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Database: UniProt
Entry: A0A093EMR5_9AVES
LinkDB: A0A093EMR5_9AVES
Original site: A0A093EMR5_9AVES 
ID   A0A093EMR5_9AVES        Unreviewed;       303 AA.
AC   A0A093EMR5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Kappa-type opioid receptor {ECO:0000256|ARBA:ARBA00021098};
DE   Flags: Fragment;
GN   ORFNames=N339_05505 {ECO:0000313|EMBL:KFV15851.1};
OS   Pterocles gutturalis (yellow-throated sandgrouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; Pterocles.
OX   NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV15851.1, ECO:0000313|Proteomes:UP000053149};
RN   [1] {ECO:0000313|EMBL:KFV15851.1, ECO:0000313|Proteomes:UP000053149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV15851.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: G-protein coupled opioid receptor that functions as a
CC       receptor for endogenous alpha-neoendorphins and dynorphins, but has low
CC       affinity for beta-endorphins. Also functions as a receptor for various
CC       synthetic opioids and for the psychoactive diterpene salvinorin A.
CC       Ligand binding causes a conformation change that triggers signaling via
CC       guanine nucleotide-binding proteins (G proteins) and modulates the
CC       activity of down-stream effectors, such as adenylate cyclase. Signaling
CC       leads to the inhibition of adenylate cyclase activity. Inhibits
CC       neurotransmitter release by reducing calcium ion currents and
CC       increasing potassium ion conductance. Plays a role in the perception of
CC       pain. Plays a role in mediating reduced physical activity upon
CC       treatment with synthetic opioids. Plays a role in the regulation of
CC       salivation in response to synthetic opioids. May play a role in arousal
CC       and regulation of autonomic and neuroendocrine functions.
CC       {ECO:0000256|ARBA:ARBA00043871}.
CC   -!- SUBUNIT: Interacts with NHERF1. Interacts with GABARAPL1.
CC       {ECO:0000256|ARBA:ARBA00034801}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000256|RuleBase:RU000688}.
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DR   EMBL; KL247675; KFV15851.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093EMR5; -.
DR   Proteomes; UP000053149; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0038048; F:dynorphin receptor activity; IEA:InterPro.
DR   GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000452; Kappa_opi_rcpt.
DR   InterPro; IPR001418; Opioid_rcpt.
DR   PANTHER; PTHR24229:SF1; KAPPA-TYPE OPIOID RECEPTOR; 1.
DR   PANTHER; PTHR24229; NEUROPEPTIDES RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00532; KAPPAOPIOIDR.
DR   PRINTS; PR00384; OPIOIDR.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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   Behavior {ECO:0000256|ARBA:ARBA00022610};
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW   ECO:0000256|RuleBase:RU000688};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000688};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053149};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU000688};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000688};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        104..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        143..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        196..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        235..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..254
FT                   /note="G-protein coupled receptors family 1 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV15851.1"
FT   NON_TER         303
FT                   /evidence="ECO:0000313|EMBL:KFV15851.1"
SQ   SEQUENCE   303 AA;  34850 MW;  5AD397F289CD8EDE CRC64;
     NKTLFFLFVR YTKMKTATNI YIFNLAMADA LVTTTMPFQS TEYLMNSWPF GDVLCKIVIS
     IDYYNMFTSI FTLTMMSVDR YIAVCHPVKA LDFRTPLKAK IINICIWLLS SSVGISAIVL
     GGTKVREDTA STECSLQFPD RDYVWWDIFM KICVFVFAFV IPVLIIIVCY TLMILRLKSV
     RLLSGSQEKD RNLRRITRLV LVVVAVFIVC WTPIHIFVLV EALGDVSHST AAISSYYFCI
     ALGYTNSSLN PILYAFLDEN FKRCFKDFCF PFKMRMDRQS TSRVRNTVQD PAYMREADGT
     NKP
//
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