmolality (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | nuclear envelope | |
Cellular Component | plasma membrane | |
Molecular Function | prostaglandin E receptor activity | |
Biological Process | adenylate cyclase-activating G protein-coupled receptor signaling pathway | |
Biological Process | cell death | |
Biological Process | G protein-coupled receptor signaling pathway | |
Biological Process | inflammatory response | |
Biological Process | intestine smooth muscle contraction | |
Biological Process | negative regulation of gastric acid secretion | |
Biological Process | phospholipase C-activating G protein-coupled receptor signaling pathway | |
Biological Process | positive regulation of cytosolic calcium ion concentration | |
Biological Process | positive regulation of fever generation |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProstaglandin E2 receptor EP3 subtype
- Short namesPGE receptor EP3 subtype; PGE2 receptor EP3 subtype
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP43115
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-53 | Extracellular | ||||
Sequence: MKETRGYGGDAPFCTRLNHSYTGMWAPERSAEARGNLTRPPGSGEDCGSVSVA | ||||||
Transmembrane | 54-78 | Helical; Name=1 | ||||
Sequence: FPITMLLTGFVGNALAMLLVSRSYR | ||||||
Topological domain | 79-91 | Cytoplasmic | ||||
Sequence: RRESKRKKSFLLC | ||||||
Transmembrane | 92-112 | Helical; Name=2 | ||||
Sequence: IGWLALTDLVGQLLTTPVVIV | ||||||
Topological domain | 113-131 | Extracellular | ||||
Sequence: VYLSKQRWEHIDPSGRLCT | ||||||
Transmembrane | 132-153 | Helical; Name=3 | ||||
Sequence: FFGLTMTVFGLSSLFIASAMAV | ||||||
Topological domain | 154-175 | Cytoplasmic | ||||
Sequence: ERALAIRAPHWYASHMKTRATR | ||||||
Transmembrane | 176-197 | Helical; Name=4 | ||||
Sequence: AVLLGVWLAVLAFALLPVLGVG | ||||||
Topological domain | 198-227 | Extracellular | ||||
Sequence: QYTVQWPGTWCFISTGRGGNGTSSSHNWGN | ||||||
Transmembrane | 228-253 | Helical; Name=5 | ||||
Sequence: LFFASAFAFLGLLALTVTFSCNLATI | ||||||
Topological domain | 254-283 | Cytoplasmic | ||||
Sequence: KALVSRCRAKATASQSSAQWGRITTETAIQ | ||||||
Transmembrane | 284-307 | Helical; Name=6 | ||||
Sequence: LMGIMCVLSVCWSPLLIMMLKMIF | ||||||
Topological domain | 308-327 | Extracellular | ||||
Sequence: NQTSVEHCKTHTEKQKECNF | ||||||
Transmembrane | 328-349 | Helical; Name=7 | ||||
Sequence: FLIAVRLASLNQILDPWVYLLL | ||||||
Topological domain | 350-390 | Cytoplasmic | ||||
Sequence: RKILLRKFCQIRYHTNNYASSSTSLPCQCSSTLMWSDHLER |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_014694 | 169 | in dbSNP:rs5670 | |||
Sequence: M → L | ||||||
Natural variant | VAR_049436 | 319 | in dbSNP:rs13306020 | |||
Sequence: T → M | ||||||
Natural variant | VAR_029218 | 366 | in dbSNP:rs13306014 | |||
Sequence: N → S | ||||||
Natural variant | VAR_014695 | 375 | in dbSNP:rs5694 | |||
Sequence: P → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 544 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000070058 | 1-390 | Prostaglandin E2 receptor EP3 subtype | |||
Sequence: MKETRGYGGDAPFCTRLNHSYTGMWAPERSAEARGNLTRPPGSGEDCGSVSVAFPITMLLTGFVGNALAMLLVSRSYRRRESKRKKSFLLCIGWLALTDLVGQLLTTPVVIVVYLSKQRWEHIDPSGRLCTFFGLTMTVFGLSSLFIASAMAVERALAIRAPHWYASHMKTRATRAVLLGVWLAVLAFALLPVLGVGQYTVQWPGTWCFISTGRGGNGTSSSHNWGNLFFASAFAFLGLLALTVTFSCNLATIKALVSRCRAKATASQSSAQWGRITTETAIQLMGIMCVLSVCWSPLLIMMLKMIFNQTSVEHCKTHTEKQKECNFFLIAVRLASLNQILDPWVYLLLRKILLRKFCQIRYHTNNYASSSTSLPCQCSSTLMWSDHLER | ||||||
Glycosylation | 18 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 36 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts (via C-terminus) with MKLN1.
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence & Isoforms
- Sequence statusComplete
This entry describes 12 isoforms produced by Alternative splicing. Additional isoforms seem to exist.
P43115-1
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.
- NameEP3A
- SynonymsEP3-I, EP3a1, EP3a2, EP(3-Ic)
- Length390
- Mass (Da)43,310
- Last updated1995-11-01 v1
- ChecksumBC76EAC78FDF5420
P43115-2
- NameEP3C
- SynonymsEP3-II
- NoteKnown as EP3D in PubMed:8075855.
- Differences from canonical
- 360-390: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → VANAVSSCSNDGQKGQPISLSNEIIQTEA
P43115-3
- NameEP3B
- SynonymsEP3-III
- NoteKnown as EP3E in PubMed:8075855.
- Differences from canonical
- 360-390: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → EEFWGN
P43115-4
- NameEP3D
- SynonymsEP3-IV
- NoteKnown as EP3F in PubMed:8075855.
- Differences from canonical
- 360-390: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → MRKRRLREQEEFWGN
P43115-5
- NameEP3E
- Differences from canonical
- 360-390: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → MRKRRLREQLICSLQNSQIQRATAHCGQVQTYRVLNREEMEVLVSSINVYTRISTVKTE
P43115-6
- NameEP3F
- Differences from canonical
- 360-390: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → MRKRRLREQAPLLPTPTVIDPSRFCAQPFRWFLDLSFPAMSSSHPQLPLTLASFKLLREPCSVQLS
P43115-7
- NameEP3G
- Differences from canonical
- 360-390: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → EMGPDGRCFCHAWRQVPRTWCSSHDREPCSVQLS
P43115-8
- NameEP3-III
- Differences from canonical
- 360-390: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → VANAVSSCSNDGQKGQPISLSNEIIQTEAEEFWGN
P43115-9
- NameEP3-IV
- Differences from canonical
- 360-390: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → VANAVSSCSNDGQKGQPISLSNEIIQTEAMRKRRLREQEEFWGN
P43115-10
- NameEP3-V
- Differences from canonical
- 360-390: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → VANAVSSCSNDGQKGQPISLSNEIIQTEAMRKRRLREQEMGPDGRCFCHAWRQVPRTWCSSHDREPCSVQLS
P43115-11
- NameEP3E2
- Differences from canonical
- 360-390: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → VANAVSSCSNDGQKGQPISLSNEIIQTEAMRKRRLREQLICSLRTLRYRGQLHIVGKYKPIVC
P43115-12
- Name12
- Differences from canonical
- 360-390: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → MRKRRLREQFWRPASSGSGCQQIRCLMESCSLTQTGVQWSDFRSLQPSPPPLTAIFASWVQVILLPQPPK
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
O00325 | O00325_HUMAN | PTGER3 | 402 | ||
A0A0B4J204 | A0A0B4J204_HUMAN | PTGER3 | 425 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 28-29 | in Ref. 3, 4 and 7 | ||||
Sequence: ER → DG | ||||||
Alternative sequence | VSP_058943 | 360-390 | in isoform 12 | |||
Sequence: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → MRKRRLREQFWRPASSGSGCQQIRCLMESCSLTQTGVQWSDFRSLQPSPPPLTAIFASWVQVILLPQPPK | ||||||
Alternative sequence | VSP_053774 | 360-390 | in isoform EP3-III | |||
Sequence: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → VANAVSSCSNDGQKGQPISLSNEIIQTEAEEFWGN | ||||||
Alternative sequence | VSP_053775 | 360-390 | in isoform EP3-IV | |||
Sequence: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → VANAVSSCSNDGQKGQPISLSNEIIQTEAMRKRRLREQEEFWGN | ||||||
Alternative sequence | VSP_053776 | 360-390 | in isoform EP3-V | |||
Sequence: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → VANAVSSCSNDGQKGQPISLSNEIIQTEAMRKRRLREQEMGPDGRCFCHAWRQVPRTWCSSHDREPCSVQLS | ||||||
Alternative sequence | VSP_001936 | 360-390 | in isoform EP3B | |||
Sequence: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → EEFWGN | ||||||
Alternative sequence | VSP_001935 | 360-390 | in isoform EP3C | |||
Sequence: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → VANAVSSCSNDGQKGQPISLSNEIIQTEA | ||||||
Alternative sequence | VSP_001937 | 360-390 | in isoform EP3D | |||
Sequence: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → MRKRRLREQEEFWGN | ||||||
Alternative sequence | VSP_001938 | 360-390 | in isoform EP3E | |||
Sequence: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → MRKRRLREQLICSLQNSQIQRATAHCGQVQTYRVLNREEMEVLVSSINVYTRISTVKTE | ||||||
Alternative sequence | VSP_053777 | 360-390 | in isoform EP3E2 | |||
Sequence: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → VANAVSSCSNDGQKGQPISLSNEIIQTEAMRKRRLREQLICSLRTLRYRGQLHIVGKYKPIVC | ||||||
Alternative sequence | VSP_001939 | 360-390 | in isoform EP3F | |||
Sequence: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → MRKRRLREQAPLLPTPTVIDPSRFCAQPFRWFLDLSFPAMSSSHPQLPLTLASFKLLREPCSVQLS | ||||||
Alternative sequence | VSP_013271 | 360-390 | in isoform EP3G | |||
Sequence: IRYHTNNYASSSTSLPCQCSSTLMWSDHLER → EMGPDGRCFCHAWRQVPRTWCSSHDREPCSVQLS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
S69200 EMBL· GenBank· DDBJ | AAB29854.1 EMBL· GenBank· DDBJ | mRNA | ||
L27488 EMBL· GenBank· DDBJ | AAC13372.1 EMBL· GenBank· DDBJ | mRNA | ||
L27489 EMBL· GenBank· DDBJ | AAC13373.1 EMBL· GenBank· DDBJ | mRNA | ||
L27490 EMBL· GenBank· DDBJ | AAC13374.1 EMBL· GenBank· DDBJ | mRNA | ||
X83857 EMBL· GenBank· DDBJ | CAA58737.1 EMBL· GenBank· DDBJ | mRNA | ||
X83858 EMBL· GenBank· DDBJ | CAA58738.1 EMBL· GenBank· DDBJ | mRNA | ||
X83859 EMBL· GenBank· DDBJ | CAA58739.1 EMBL· GenBank· DDBJ | mRNA | ||
X83860 EMBL· GenBank· DDBJ | CAA58740.1 EMBL· GenBank· DDBJ | mRNA | ||
X83861 EMBL· GenBank· DDBJ | CAA58741.1 EMBL· GenBank· DDBJ | mRNA | ||
X83862 EMBL· GenBank· DDBJ | CAA58742.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
X83863 EMBL· GenBank· DDBJ | CAA58743.1 EMBL· GenBank· DDBJ | mRNA | ||
L26976 EMBL· GenBank· DDBJ | AAA60076.1 EMBL· GenBank· DDBJ | mRNA | ||
S69326 EMBL· GenBank· DDBJ | AAB30208.1 EMBL· GenBank· DDBJ | mRNA | ||
L32660 EMBL· GenBank· DDBJ | AAA68191.1 EMBL· GenBank· DDBJ | mRNA | ||
L32661 EMBL· GenBank· DDBJ | AAA68192.1 EMBL· GenBank· DDBJ | mRNA | ||
L32662 EMBL· GenBank· DDBJ | AAA68193.1 EMBL· GenBank· DDBJ | mRNA | ||
D38297 EMBL· GenBank· DDBJ | BAA07416.1 EMBL· GenBank· DDBJ | mRNA | ||
D38298 EMBL· GenBank· DDBJ | BAA07417.1 EMBL· GenBank· DDBJ | mRNA | ||
D38299 EMBL· GenBank· DDBJ | BAA07418.1 EMBL· GenBank· DDBJ | mRNA | ||
D38300 EMBL· GenBank· DDBJ | BAA07419.1 EMBL· GenBank· DDBJ | mRNA | ||
D38301 EMBL· GenBank· DDBJ | BAA07420.1 EMBL· GenBank· DDBJ | mRNA | ||
U13214 EMBL· GenBank· DDBJ | AAA21130.1 EMBL· GenBank· DDBJ | mRNA | ||
U13215 EMBL· GenBank· DDBJ | AAA21131.1 EMBL· GenBank· DDBJ | mRNA | ||
U13216 EMBL· GenBank· DDBJ | AAA21132.1 EMBL· GenBank· DDBJ | mRNA | ||
U13217 EMBL· GenBank· DDBJ | AAA21133.1 EMBL· GenBank· DDBJ | mRNA | ||
U13218 EMBL· GenBank· DDBJ | AAA21134.1 EMBL· GenBank· DDBJ | mRNA | ||
D86096 EMBL· GenBank· DDBJ | BAA19951.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D86096 EMBL· GenBank· DDBJ | BAA19952.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D86096 EMBL· GenBank· DDBJ | BAA19953.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D86096 EMBL· GenBank· DDBJ | BAA19954.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D86096 EMBL· GenBank· DDBJ | BAA19956.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D86096 EMBL· GenBank· DDBJ | BAA19957.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D86098 EMBL· GenBank· DDBJ | BAA19959.1 EMBL· GenBank· DDBJ | mRNA | ||
AY429108 EMBL· GenBank· DDBJ | AAR07903.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315825 EMBL· GenBank· DDBJ | BAF98716.1 EMBL· GenBank· DDBJ | mRNA | ||
AB451481 EMBL· GenBank· DDBJ | BAG70295.1 EMBL· GenBank· DDBJ | mRNA | ||
AL031429 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL158087 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471059 EMBL· GenBank· DDBJ | EAX06439.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471059 EMBL· GenBank· DDBJ | EAX06446.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC024229 EMBL· GenBank· DDBJ | AAH24229.1 EMBL· GenBank· DDBJ | mRNA | ||
BC118578 EMBL· GenBank· DDBJ | AAI18579.1 EMBL· GenBank· DDBJ | mRNA |