ID   RYAR_TRICA              Reviewed;         367 AA.
AC   G4WMX4;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=RYamide receptor {ECO:0000303|PubMed:21843505};
GN   Name=RYa-R {ECO:0000303|PubMed:21843505};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000312|EMBL:ADZ17181.1};
RN   [1] {ECO:0000312|EMBL:ADZ17181.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21843505; DOI=10.1016/j.bbrc.2011.07.131;
RA   Collin C., Hauser F., Krogh-Meyer P., Hansen K.K., Gonzalez de Valdivia E.,
RA   Williamson M., Grimmelikhuijzen C.J.;
RT   "Identification of the Drosophila and Tribolium receptors for the recently
RT   discovered insect RYamide neuropeptides.";
RL   Biochem. Biophys. Res. Commun. 412:578-583(2011).
CC   -!- FUNCTION: Receptor for the neuropeptides RYamide-1 and RYamide-2. The
CC       activity of this receptor is mediated by G proteins which activate a
CC       phosphatidyl-inositol-calcium second messenger system. RYamide-2 is the
CC       most potent activator. {ECO:0000269|PubMed:21843505}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21843505};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000305}.
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DR   EMBL; HQ709383; ADZ17181.1; -; mRNA.
DR   RefSeq; NP_001280539.1; NM_001293610.1.
DR   AlphaFoldDB; G4WMX4; -.
DR   SMR; G4WMX4; -.
DR   STRING; 7070.TC001056-PA; -.
DR   GeneID; 664001; -.
DR   KEGG; tca:664001; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   HOGENOM; CLU_009579_6_1_1; -.
DR   OrthoDB; 715197at2759; -.
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:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000611; NPY_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01012; NRPEPTIDEYR.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..367
FT                   /note="RYamide receptor"
FT                   /id="PRO_0000439157"
FT   TOPO_DOM        1..35
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        36..56
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..66
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        67..87
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        88..113
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        114..134
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..143
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        144..164
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..212
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        213..233
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        234..258
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        259..279
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        280..282
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        283..303
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..367
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        8
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   367 AA;  41851 MW;  E99D9449EFA565A5 CRC64;
     MDANTTRNES FSLDCELVNP NSTLANVYFL SAVYSMYAII FVVALIGNSF VCYIVLSSPP
     MRTVTNFFIL NLAIGDVLIT LLCVPFTSVS LLMQYWPFGG ILCPVVNYSQ ALSVFVSAYT
     LVAISIDKYM IIMWPLKPRI SKRFATYIIA LVWLIAGITV LPSATFTTLI NDENILGTSA
     YEQCDKYICA EEYSKVGQEY GDLYTKVLMF LQYVIPSLVL LFTYTSIGVV IWCHRIPGEA
     ENSRDQRIAK NKTKMIKMMV TVVCVYTICW LPYNVLMIFK EHISGSVMVY LYFPLHGLAM
     SHACYNPIIY CYMNARFRNG FLQVMMSIPC LRRCNSINDI SKILTCRWKV RRVHLYREIT
     RAQPTSA