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Q61616

- DRD1_MOUSE

UniProt

Q61616 - DRD1_MOUSE

Protein

D(1A) dopamine receptor

Gene

Drd1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (30 May 2003)
      Previous versions | rss
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    Functioni

    Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase.

    GO - Molecular functioni

    1. dopamine binding Source: Ensembl
    2. dopamine neurotransmitter receptor activity Source: MGI
    3. dopamine neurotransmitter receptor activity, coupled via Gs Source: MGI
    4. G-protein coupled receptor activity Source: MGI
    5. protein binding Source: MGI

    GO - Biological processi

    1. activation of adenylate cyclase activity Source: MGI
    2. adenylate cyclase-activating dopamine receptor signaling pathway Source: MGI
    3. adult walking behavior Source: MGI
    4. associative learning Source: MGI
    5. astrocyte development Source: MGI
    6. behavioral fear response Source: MGI
    7. behavioral response to cocaine Source: MGI
    8. cellular response to catecholamine stimulus Source: Ensembl
    9. cerebral cortex GABAergic interneuron migration Source: MGI
    10. conditioned taste aversion Source: MGI
    11. dentate gyrus development Source: MGI
    12. dopamine receptor signaling pathway Source: MGI
    13. dopamine transport Source: MGI
    14. feeding behavior Source: MGI
    15. glucose import Source: MGI
    16. G-protein coupled receptor signaling pathway Source: MGI
    17. grooming behavior Source: MGI
    18. habituation Source: MGI
    19. hippocampus development Source: MGI
    20. learning Source: MGI
    21. locomotory behavior Source: MGI
    22. long term synaptic depression Source: MGI
    23. long-term synaptic potentiation Source: MGI
    24. maternal behavior Source: MGI
    25. mating behavior Source: MGI
    26. memory Source: MGI
    27. muscle contraction Source: MGI
    28. neuronal action potential Source: MGI
    29. operant conditioning Source: MGI
    30. peristalsis Source: MGI
    31. phospholipase C-activating dopamine receptor signaling pathway Source: MGI
    32. positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway Source: InterPro
    33. positive regulation of cell migration Source: MGI
    34. positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: Ensembl
    35. positive regulation of release of sequestered calcium ion into cytosol Source: Ensembl
    36. positive regulation of synaptic transmission, glutamatergic Source: MGI
    37. protein import into nucleus Source: MGI
    38. regulation of dopamine metabolic process Source: MGI
    39. response to amphetamine Source: MGI
    40. response to cocaine Source: MGI
    41. response to drug Source: MGI
    42. sensitization Source: MGI
    43. striatum development Source: MGI
    44. synaptic transmission, dopaminergic Source: MGI
    45. temperature homeostasis Source: MGI
    46. transmission of nerve impulse Source: MGI
    47. vasodilation Source: InterPro
    48. visual learning Source: MGI

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D(1A) dopamine receptor
    Alternative name(s):
    Dopamine D1 receptor
    Gene namesi
    Name:Drd1
    Synonyms:Drd1a, Gpcr15
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:99578. Drd1a.

    Subcellular locationi

    Cell membrane By similarity; Multi-pass membrane protein By similarity. Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
    Note: Transport from the endoplasmic reticulum to the cell surface is regulated by interaction with DNAJC14.By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of plasma membrane Source: InterPro
    3. membrane Source: MGI
    4. nucleus Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 446446D(1A) dopamine receptorPRO_0000069375Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi4 – 41N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi95 ↔ 186PROSITE-ProRule annotation
    Lipidationi347 – 3471S-palmitoyl cysteineBy similarity
    Lipidationi351 – 3511S-palmitoyl cysteineBy similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Proteomic databases

    PaxDbiQ61616.
    PRIDEiQ61616.

    PTM databases

    PhosphoSiteiQ61616.

    Expressioni

    Gene expression databases

    BgeeiQ61616.
    CleanExiMM_DRD1A.
    GenevestigatoriQ61616.

    Interactioni

    Subunit structurei

    Interacts with DNAJC14 via its C-terminus. Interacts with DRD1IP.By similarity

    Protein-protein interaction databases

    BioGridi199305. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61616.
    SMRiQ61616. Positions 28-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2222ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini49 – 5911CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini87 – 959ExtracellularSequence Analysis
    Topological domaini119 – 13719CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini163 – 19230ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini219 – 27254CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini300 – 31213ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini338 – 446109CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei23 – 4826Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei60 – 8627Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei96 – 11823Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei138 – 16225Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei193 – 21826Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei273 – 29927Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei313 – 33725Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG262978.
    GeneTreeiENSGT00750000117368.
    HOGENOMiHOG000239242.
    HOVERGENiHBG106962.
    InParanoidiB2RPW8.
    KOiK04144.
    OMAiSPTTFDV.
    OrthoDBiEOG780RMN.
    PhylomeDBiQ61616.
    TreeFamiTF325181.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR001413. Dopamine_D1_rcpt.
    IPR000929. Dopamine_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view]
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00565. DOPAMINED1AR.
    PR00242. DOPAMINER.
    PR00237. GPCRRHODOPSN.
    PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q61616-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPNTSTMDE TGLPVERDFS FRILTACFLS LLILSTLLGN TLVCAAVIRF    50
    RHLRSKVTNF FVISLAVSDL LVAVLVMPWK AVAEIAGFWP FGSFCNIWVA 100
    FDIMCSTASI LNLCVISVDR YWAISSPFQY ERKMTPKAAF ILISVAWTLS 150
    VLISFIPVQL SWHKAKPTWP LDGNFTSLED AEDDNCDTRL SRTYAISSSL 200
    ISFYIPVAIM IVTYTSIYRI AQKQIRRISA LERAAVHAKN CQTTTGNGNP 250
    VECSQSESSF KMSFKRETKV LKTLSVIMGV FVCCWLPFFI SNCMVPFCGS 300
    EETQPFCIDS ITFDVFVWFG WANSSLNPII YAFNADFQKA FSTLLGCYRL 350
    CPTTNNAIET VSINNNGAVM FSSHHEPRGS ISKDCNLVYL IPHAVGSSED 400
    LKREEAGGIP KPLEKLSPAL SVILDYDTDV SLEKIQPVTH SGQHST 446
    Length:446
    Mass (Da):49,612
    Last modified:May 30, 2003 - v2
    Checksum:i509BA66F9DF82A74
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti193 – 1964TYAI → DIRH(PubMed:8288218)Curated
    Sequence conflicti240 – 2401N → S in AAA16848. (PubMed:8288218)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK044723 mRNA. Translation: BAC32050.1.
    BC137641 mRNA. Translation: AAI37642.1.
    BC137655 mRNA. Translation: AAI37656.1.
    L20336 mRNA. Translation: AAA16848.1.
    CCDSiCCDS26524.1.
    RefSeqiNP_001278730.1. NM_001291801.1.
    NP_034206.1. NM_010076.3.
    UniGeneiMm.54161.

    Genome annotation databases

    EnsembliENSMUST00000021932; ENSMUSP00000021932; ENSMUSG00000021478.
    GeneIDi13488.
    KEGGimmu:13488.
    UCSCiuc011yzm.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK044723 mRNA. Translation: BAC32050.1 .
    BC137641 mRNA. Translation: AAI37642.1 .
    BC137655 mRNA. Translation: AAI37656.1 .
    L20336 mRNA. Translation: AAA16848.1 .
    CCDSi CCDS26524.1.
    RefSeqi NP_001278730.1. NM_001291801.1.
    NP_034206.1. NM_010076.3.
    UniGenei Mm.54161.

    3D structure databases

    ProteinModelPortali Q61616.
    SMRi Q61616. Positions 28-346.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199305. 1 interaction.

    Chemistry

    BindingDBi Q61616.
    ChEMBLi CHEMBL3071.
    GuidetoPHARMACOLOGYi 214.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei Q61616.

    Proteomic databases

    PaxDbi Q61616.
    PRIDEi Q61616.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021932 ; ENSMUSP00000021932 ; ENSMUSG00000021478 .
    GeneIDi 13488.
    KEGGi mmu:13488.
    UCSCi uc011yzm.2. mouse.

    Organism-specific databases

    CTDi 13488.
    MGIi MGI:99578. Drd1a.

    Phylogenomic databases

    eggNOGi NOG262978.
    GeneTreei ENSGT00750000117368.
    HOGENOMi HOG000239242.
    HOVERGENi HBG106962.
    InParanoidi B2RPW8.
    KOi K04144.
    OMAi SPTTFDV.
    OrthoDBi EOG780RMN.
    PhylomeDBi Q61616.
    TreeFami TF325181.

    Miscellaneous databases

    NextBioi 283997.
    PROi Q61616.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q61616.
    CleanExi MM_DRD1A.
    Genevestigatori Q61616.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR001413. Dopamine_D1_rcpt.
    IPR000929. Dopamine_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view ]
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00565. DOPAMINED1AR.
    PR00242. DOPAMINER.
    PR00237. GPCRRHODOPSN.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
      , 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: Retina.
    2. "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.
    3. "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 193-279.
      Tissue: Testis.

    Entry informationi

    Entry nameiDRD1_MOUSE
    AccessioniPrimary (citable) accession number: Q61616
    Secondary accession number(s): B2RPW8, Q8C8P8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 30, 2003
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3