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P28566 (5HT1E_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5-hydroxytryptamine receptor 1E

Short name=5-HT-1E
Short name=5-HT1E
Alternative name(s):
S31
Serotonin receptor 1E
Gene names
Name:HTR1E
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Ref.1 Ref.2 Ref.3 Ref.9 Ref.11

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.1 Ref.2 Ref.3 Ref.9 Ref.11.

Tissue specificity

Detected in brain. Ref.9

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3653655-hydroxytryptamine receptor 1E
PRO_0000068933

Regions

Topological domain1 – 2222Extracellular By similarity
Transmembrane23 – 4725Helical; Name=1; By similarity
Topological domain48 – 5912Cytoplasmic By similarity
Transmembrane60 – 8223Helical; Name=2; By similarity
Topological domain83 – 9614Extracellular By similarity
Transmembrane97 – 11822Helical; Name=3; By similarity
Topological domain119 – 13820Cytoplasmic By similarity
Transmembrane139 – 15921Helical; Name=4; By similarity
Topological domain160 – 17920Extracellular By similarity
Transmembrane180 – 20223Helical; Name=5; By similarity
Topological domain203 – 29189Cytoplasmic By similarity
Transmembrane292 – 31423Helical; Name=6; By similarity
Topological domain315 – 32410Extracellular By similarity
Transmembrane325 – 34723Helical; Name=7; By similarity
Topological domain348 – 36518Cytoplasmic By similarity
Region98 – 10710Agonist binding By similarity
Region304 – 3085Agonist binding By similarity
Motif119 – 1213DRY motif; important for ligand-induced conformation changes By similarity
Motif340 – 3445NPxxY motif; important for ligand-induced conformation changes and signaling By similarity

Amino acid modifications

Glycosylation21N-linked (GlcNAc...) Potential
Glycosylation51N-linked (GlcNAc...) Potential
Disulfide bond95 ↔ 173 By similarity

Natural variations

Natural variant2081A → T.
Corresponds to variant rs3828741 [ dbSNP | Ensembl ].
VAR_022061
Natural variant2621S → F. Ref.13
Corresponds to variant rs6303 [ dbSNP | Ensembl ].
VAR_014165

Sequences

Sequence LengthMass (Da)Tools
P28566 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 4C31DD783A3F7483

FASTA36541,682
        10         20         30         40         50         60 
MNITNCTTEA SMAIRPKTIT EKMLICMTLV VITTLTTLLN LAVIMAIGTT KKLHQPANYL 

        70         80         90        100        110        120 
ICSLAVTDLL VAVLVMPLSI IYIVMDRWKL GYFLCEVWLS VDMTCCTCSI LHLCVIALDR 

       130        140        150        160        170        180 
YWAITNAIEY ARKRTAKRAA LMILTVWTIS IFISMPPLFW RSHRRLSPPP SQCTIQHDHV 

       190        200        210        220        230        240 
IYTIYSTLGA FYIPLTLILI LYYRIYHAAK SLYQKRGSSR HLSNRSTDSQ NSFASCKLTQ 

       250        260        270        280        290        300 
TFCVSDFSTS DPTTEFEKFH ASIRIPPFDN DLDHPGERQQ ISSTRERKAA RILGLILGAF 

       310        320        330        340        350        360 
ILSWLPFFIK ELIVGLSIYT VSSEVADFLT WLGYVNSLIN PLLYTSFNED FKLAFKKLIR 


CREHT 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of a serotonin receptor from human brain (5HT1E): a fifth 5HT1-like subtype."
McAllister G., Charlesworth A., Snodin C., Beer M.S., Noble A.J., Middlemiss D.N., Iversen L.L., Whiting P.
Proc. Natl. Acad. Sci. U.S.A. 89:5517-5521(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
Tissue: Brain.
[2]"Molecular cloning of a human gene (S31) encoding a novel serotonin receptor mediating inhibition of adenylyl cyclase."
Levy F.O., Gudermann T., Birnbaumer M., Kaumann A.J., Birnbaumer L.
FEBS Lett. 296:201-206(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[3]"Human gene S31 encodes the pharmacologically defined serotonin 5-hydroxytryptamine1E receptor."
Zgombick J.M., Schechter L.E., Macchi M., Hartig P.R., Branchek T.A., Weinshank R.L.
Mol. Pharmacol. 42:180-185(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[4]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [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 (SEP-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].
[8]"Human-specific amino acid changes found in 103 protein-coding genes."
Kitano T., Liu Y.-H., Ueda S., Saitou N.
Mol. Biol. Evol. 21:936-944(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-363.
[9]"Molecular cloning and pharmacological characterization of the guinea pig 5-HT1E receptor."
Bai F., Yin T., Johnstone E.M., Su C., Varga G., Little S.P., Nelson D.L.
Eur. J. Pharmacol. 484:127-139(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[10]"Serotonin receptors."
Nichols D.E., Nichols C.D.
Chem. Rev. 108:1614-1641(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[11]"Toward selective drug development for the human 5-hydroxytryptamine 1E receptor: a comparison of 5-hydroxytryptamine 1E and 1F receptor structure-affinity relationships."
Klein M.T., Dukat M., Glennon R.A., Teitler M.
J. Pharmacol. Exp. Ther. 337:860-867(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]"Serotonin receptors - from molecular biology to clinical applications."
Pytliak M., Vargova V., Mechirova V., Felsoci M.
Physiol. Res. 60:15-25(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[13]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PHE-262.
[14]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M91467 mRNA. Translation: AAA58353.1.
Z11166 Genomic DNA. Translation: CAA77558.1.
M92826 Genomic DNA. Translation: AAA58355.1.
AF498980 mRNA. Translation: AAM21127.1.
AL157777 Genomic DNA. Translation: CAC10582.1.
CH471051 Genomic DNA. Translation: EAW48616.1.
CH471051 Genomic DNA. Translation: EAW48617.1.
BC069751 mRNA. Translation: AAH69751.1.
AB041373 Genomic DNA. Translation: BAA94458.1.
CCDSCCDS5006.1.
PIRA45260. S20579.
RefSeqNP_000856.1. NM_000865.2.
UniGeneHs.1611.

3D structure databases

ProteinModelPortalP28566.
SMRP28566. Positions 22-360.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109586. 2 interactions.
STRING9606.ENSP00000307766.

Chemistry

BindingDBP28566.
ChEMBLCHEMBL2096904.
DrugBankDB00216. Eletriptan.
GuidetoPHARMACOLOGY4.

Protein family/group databases

GPCRDBSearch...

Polymorphism databases

DMDM112822.

Proteomic databases

PaxDbP28566.
PRIDEP28566.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305344; ENSP00000307766; ENSG00000168830.
GeneID3354.
KEGGhsa:3354.
UCSCuc003pli.3. human.

Organism-specific databases

CTD3354.
GeneCardsGC06P087647.
HGNCHGNC:5291. HTR1E.
HPAHPA004931.
MIM182132. gene.
neXtProtNX_P28566.
PharmGKBPA29552.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249628.
HOGENOMHOG000239242.
HOVERGENHBG106962.
InParanoidP28566.
KOK04153.
OMAPLSITYI.
OrthoDBEOG7NCV3Q.
PhylomeDBP28566.
TreeFamTF316350.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeP28566.
CleanExHS_HTR1E.
GenevestigatorP28566.

Family and domain databases

Gene3D1.20.1070.10. 2 hits.
InterProIPR027425. 5HT1E_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24247:SF33. PTHR24247:SF33. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR01101. 5HTRECEPTOR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWiki5-HT1E_receptor.
GenomeRNAi3354.
NextBio13262.
PROP28566.
SOURCESearch...

Entry information

Entry name5HT1E_HUMAN
AccessionPrimary (citable) accession number: P28566
Secondary accession number(s): E1P503, Q9P1Y1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: July 9, 2014
This is version 137 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

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List of human entries with polymorphisms or disease mutations

Human chromosome 6

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