ID   ADRA2_LABOS             Reviewed;         432 AA.
AC   Q91081;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Alpha-2 adrenergic receptor;
DE   AltName: Full=Alpha-2 adrenoreceptor;
DE            Short=Alpha-2 adrenoceptor;
OS   Labrus ossifagus (Cuckoo wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=30800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=7693288; DOI=10.1111/j.1476-5381.1993.tb13771.x;
RA   Svensson S.P.S., Bailey T.J., Pepperl D.J., Grundstroem N., Ala-Uotila S.,
RA   Scheinin M., Karlsson J.O.G., Regan J.W.;
RT   "Cloning and expression of a fish alpha 2-adrenoceptor.";
RL   Br. J. Pharmacol. 110:54-60(1993).
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; U07743; AAA17386.1; -; Unassigned_DNA.
DR   PIR; I50829; I50829.
DR   AlphaFoldDB; Q91081; -.
DR   SMR; Q91081; -.
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:0004938; F:alpha2-adrenergic receptor activity; IEA:InterPro.
DR   GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR   GO; GO:0006940; P:regulation of smooth muscle contraction; IEA:InterPro.
DR   GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR   InterPro; IPR002233; ADR_fam.
DR   InterPro; IPR000735; ADRA2C_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24248:SF25; PTHR24248:SF25; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01103; ADRENERGICR.
DR   PRINTS; PR00560; ADRENRGCA2CR.
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; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..432
FT                   /note="Alpha-2 adrenergic receptor"
FT                   /id="PRO_0000069110"
FT   TOPO_DOM        1..32
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        33..57
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        58..69
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        70..95
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        96..105
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        106..128
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        129..149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        150..172
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        173..188
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        189..212
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        213..356
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        357..380
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        381..393
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        394..413
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        414..432
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          222..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..304
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        5
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        18
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        105..183
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   432 AA;  48563 MW;  0A42FAF9849FA8BA CRC64;
     MDPLNATGMD AFTAIHLNAS WSADSGYSLA AIASIAALVS FLILFTVVGN ILVVIAVLTS
     RALKAPQNLF LVSLATADIL VATLVMPFSL ANELMGYWYF GKVWCGIYLA LDVLFCTSSI
     VHLCAISLDR YWSVTQAVEY NLKRTPKRVK CIIVIVWLIS AFISSPPLLS IDSNNYISSQ
     PQCMLNDDTW YILSSSMASF FAPCLIMILV YIRIYQVAKT RTRSMSGKEP RPDGVTQTEN
     GLNKANSPCH GDRENGHCQC PPTPSQRTVT IGQQTDDADM DESFSSEGKG HKPQRQDSQR
     AKRPGLKKSS ISKQSARISR VSNKSVDLFA SRRKRRRSSI AEKKVSQARE KRFTFVLAVV
     MGVFVVCWFP FFFSYSLHAV CRDYCKIPDT LFKFFWIGYC NSSLNPAIYT IFNRDFRRAF
     QKILCKSWKK SF