ID   ADRA2_CARAU             Reviewed;         436 AA.
AC   P32251;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Alpha-2 adrenergic receptor;
DE   AltName: Full=Alpha-2 adrenoreceptor;
DE            Short=Alpha-2 adrenoceptor;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Shih Y.-L., Chang N.-C.A., Chang A.C., Lo S.J.;
RT   "Molecular cloning and expression of goldfish adrenoceptor.";
RL   Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-
CC       induced inhibition of adenylate cyclase through the action of G
CC       proteins.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; L09064; AAA49163.1; -; Genomic_DNA.
DR   AlphaFoldDB; P32251; -.
DR   SMR; P32251; -.
DR   Proteomes; UP000515129; Genome assembly.
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:0004935; F:adrenergic receptor activity; IEA:InterPro.
DR   InterPro; IPR002233; ADR_fam.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01103; ADRENERGICR.
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   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..436
FT                   /note="Alpha-2 adrenergic receptor"
FT                   /id="PRO_0000069109"
FT   TOPO_DOM        1..27
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        28..52
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        53..64
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        65..90
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        91..100
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        101..123
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        124..144
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        145..167
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        168..178
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        179..202
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        203..329
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        330..353
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        354..366
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        367..387
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        388..436
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          238..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..280
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        7
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        14
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        100..173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   436 AA;  49258 MW;  8A471EEA068DDED4 CRC64;
     MDVTQSNATK DDANITVTPW PYTETAAAFI ILVVSVIILV SIVGNVLVIV AVLTSRALRA
     PQNLFLVSLA CADILVATLV IPFSLANEIM GYWFFGSTWC AFYLALDVLF CTSSIVHLCA
     ISLDRYWSVT KAVSYNLKRT PKRIKSMIAV VWVISAVISF PPLIMTKHDE KECLINDETW
     YILSSSLVSF FAPGFIMITV YCKIYRVAKQ RSSTVFVAKN GLERQPSQSE TCFVRKDKFE
     KESPSSNSSE SNQRQEELDD IDLEESATSD NKPKSSRFSN RRRVDGARCC PQRTCRISWV
     SSQEQSSKQL AVASKTKVAQ MREKRFTFVL TVVMGVFVLC WFPFFFTYSL HAICGDSCEP
     PEALFKLFFW IGYCNSSVNP IIYTIFNRDF RKAFKKICLL DCAAHLRDSC LGTLGRLNAK
     CIFECHQKSN QEETAN