ADA2A_BOVIN
ID ADA2A_BOVIN Reviewed; 468 AA.
AC Q28838; A0A3Q1LKS4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2019, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Alpha-2A adrenergic receptor {ECO:0000250|UniProtKB:P08913};
DE AltName: Full=Alpha-2A adrenoreceptor;
DE Short=Alpha-2A adrenoceptor;
DE Short=Alpha-2AAR;
DE AltName: Full=Alpha-2D adrenergic receptor;
GN Name=ADRA2A {ECO:0000250|UniProtKB:P08913};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9450652; DOI=10.1023/a:1006830303140;
RA Venkataraman V., Duda T., Sharma R.K.;
RT "The bovine alpha 2D-adrenergic receptor gene: structure, expression in
RT retina, and pharmacological characterization of the encoded receptor.";
RL Mol. Cell. Biochem. 177:113-123(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 186-225.
RX PubMed=8412494; DOI=10.1016/0024-3205(93)90600-8;
RA Blaxall H.S., Heck D.A., Bylund D.B.;
RT "Molecular determinants of the alpha-2D adrenergic receptor subtype.";
RL Life Sci. 53:PL255-PL259(1993).
CC -!- FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-
CC induced inhibition of adenylate cyclase through the action of G
CC proteins. Component of the ATAC complex, a complex with histone
CC acetyltransferase activity on histones H3 and H4 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the ADA2A-containing complex (ATAC), composed of
CC KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Retina, brain and olfactory lobe.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Adrenergic receptor subfamily. ADRA2A sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-16 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24958.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC24958.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U79030; AAC24958.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DAAA02059210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S66295; AAB28450.1; -; mRNA.
DR PIR; I46958; I46958.
DR RefSeq; NP_776924.1; NM_174499.1.
DR RefSeq; XP_015316217.1; XM_015460731.1.
DR PDB; 6K41; EM; 2.90 A; R=37-44.
DR PDBsum; 6K41; -.
DR AlphaFoldDB; Q28838; -.
DR BMRB; Q28838; -.
DR SMR; Q28838; -.
DR ChEMBL; CHEMBL4744; -.
DR DrugCentral; Q28838; -.
DR PRIDE; Q28838; -.
DR Ensembl; ENSBTAT00000054173; ENSBTAP00000057072; ENSBTAG00000039292.
DR GeneID; 282135; -.
DR KEGG; bta:282135; -.
DR CTD; 150; -.
DR VEuPathDB; HostDB:ENSBTAG00000039292; -.
DR VGNC; VGNC:106632; ADRA2A.
DR GeneTree; ENSGT00940000161451; -.
DR InParanoid; Q28838; -.
DR OMA; KILCRVD; -.
DR OrthoDB; 737211at2759; -.
DR PRO; PR:Q28838; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000039292; Expressed in myometrium and 87 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0098691; C:dopaminergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0031696; F:alpha-2C adrenergic receptor binding; IEA:Ensembl.
DR GO; GO:0004938; F:alpha2-adrenergic receptor activity; IBA:GO_Central.
DR GO; GO:0051379; F:epinephrine binding; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0032795; F:heterotrimeric G-protein binding; IEA:Ensembl.
DR GO; GO:0051380; F:norepinephrine binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0031996; F:thioesterase binding; IEA:Ensembl.
DR GO; GO:0032148; P:activation of protein kinase B activity; IEA:Ensembl.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0071881; P:adenylate cyclase-inhibiting adrenergic receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
DR GO; GO:0042596; P:fear response; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IEA:Ensembl.
DR GO; GO:0071882; P:phospholipase C-activating adrenergic receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl.
DR GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; IEA:Ensembl.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IEA:Ensembl.
DR GO; GO:0090303; P:positive regulation of wound healing; IEA:Ensembl.
DR GO; GO:0035624; P:receptor transactivation; IEA:Ensembl.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; IEA:InterPro.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR InterPro; IPR002233; ADR_fam.
DR InterPro; IPR001946; ADRA2A_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01103; ADRENERGICR.
DR PRINTS; PR00558; ADRENRGCA2AR.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Methylation; Palmitate;
KW Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..468
FT /note="Alpha-2A adrenergic receptor"
FT /id="PRO_0000069078"
FT TOPO_DOM 1..48
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 49..74
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 75..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 86..111
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 112..121
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 122..144
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 145..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 165..188
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 189..207
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 208..232
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 233..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 393..417
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 418..427
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 428..448
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 449..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 242..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22909"
FT MOD_RES 370
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01338"
FT LIPID 460
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 121..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 468 AA; 51123 MW; 5BF2624C369A0707 CRC64;
MFRQEQPLAE GSFAPMGSLQ PDAGNASWNG TEAPGGGARA TPYSLQVTLT LVCLAGLLML
FTVFGNVLVI IAVFTSRALK APQNLFLVSL ASADILVATL VIPFSLANEV MGYWYFGKAW
CEIYLALDVL FCTSSIVHLC AISLDRYWSI TQAIEYNLKR TPRRIKAIIV TVWVISAVIS
FPPLISFEKK RGRSGQPSAE PRCEINDQKW YVISSSIGSF FAPCLIMILV YVRIYQIAKR
RTRVPPSRRG PDATAAELPG SAERRPNGLG PERGGVGPVG AEVESLQVQL NGAPGEPAPA
GPPDADALDL EESSSSEHAE RPPGSRRSER GPRAKGKARA SQVKPGDSLP RRGPGATGLG
APTAGPAEER SGGGAKASRW RGRQNREKRF TFVLAVVIGV FVVCWFPFFF TYTLTAIGCP
VPPTLFKFFF WFGYCNSSLN PVIYTIFNHD FRRAFKKILC RGDRKRIV
