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Q64264 (5HT1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 1A

Short name=5-HT-1A
Short name=5-HT1A
Alternative name(s):
Serotonin receptor 1A
Gene names
Name:Htr1a
Synonyms:Gpcr18
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length421 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 drugs 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. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling inhibits adenylate cyclase activity and activates a phosphatidylinositol-calcium second messenger system that regulates the release of Ca2+ ions from intracellular stores. Plays a role in the regulation of 5-hydroxytryptamine release and in the regulation of dopamine and 5-hydroxytryptamine metabolism. Plays a role in the regulation of dopamine and 5-hydroxytryptamine levels in the brain, and thereby affects neural activity, mood and behavior. Plays a role in the response to anxiogenic stimuli. Ref.1 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Subunit structure

Heterodimer; heterodimerizes with GPER1 By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.1.

Tissue specificity

Most abundantly expressed in midbrain, in dorsal raphe and hippocampus. Detected at lower levels in amygdala and brain cortex. Ref.7

Disruption phenotype

Mutant mice display decreased exploratory behavior and increased fear-related behavior in anxiogenic environments. Mutant mice display altered monoamine metabolism in specific parts of the brain, especially in dorsal and medial raphe nuclei, thalamus and hypothalamus, leading to altered levels of 5-hydroxytryptamine, dopamine and their metabolites, as well as altered noradrenaline levels. Ref.7 Ref.8 Ref.9

Sequence similarities

Belongs to the G-protein coupled receptor 1 family. 5-hydroxytryptamine receptor subfamily. HTR1A sub-subfamily.

Ontologies

Keywords
   Biological processBehavior
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadenylate cyclase-inhibiting serotonin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

behavioral fear response

Inferred from mutant phenotype Ref.7. Source: UniProtKB

cell proliferation

Inferred from electronic annotation. Source: InterPro

exploration behavior

Inferred from mutant phenotype Ref.7. Source: UniProtKB

regulation of behavior

Inferred from electronic annotation. Source: InterPro

regulation of dopamine metabolic process

Inferred from mutant phenotype Ref.8. Source: UniProtKB

regulation of hormone secretion

Inferred from electronic annotation. Source: InterPro

regulation of serotonin secretion

Inferred from mutant phenotype Ref.7. Source: UniProtKB

serotonin metabolic process

Inferred from mutant phenotype Ref.8. Source: UniProtKB

serotonin receptor signaling pathway

Inferred from mutant phenotype Ref.7. Source: UniProtKB

vasoconstriction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentintegral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionserotonin receptor activity

Inferred from mutant phenotype Ref.7. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4214215-hydroxytryptamine receptor 1A
PRO_0000068904

Regions

Topological domain1 – 3636Extracellular By similarity
Transmembrane37 – 6226Helical; Name=1; By similarity
Topological domain63 – 7311Cytoplasmic By similarity
Transmembrane74 – 9825Helical; Name=2; By similarity
Topological domain99 – 11012Extracellular By similarity
Transmembrane111 – 13222Helical; Name=3; By similarity
Topological domain133 – 15220Cytoplasmic By similarity
Transmembrane153 – 17826Helical; Name=4; By similarity
Topological domain179 – 19113Extracellular By similarity
Transmembrane192 – 21726Helical; Name=5; By similarity
Topological domain218 – 345128Cytoplasmic By similarity
Transmembrane346 – 36722Helical; Name=6; By similarity
Topological domain368 – 37811Extracellular By similarity
Transmembrane379 – 40325Helical; Name=7; By similarity
Topological domain404 – 42118Cytoplasmic By similarity
Region112 – 12110Agonist binding By similarity
Region358 – 3625Agonist binding By similarity
Motif133 – 1353DRY motif; important for ligand-induced conformation changes By similarity
Motif396 – 4005NPxxY motif; important for ligand-induced conformation changes and signaling By similarity

Amino acid modifications

Glycosylation101N-linked (GlcNAc...) Potential
Glycosylation111N-linked (GlcNAc...) Potential
Glycosylation241N-linked (GlcNAc...) Potential
Glycosylation301N-linked (GlcNAc...) Potential
Disulfide bond109 ↔ 187 By similarity
Cross-link334Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Natural variant17 – 193EPF → DHL in strain: C3H/An.

Experimental info

Sequence conflict1771T → A in AAA81519. Ref.1
Sequence conflict2421F → L in AAA16850. Ref.6
Sequence conflict2471A → V in AAA16850. Ref.6
Sequence conflict2631C → W in AAA16850. Ref.6
Sequence conflict3041H → D in AAA81519. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q64264 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 74F519DF7CC0C7AA

FASTA42146,176
        10         20         30         40         50         60 
MDMFSLGQGN NTTTSLEPFG TGGNDTGLSN VTFSYQVITS LLLGTLIFCA VLGNACVVAA 

        70         80         90        100        110        120 
IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC 

       130        140        150        160        170        180 
TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED 

       190        200        210        220        230        240 
RSNPNECTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKVEKKGAGT 

       250        260        270        280        290        300 
SFGTSSAPPP KKSLNGQPGS GDCRRSAENR AVGTPCANGA VRQGEDDATL EVIEVHRVGN 

       310        320        330        340        350        360 
SKGHLPLPSE SGATSYVPAC LERKNERTAE AKRKMALARE RKTVKTLGII MGTFILCWLP 

       370        380        390        400        410        420 
FFIVALVLPF CESSCHMPEL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIIKCKFC 


R 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and differentiation-induced expression of a murine serotonin 1A receptor in a septal cell line."
Charest A., Wainer B.H., Albert P.R.
J. Neurosci. 13:5164-5171(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
Strain: NIH Swiss.
Tissue: Brain.
[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: Brain cortex, Corpora quadrigemina and Hippocampus.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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.
[5]"The serotonin 1a receptor gene contains a TATA-less promoter that responds to MAZ and Sp1."
Parks C.L., Shenk T.
J. Biol. Chem. 271:4417-4430(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
Strain: C3H/An.
[6]"Identification, chromosomal location, and genome organization of mammalian G-protein-coupled receptors."
Wilkie T.M., Chen Y., Gilbert D.J., Moore K.J., Yu L., Simon M.I., Copeland N.G., Jenkins N.A.
Genomics 18:175-184(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 136-353.
Tissue: Testis.
[7]"Serotonin receptor 1A knockout: an animal model of anxiety-related disorder."
Ramboz S., Oosting R., Amara D.A., Kung H.F., Blier P., Mendelsohn M., Mann J.J., Brunner D., Hen R.
Proc. Natl. Acad. Sci. U.S.A. 95:14476-14481(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, FUNCTION.
[8]"Altered serotonin and dopamine metabolism in the CNS of serotonin 5-HT(1A) or 5-HT(1B) receptor knockout mice."
Ase A.R., Reader T.A., Hen R., Riad M., Descarries L.
J. Neurochem. 75:2415-2426(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[9]"Embryonic and postnatal development of the serotonergic raphe system and its target regions in 5-HT1A receptor deletion or overexpressing mouse mutants."
Deng D.R., Djalali S., Holtje M., Grosse G., Stroh T., Voigt I., Kusserow H., Theuring F., Ahnert-Hilger G., Hortnagl H.
Neuroscience 147:388-402(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[10]"Sporadic autonomic dysregulation and death associated with excessive serotonin autoinhibition."
Audero E., Coppi E., Mlinar B., Rossetti T., Caprioli A., Banchaabouchi M.A., Corradetti R., Gross C.
Science 321:130-133(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Serotonin-1A autoreceptors are necessary and sufficient for the normal formation of circuits underlying innate anxiety."
Richardson-Jones J.W., Craige C.P., Nguyen T.H., Kung H.F., Gardier A.M., Dranovsky A., David D.J., Guiard B.P., Beck S.G., Hen R., Leonardo E.D.
J. Neurosci. 31:6008-6018(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U39391 mRNA. Translation: AAA81519.1.
AK043668 mRNA. Translation: BAC31611.1.
AK049814 mRNA. Translation: BAC33931.1.
AK049884 mRNA. Translation: BAC33970.1.
AK140194 mRNA. Translation: BAE24273.1.
CH466568 Genomic DNA. Translation: EDL18479.1.
BC138669 mRNA. Translation: AAI38670.1.
BC138681 mRNA. Translation: AAI38682.1.
U33820 Genomic DNA. Translation: AAC52572.1.
L20339 mRNA. Translation: AAA16850.1.
CCDSCCDS26756.1.
PIRI49375.
RefSeqNP_032334.2. NM_008308.4.
UniGeneMm.4716.

3D structure databases

ProteinModelPortalQ64264.
SMRQ64264. Positions 30-418.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000022235.

Chemistry

BindingDBQ64264.
ChEMBLCHEMBL3737.
GuidetoPHARMACOLOGY1.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteQ64264.

Proteomic databases

PRIDEQ64264.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022235; ENSMUSP00000022235; ENSMUSG00000021721.
GeneID15550.
KEGGmmu:15550.
UCSCuc007rtu.2. mouse.

Organism-specific databases

CTD3350.
MGIMGI:96273. Htr1a.

Phylogenomic databases

eggNOGNOG249628.
GeneTreeENSGT00750000117301.
HOGENOMHOG000239242.
HOVERGENHBG106962.
InParanoidQ8BGS4.
KOK04153.
OMAREWRQGV.
OrthoDBEOG7NCV3Q.
TreeFamTF316350.

Gene expression databases

BgeeQ64264.
CleanExMM_HTR1A.
GenevestigatorQ64264.

Family and domain databases

Gene3D1.20.1070.10. 2 hits.
InterProIPR000610. 5HT1A_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24247:SF20. PTHR24247:SF20. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00512. 5HT1ARECEPTR.
PR01101. 5HTRECEPTOR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio288480.
PROQ64264.
SOURCESearch...

Entry information

Entry name5HT1A_MOUSE
AccessionPrimary (citable) accession number: Q64264
Secondary accession number(s): Q60956, Q61617, Q8BGS4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 127 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

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