ADA1B_CANLF
ID ADA1B_CANLF Reviewed; 417 AA.
AC P11615;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Alpha-1B adrenergic receptor;
DE AltName: Full=Alpha-1B adrenoreceptor;
DE Short=Alpha-1B adrenoceptor;
DE Flags: Fragment;
GN Name=ADRA1B; Synonyms=RDC5;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thyroid;
RX PubMed=2541503; DOI=10.1126/science.2541503;
RA Libert F., Parmentier M., Lefort A., Dinsart C., van Sande J., Maenhaut C.,
RA Simons M.-J., Dumont J.E., Vassart G.;
RT "Selective amplification and cloning of four new members of the G protein-
RT coupled receptor family.";
RL Science 244:569-572(1989).
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:P35368}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Cell membrane
CC {ECO:0000250|UniProtKB:P35368}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35368}. Membrane,
CC caveola {ECO:0000250|UniProtKB:P35368}. Note=Location at the nuclear
CC membrane facilitates heterooligomerization and regulates ERK-mediated
CC signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as
CC LAP2 at the nuclear membrane of cardiac myocytes (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Adrenergic receptor subfamily. ADRA1B sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X14050; CAA32208.1; -; mRNA.
DR PIR; E30341; E30341.
DR RefSeq; NP_001183964.2; NM_001197035.2.
DR AlphaFoldDB; P11615; -.
DR SMR; P11615; -.
DR STRING; 9612.ENSCAFP00000025460; -.
DR PaxDb; P11615; -.
DR GeneID; 403962; -.
DR KEGG; cfa:403962; -.
DR CTD; 147; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P11615; -.
DR OrthoDB; 1095345at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0001996; P:positive regulation of heart rate by epinephrine-norepinephrine; IBA:GO_Central.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IBA:GO_Central.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IEA:InterPro.
DR InterPro; IPR002233; ADR_fam.
DR InterPro; IPR001115; ADRA1B_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24248:SF17; PTHR24248:SF17; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
DR PRINTS; PR00556; ADRENRGCA1BR.
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; Disulfide bond; G-protein coupled receptor;
KW Lipoprotein; Membrane; Nucleus; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN <1..417
FT /note="Alpha-1B adrenergic receptor"
FT /id="PRO_0000069068"
FT TRANSMEM <1..8
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 9..20
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 21..44
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 45..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 65..87
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 88..104
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 105..127
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 128..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 199..222
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 223..229
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 230..254
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 255..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 295..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 371..381
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 308..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97717"
FT LIPID 268
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT DISULFID 21..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 1
SQ SEQUENCE 417 AA; 45892 MW; D523397626E12F64 CRC64;
VLPFSAALEV LGYWVLGRIF CDIWAAVDVL CCTASILSLC AISIDRYIGV RYSLQYPTLV
TRRKAILALL GVWVLSTVIS IGPLLGWKEP APNDDKECGV TEEPFYALFS SLGSFYIPLA
VILVMYCRVY IVAKRTTKNL EAGVMKEMSN SKELTLRIHS KNFHEDTLSS TKAKGHNPRS
SIAVKLFKFS REKKAAKTLG IVVGMFILCW LPFFIALPLG SLFSTLKPPD AVFKVVFWLG
YFNSCLNPII YPCSSKEFKR AFVRILGCQC RGRRRRRRRR RLGGCAYTYR PWTRGGSLER
SQSRKDSLDD SGSCLSGSQR TLPSASPSPG YLGRAAPPPV ELCAVPEWKA PGALLSLPAP
QPPGRRGRRD SGPLFTFRLL AERGSPAAGD GACRPAPDAA NGQPGFKTNM PLAPGQF
