ADB4C_MELGA
ID ADB4C_MELGA Reviewed; 428 AA.
AC P43141;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Beta-4C adrenergic receptor;
DE AltName: Full=Beta-4C adrenoreceptor;
DE Short=Beta-4C adrenoceptor;
GN Name=ADRB4C;
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=7929160; DOI=10.1016/s0021-9258(17)31464-3;
RA Chen X.-H., Harden T.K., Nicholas R.A.;
RT "Molecular cloning and characterization of a novel beta-adrenergic
RT receptor.";
RL J. Biol. Chem. 269:24810-24819(1994).
CC -!- FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced
CC activation of adenylate cyclase through the action of G proteins.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Broad tissue distribution.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Adrenergic receptor subfamily. ADRB4C sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U13977; AAA62150.1; -; mRNA.
DR EMBL; U13978; AAA62151.1; -; Genomic_DNA.
DR PIR; A55044; A55044.
DR RefSeq; NP_001290112.1; NM_001303183.1.
DR AlphaFoldDB; P43141; -.
DR SMR; P43141; -.
DR GeneID; 100379211; -.
DR KEGG; mgp:100379211; -.
DR CTD; 155; -.
DR InParanoid; P43141; -.
DR OrthoDB; 750855at2759; -.
DR Proteomes; UP000001645; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004940; F:beta1-adrenergic receptor activity; IEA:InterPro.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0045823; P:positive regulation of heart contraction; IEA:InterPro.
DR InterPro; IPR002233; ADR_fam.
DR InterPro; IPR000507; ADRB1_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
DR PRINTS; PR00561; ADRENRGCB1AR.
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; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..428
FT /note="Beta-4C adrenergic receptor"
FT /id="PRO_0000069111"
FT TOPO_DOM 1..25
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 26..49
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 50..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 59..77
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 78..97
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 98..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 120..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 142..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 165..189
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 190..211
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 212..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 262..283
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 284..294
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 295..315
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 316..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 359..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 329
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 428 AA; 47398 MW; E82DC920BE3B6889 CRC64;
MTPLPAGNGS VPNCSWAAVL SRQWAVGAAL SITILVIVAG NLLVIVAIAK TPRLQTMTNV
FVTSLACADL VMGLLVVPPG ATILLSGHWP YGTVVCELWT SLDVLCVTAS IETLCAIAVD
RYLAITAPLQ YEALVTKGRA WAVVCMVWAI SAFISFLPIM NHWWRDGADE QAVRCYDDPR
CCDFVTNMTY AIVSSTVSFY VPLLVMIFVY VRVFAVATRH VQLIGKDKVR FLQENPSLSS
RGGRWRRPSR LLAIKEHKAL KTLGIIMGTF TLCWLPFFVA NIIKVFCRPL VPDQLFLFLN
WLGYVNSAFN PIIYCRSPDF RSAFRKLLCC PRRADRRLHA APQDPQHCSC AFSPRGDPME
DSKAVDPGHL REDSEVQGSG RREENASSHG GGHQQRPLGE CWLQGMQSML CEQLDEFTST
EMPAGPSV
