ADA1A_RABIT
ID ADA1A_RABIT Reviewed; 466 AA.
AC O02824;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Alpha-1A adrenergic receptor;
DE AltName: Full=Alpha-1A adrenoreceptor;
DE Short=Alpha-1A adrenoceptor;
DE AltName: Full=Alpha-1C adrenergic receptor;
GN Name=ADRA1A; Synonyms=ADRA1C;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9180361; DOI=10.1016/s0024-3205(97)00194-x;
RA Miyamoto S., Taniguchi T., Suzuki F., Takita M., Kosaka N., Negoro E.,
RA Okuda T., Kosaka H., Murata S., Nakamura S., Akagi Y., Oshita M.,
RA Watanabe Y., Muramatsu I.;
RT "Cloning, functional expression and tissue distribution of rabbit alpha1a-
RT adrenoceptor.";
RL Life Sci. 60:2069-2074(1997).
CC -!- FUNCTION: This alpha-adrenergic receptor mediates its action by
CC association with G proteins that activate a phosphatidylinositol-
CC calcium second messenger system. Its effect is mediated by G(q) and
CC G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate
CC phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homo- and heterooligomer. Heterooligomerizes with ADRA1B
CC homooligomers in cardiac myocytes. Interacts with CAVIN4.
CC {ECO:0000250|UniProtKB:P35348}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane; Multi-pass membrane protein.
CC Cell membrane {ECO:0000250|UniProtKB:P35348}; Multi-pass membrane
CC protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35348}.
CC Membrane, caveola {ECO:0000250|UniProtKB:P35348}. Note=Location at the
CC nuclear membrane facilitates heterooligomerization and regulates ERK-
CC mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as
CC well as LAP2 at the nuclear membrane of cardiac myocytes (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Abundant in liver, vas deferens, brain, and aorta,
CC but not in heart.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Adrenergic receptor subfamily. ADRA1A sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U81982; AAB61334.1; -; mRNA.
DR RefSeq; NP_001075849.1; NM_001082380.1.
DR AlphaFoldDB; O02824; -.
DR SMR; O02824; -.
DR STRING; 9986.ENSOCUP00000018013; -.
DR BindingDB; O02824; -.
DR ChEMBL; CHEMBL3637; -.
DR Ensembl; ENSOCUT00000023786; ENSOCUP00000018013; ENSOCUG00000000775.
DR Ensembl; ENSOCUT00000035932; ENSOCUP00000028378; ENSOCUG00000000775.
DR GeneID; 100009237; -.
DR KEGG; ocu:100009237; -.
DR CTD; 148; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000159105; -.
DR InParanoid; O02824; -.
DR OrthoDB; 1095345at2759; -.
DR PRO; PR:O02824; -.
DR Proteomes; UP000001811; Chromosome 2.
DR Bgee; ENSOCUG00000000775; Expressed in liver and 14 other tissues.
DR ExpressionAtlas; O02824; baseline.
DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004937; F:alpha1-adrenergic receptor activity; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0007512; P:adult heart development; IEA:Ensembl.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
DR GO; GO:0001985; P:negative regulation of heart rate involved in baroreceptor response to increased systemic arterial blood pressure; IEA:Ensembl.
DR GO; GO:0150099; P:neuron-glial cell signaling; IEA:Ensembl.
DR GO; GO:0001994; P:norepinephrine-epinephrine vasoconstriction involved in regulation of systemic arterial blood pressure; IEA:Ensembl.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0097195; P:pilomotor reflex; IEA:Ensembl.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IEA:Ensembl.
DR GO; GO:0001996; P:positive regulation of heart rate by epinephrine-norepinephrine; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:1903997; P:positive regulation of non-membrane spanning protein tyrosine kinase activity; IEA:Ensembl.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0001997; P:positive regulation of the force of heart contraction by epinephrine-norepinephrine; IEA:Ensembl.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IEA:InterPro.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR InterPro; IPR002233; ADR_fam.
DR InterPro; IPR001004; ADRA1A_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
DR PRINTS; PR00557; ADRENRGCA1AR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Nucleus; Palmitate; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..466
FT /note="Alpha-1A adrenergic receptor"
FT /id="PRO_0000069065"
FT TOPO_DOM 1..25
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 26..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 52..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 64..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 90..99
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 100..122
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 123..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 144..168
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 169..181
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 182..205
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 206..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 273..297
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 298..304
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 305..329
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 330..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 334..349
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT LIPID 345
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 466 AA; 51365 MW; 9446D356B50FCDE0 CRC64;
MVFLSGNASD SSNCTHPPAP VNISKAILLG VILGGLILFG VLGNILVILS VACHRHLHSV
THYYIVNLAV ADLLLTSTVL PFSAIFEILG YWAFGRVFCN IWAAVDVLCC TASIISLCVI
SIDRYIGVSY PLRYPTIVTQ RRGLRALLCV WAFSLVISVG PLFGWRQPAP DDETICQINE
EPGYVLFSAL GSFYVPLTII LAMYCRVYVV AKRESRGLKS GLKTDKSDSE QVTLRIHRKN
APAGGSGVAS AKNKTHFSVR LLKFSREKKA AKTLGIVVGC FVLCWLPFFL VMPIGSFFPD
FKPPETVFKI VFWLGYLNSC INPIIYPCSS QEFKKAFQNV LKIQCLRRKQ SSKHALGYTL
HAPSQALEGQ HKDMVRIPVG SGETFYKISK TDGVCEWKFF SSMPRGSARI TVPKDQSACT
TARVRSKSFL QVCCCVGPST PNPGENHQVP TIKIHTISLS ENGEEV
