GenomeNet

Database: UniProt
Entry: F7GIU0_MACMU
LinkDB: F7GIU0_MACMU
Original site: F7GIU0_MACMU 
ID   F7GIU0_MACMU            Unreviewed;       421 AA.
AC   F7GIU0; G7MU57;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=5-hydroxytryptamine receptor 1A {ECO:0000256|ARBA:ARBA00017605};
DE   AltName: Full=Serotonin receptor 1A {ECO:0000256|ARBA:ARBA00032310};
GN   Name=HTR1A {ECO:0000313|EMBL:AGN73490.1,
GN   ECO:0000313|Ensembl:ENSMMUP00000002380.1,
GN   ECO:0000313|VGNC:VGNC:73536};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000002380.1, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|EMBL:AGN73490.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mmul01 {ECO:0000313|EMBL:AGN73490.1}, Mmul02
RC   {ECO:0000313|EMBL:AGN73491.1}, Mmul03 {ECO:0000313|EMBL:AGN73492.1},
RC   Mmul05 {ECO:0000313|EMBL:AGN73493.1}, Mmul06
RC   {ECO:0000313|EMBL:AGN73494.1}, Mmul07 {ECO:0000313|EMBL:AGN73495.1},
RC   Mmul09 {ECO:0000313|EMBL:AGN73496.1}, Mmul13
RC   {ECO:0000313|EMBL:AGN73497.1}, Mmul14 {ECO:0000313|EMBL:AGN73498.1},
RC   Mmul15 {ECO:0000313|EMBL:AGN73499.1}, Mmul16
RC   {ECO:0000313|EMBL:AGN73500.1}, Mmul18 {ECO:0000313|EMBL:AGN73501.1},
RC   Mmul19 {ECO:0000313|EMBL:AGN73502.1}, Mmul20
RC   {ECO:0000313|EMBL:AGN73503.1}, Mmul22 {ECO:0000313|EMBL:AGN73504.1},
RC   Mmul23 {ECO:0000313|EMBL:AGN73505.1}, Mmul24
RC   {ECO:0000313|EMBL:AGN73506.1}, Mmul25 {ECO:0000313|EMBL:AGN73507.1},
RC   Mmul26 {ECO:0000313|EMBL:AGN73508.1}, and Mmul27
RC   {ECO:0000313|EMBL:AGN73509.1};
RA   Shattuck M.R., Satkoski-Trask J., Deinard A., Tito R.Y., Smith D.G.,
RA   Melnick D.J., Malhi R.S.;
RT   "Natural selection on genes underlying the serotonin system in Macaca.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSMMUP00000002380.1}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000002380.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
CC       (serotonin). Also functions as a receptor for various drugs and
CC       psychoactive substances. Ligand binding causes a conformation change
CC       that triggers signaling via guanine nucleotide-binding proteins (G
CC       proteins) and modulates the activity of down-stream effectors, such as
CC       adenylate cyclase. Beta-arrestin family members inhibit signaling via G
CC       proteins and mediate activation of alternative signaling pathways.
CC       Signaling inhibits adenylate cyclase activity and activates a
CC       phosphatidylinositol-calcium second messenger system that regulates the
CC       release of Ca(2+) ions from intracellular stores. Plays a role in the
CC       regulation of 5-hydroxytryptamine release and in the regulation of
CC       dopamine and 5-hydroxytryptamine metabolism. Plays a role in the
CC       regulation of dopamine and 5-hydroxytryptamine levels in the brain, and
CC       thereby affects neural activity, mood and behavior. Plays a role in the
CC       response to anxiogenic stimuli. {ECO:0000256|ARBA:ARBA00024768}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell
CC       projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000256|RuleBase:RU000688}.
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DR   EMBL; KC862395; AGN73490.1; -; Genomic_DNA.
DR   EMBL; KC862396; AGN73491.1; -; Genomic_DNA.
DR   EMBL; KC862397; AGN73492.1; -; Genomic_DNA.
DR   EMBL; KC862398; AGN73493.1; -; Genomic_DNA.
DR   EMBL; KC862399; AGN73494.1; -; Genomic_DNA.
DR   EMBL; KC862400; AGN73495.1; -; Genomic_DNA.
DR   EMBL; KC862401; AGN73496.1; -; Genomic_DNA.
DR   EMBL; KC862402; AGN73497.1; -; Genomic_DNA.
DR   EMBL; KC862403; AGN73498.1; -; Genomic_DNA.
DR   EMBL; KC862404; AGN73499.1; -; Genomic_DNA.
DR   EMBL; KC862405; AGN73500.1; -; Genomic_DNA.
DR   EMBL; KC862406; AGN73501.1; -; Genomic_DNA.
DR   EMBL; KC862407; AGN73502.1; -; Genomic_DNA.
DR   EMBL; KC862408; AGN73503.1; -; Genomic_DNA.
DR   EMBL; KC862409; AGN73504.1; -; Genomic_DNA.
DR   EMBL; KC862410; AGN73505.1; -; Genomic_DNA.
DR   EMBL; KC862411; AGN73506.1; -; Genomic_DNA.
DR   EMBL; KC862412; AGN73507.1; -; Genomic_DNA.
DR   EMBL; KC862413; AGN73508.1; -; Genomic_DNA.
DR   EMBL; KC862414; AGN73509.1; -; Genomic_DNA.
DR   RefSeq; NP_001185629.1; NM_001198700.1.
DR   STRING; 9544.ENSMMUP00000002380; -.
DR   PaxDb; 9544-ENSMMUP00000002380; -.
DR   Ensembl; ENSMMUT00000002517.3; ENSMMUP00000002380.1; ENSMMUG00000001789.3.
DR   GeneID; 694991; -.
DR   KEGG; mcc:694991; -.
DR   CTD; 3350; -.
DR   VEuPathDB; HostDB:ENSMMUG00000001789; -.
DR   VGNC; VGNC:73536; HTR1A.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000154484; -.
DR   HOGENOM; CLU_009579_11_1_1; -.
DR   OMA; CAESCYM; -.
DR   OrthoDB; 2999405at2759; -.
DR   TreeFam; TF316350; -.
DR   Proteomes; UP000006718; Chromosome 6.
DR   Bgee; ENSMMUG00000001789; Expressed in prefrontal cortex and 3 other cell types or tissues.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0090722; F:receptor-receptor interaction; IEA:Ensembl.
DR   GO; GO:0051378; F:serotonin binding; IBA:GO_Central.
DR   GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0035640; P:exploration behavior; IEA:Ensembl.
DR   GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:Ensembl.
DR   GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
DR   GO; GO:0042053; P:regulation of dopamine metabolic process; IEA:Ensembl.
DR   GO; GO:0046883; P:regulation of hormone secretion; IEA:InterPro.
DR   GO; GO:0014062; P:regulation of serotonin secretion; IEA:Ensembl.
DR   GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR   GO; GO:0042428; P:serotonin metabolic process; IEA:Ensembl.
DR   GO; GO:0007210; P:serotonin receptor signaling pathway; IEA:Ensembl.
DR   CDD; cd15330; 7tmA_5-HT1A_vertebrates; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000610; 5HT1A_rcpt.
DR   InterPro; IPR002231; 5HT_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24248:SF191; G-PROTEIN COUPLED RECEPTORS FAMILY 1 PROFILE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00512; 5HT1ARECEPTR.
DR   PRINTS; PR01101; 5HTRECEPTOR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   G-protein coupled receptor {ECO:0000256|RuleBase:RU000688};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|RuleBase:RU000688, ECO:0000313|EMBL:AGN73490.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU000688};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000688};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        40..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        69..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        152..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        194..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        346..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        379..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          52..399
FT                   /note="G-protein coupled receptors family 1 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   421 AA;  45990 MW;  B66F6537793DEE16 CRC64;
     MDVLSPGQGN NTTSPPGPFE TSGNTTGISD VTSYQVITSL LLGTLIFCAV LGNACVVAAI
     ALERSLQNVA NYLIGSLAVT DLMVSVLVLP MAALYQVLNK WTLGQVTCDL FIALDVLCCT
     SSILHLCAIA LDRYWAITDP IDYVNKRTPR RAAALISLTW LIGFLISIPP MLGWRTPEDR
     SDPDACTISK DHGYTIYSTF GAFYIPLLLM LVLYGRIFRA ARFRIRKTVK KVEKTGADTR
     HGASPTPQPK KSVNGESGGR NWRLGVESKA GGALCANGAV RQGDDGAALE VIEVHRVGNS
     KEHLPLPSEA GSTPCASASF ERKNERNADA KRKMALARER KTVKTLGIIM GTFILCWLPF
     FIVALVLPFC ESSCHMPTLL GAIINWLGYS NSLLNPVIYA YFNKDFQNAF KKIIKCKFCR
     Q
//
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