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P18090

- ADRB1_RAT

UniProt

P18090 - ADRB1_RAT

Protein

Beta-1 adrenergic receptor

Gene

Adrb1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Mediates Ras activation through G(s)-alpha- and cAMP-mediated signaling.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei138 – 1381Agonist or antagonistBy similarity
    Binding sitei143 – 1431Agonist or antagonistBy similarity

    GO - Molecular functioni

    1. beta1-adrenergic receptor activity Source: RGD
    2. dopamine binding Source: RGD
    3. drug binding Source: RGD
    4. epinephrine binding Source: RGD
    5. norepinephrine binding Source: RGD
    6. protein binding Source: IntAct
    7. Ras guanyl-nucleotide exchange factor activity Source: UniProtKB
    8. receptor signaling protein activity Source: UniProtKB

    GO - Biological processi

    1. adenylate cyclase-activating adrenergic receptor signaling pathway Source: UniProtKB
    2. aging Source: RGD
    3. apoptotic process Source: RGD
    4. brown fat cell differentiation Source: Ensembl
    5. diet induced thermogenesis Source: Ensembl
    6. fear response Source: Ensembl
    7. glycogen catabolic process Source: RGD
    8. G-protein coupled receptor signaling pathway Source: RGD
    9. heat generation Source: Ensembl
    10. lipid homeostasis Source: RGD
    11. memory Source: RGD
    12. negative regulation of multicellular organism growth Source: Ensembl
    13. negative regulation of smooth muscle contraction Source: RGD
    14. negative regulation of urine volume Source: RGD
    15. positive regulation of apoptotic process Source: RGD
    16. positive regulation of cAMP biosynthetic process Source: RGD
    17. positive regulation of cAMP-mediated signaling Source: UniProtKB
    18. positive regulation of cation channel activity Source: RGD
    19. positive regulation of cell growth involved in cardiac muscle cell development Source: RGD
    20. positive regulation of heart rate Source: RGD
    21. positive regulation of heart rate by epinephrine-norepinephrine Source: Ensembl
    22. positive regulation of Ras GTPase activity Source: UniProtKB
    23. positive regulation of renin secretion into blood stream Source: RGD
    24. positive regulation of saliva secretion Source: RGD
    25. positive regulation of systemic arterial blood pressure Source: RGD
    26. positive regulation of the force of heart contraction by norepinephrine Source: RGD
    27. protein localization to organelle Source: RGD
    28. regulation of calcium ion transport Source: RGD
    29. regulation of cardiac muscle cell contraction Source: RGD
    30. regulation of inhibitory postsynaptic membrane potential Source: RGD
    31. response to cold Source: Ensembl
    32. Rho protein signal transduction Source: RGD
    33. sensory perception of pain Source: RGD
    34. vasodilation by norepinephrine-epinephrine involved in regulation of systemic arterial blood pressure Source: Ensembl
    35. wound healing Source: RGD

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-1 adrenergic receptor
    Alternative name(s):
    Beta-1 adrenoreceptor
    Short name:
    Beta-1 adrenoceptor
    Gene namesi
    Name:Adrb1
    Synonyms:Adrb1r
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi2059. Adrb1.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication. Early endosome By similarity
    Note: Localized at the plasma membrane. Found in the Golgi upon GOPC overexpression By similarity. Colocalizes with RAPGEF2 at the plasma membrane.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: RGD
    2. early endosome Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW
    4. intracellular membrane-bounded organelle Source: RGD
    5. membrane Source: RGD
    6. nucleus Source: RGD
    7. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi466 – 4661V → A: Abolishes interaction with MAGI3. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 466466Beta-1 adrenergic receptorPRO_0000069124Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi15 – 151N-linked (GlcNAc...)Curated
    Disulfide bondi131 ↔ 216PROSITE-ProRule annotation
    Disulfide bondi209 ↔ 215PROSITE-ProRule annotation
    Modified residuei296 – 2961Phosphoserine; by PKASequence Analysis
    Modified residuei301 – 3011Phosphoserine; by PKASequence Analysis
    Lipidationi381 – 3811S-palmitoyl cysteineBy similarity
    Modified residuei401 – 4011Phosphoserine; by PKASequence Analysis

    Post-translational modificationi

    Homologous desensitization of the receptor is mediated by its phosphorylation by beta-adrenergic receptor kinase.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PRIDEiP18090.

    PTM databases

    PhosphoSiteiP18090.

    Expressioni

    Tissue specificityi

    Expressed in cortical neurons and coronary artery smooth muscle cells (at protein level).1 Publication

    Gene expression databases

    GenevestigatoriP18090.

    Interactioni

    Subunit structurei

    Interacts (via C-terminus PDZ motif) with RAPGEF2; the interaction is direct By similarity. Interacts with GOPC, MAGI3 and DLG4.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Magi3Q9JK713EBI-991303,EBI-696226

    Protein-protein interaction databases

    DIPiDIP-36293N.
    IntActiP18090. 1 interaction.
    STRINGi10116.ENSRNOP00000022813.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FF9model-A34-384[»]
    ProteinModelPortaliP18090.
    SMRiP18090. Positions 56-380.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5555ExtracellularBy similarityAdd
    BLAST
    Topological domaini85 – 939CytoplasmicBy similarity
    Topological domaini121 – 13212ExtracellularBy similarityAdd
    BLAST
    Topological domaini155 – 17218CytoplasmicBy similarityAdd
    BLAST
    Topological domaini197 – 22226ExtracellularBy similarityAdd
    BLAST
    Topological domaini249 – 30860CytoplasmicBy similarityAdd
    BLAST
    Topological domaini339 – 3435ExtracellularBy similarity
    Topological domaini367 – 466100CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei56 – 8429Helical; Name=1By similarityAdd
    BLAST
    Transmembranei94 – 12027Helical; Name=2By similarityAdd
    BLAST
    Transmembranei133 – 15422Helical; Name=3By similarityAdd
    BLAST
    Transmembranei173 – 19624Helical; Name=4By similarityAdd
    BLAST
    Transmembranei223 – 24826Helical; Name=5By similarityAdd
    BLAST
    Transmembranei309 – 33830Helical; Name=6By similarityAdd
    BLAST
    Transmembranei344 – 36623Helical; Name=7By similarityAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni218 – 23215Agonist and antagonist bindingBy similarityAdd
    BLAST
    Regioni326 – 3338Agonist and antagonist bindingBy similarity
    Regioni352 – 3565Agonist and antagonist bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi463 – 4664PDZ-BindingBy similarity

    Domaini

    The PDZ domain-binding motif mediates competitive interactions with GOPC, MAGI3 and DLG4 and plays a role in subcellular location of the receptor.

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB1 sub-subfamily.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG262978.
    GeneTreeiENSGT00720000108411.
    HOGENOMiHOG000239242.
    HOVERGENiHBG106962.
    InParanoidiP18090.
    KOiK04141.
    OrthoDBiEOG7BS4BS.
    PhylomeDBiP18090.
    TreeFamiTF316350.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR002233. ADR_fam.
    IPR000507. ADRB1_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view]
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR01103. ADRENERGICR.
    PR00561. ADRENRGCB1AR.
    PR00237. GPCRRHODOPSN.
    PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P18090-1 [UniParc]FASTAAdd to Basket

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    MGAGALALGA SEPCNLSSAA PLPDGAATAA RLLVLASPPA SLLPPASEGS    50
    APLSQQWTAG MGLLLALIVL LIVVGNVLVI VAIAKTPRLQ TLTNLFIMSL 100
    ASADLVMGLL VVPFGATIVV WGRWEYGSFF CELWTSVDVL CVTASIETLC 150
    VIALDRYLAI TLPFRYQSLL TRARARALVC TVWAISALVS FLPILMHWWR 200
    AESDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM AFVYLRVFRE 250
    AQKQVKKIDS CERRFLTGPP RPPSPAPSPS PGPPRPADSL ANGRSSKRRP 300
    SRLVALREQK ALKTLGIIMG VFTLCWLPFF LANVVKAFHR DLVPDRLFVF 350
    FNWLGYANSA FNPIIYCRSP DFRKAFQRLL CCARRAACRR RAAHGDRPRA 400
    SGCLARAGPP PSPGAPSDDD DDDAGATPPA RLLEPWAGCN GGTTTVDSDS 450
    SLDEPGRQGF SSESKV 466
    Length:466
    Mass (Da):50,472
    Last modified:November 1, 1990 - v1
    Checksum:i2955CB024944A12B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1621L → S in BAA00527. (PubMed:2167473)Curated
    Sequence conflicti267 – 2671T → S in BAA00527. (PubMed:2167473)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05561 Genomic DNA. Translation: AAA40792.1.
    D00634 Genomic DNA. Translation: BAA00527.1.
    PIRiS12591.
    RefSeqiNP_036833.1. NM_012701.1.
    UniGeneiRn.87064.

    Genome annotation databases

    EnsembliENSRNOT00000022813; ENSRNOP00000022813; ENSRNOG00000017002.
    GeneIDi24925.
    KEGGirno:24925.
    UCSCiRGD:2059. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05561 Genomic DNA. Translation: AAA40792.1 .
    D00634 Genomic DNA. Translation: BAA00527.1 .
    PIRi S12591.
    RefSeqi NP_036833.1. NM_012701.1.
    UniGenei Rn.87064.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FF9 model - A 34-384 [» ]
    ProteinModelPortali P18090.
    SMRi P18090. Positions 56-380.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36293N.
    IntActi P18090. 1 interaction.
    STRINGi 10116.ENSRNOP00000022813.

    Chemistry

    BindingDBi P18090.
    ChEMBLi CHEMBL3252.
    GuidetoPHARMACOLOGYi 28.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P18090.

    Proteomic databases

    PRIDEi P18090.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000022813 ; ENSRNOP00000022813 ; ENSRNOG00000017002 .
    GeneIDi 24925.
    KEGGi rno:24925.
    UCSCi RGD:2059. rat.

    Organism-specific databases

    CTDi 153.
    RGDi 2059. Adrb1.

    Phylogenomic databases

    eggNOGi NOG262978.
    GeneTreei ENSGT00720000108411.
    HOGENOMi HOG000239242.
    HOVERGENi HBG106962.
    InParanoidi P18090.
    KOi K04141.
    OrthoDBi EOG7BS4BS.
    PhylomeDBi P18090.
    TreeFami TF316350.

    Miscellaneous databases

    NextBioi 604879.
    PROi P18090.

    Gene expression databases

    Genevestigatori P18090.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR002233. ADR_fam.
    IPR000507. ADRB1_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view ]
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR01103. ADRENERGICR.
    PR00561. ADRENRGCB1AR.
    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. "Molecular cloning and expression of the rat beta 1-adrenergic receptor gene."
      Machida C.A., Bunzow J.R., Searles R.P., van Tol H.H.M., Tester B., Neve K.A., Teal P., Nipper V., Civelli O.
      J. Biol. Chem. 265:12960-12965(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Primary structure of the rat beta-1 adrenergic receptor gene."
      Shimomura H., Terada A.
      Nucleic Acids Res. 18:4591-4591(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Direct binding of the beta1 adrenergic receptor to the cyclic AMP-dependent guanine nucleotide exchange factor CNrasGEF leads to Ras activation."
      Pak Y., Pham N., Rotin D.
      Mol. Cell. Biol. 22:7942-7952(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "Proteomic analysis of beta1-adrenergic receptor interactions with PDZ scaffold proteins."
      He J., Bellini M., Inuzuka H., Xu J., Xiong Y., Yang X., Castleberry A.M., Hall R.A.
      J. Biol. Chem. 281:2820-2827(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAGI3, MUTAGENESIS OF VAL-466.

    Entry informationi

    Entry nameiADRB1_RAT
    AccessioniPrimary (citable) accession number: P18090
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3