RYA_TRICA
ID RYA_TRICA Reviewed; 128 AA.
AC D6WT67;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=RYamide neuropeptides {ECO:0000303|PubMed:21843505};
DE Contains:
DE RecName: Full=RYamide-1 {ECO:0000303|PubMed:21843505};
DE Contains:
DE RecName: Full=RYamide-2 {ECO:0000303|PubMed:21843505};
DE Flags: Precursor;
GN Name=RYa {ECO:0000303|PubMed:21843505};
GN ORFNames=TC008650 {ECO:0000312|EMBL:EFA05855.1};
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|Proteomes:UP000007266};
RN [1] {ECO:0000312|EMBL:AEP22448.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF RYAMIDE-1 AND RYAMIDE-2, FUNCTION,
RP SUBCELLULAR LOCATION, AND AMIDATION AT TYR-44 AND TYR-73.
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).
RN [2] {ECO:0000312|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000312|Proteomes:UP000007266};
RX PubMed=18362917; DOI=10.1038/nature06784;
RG Tribolium Genome Sequencing Consortium;
RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT "The genome of the model beetle and pest Tribolium castaneum.";
RL Nature 452:949-955(2008).
RN [3] {ECO:0000312|Proteomes:UP000007266}
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2 {ECO:0000312|Proteomes:UP000007266};
RX PubMed=19820115; DOI=10.1093/nar/gkp807;
RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT for Tribolium castaneum.";
RL Nucleic Acids Res. 38:D437-D442(2010).
CC -!- FUNCTION: Neuropeptides RYamide-1 and RYamide-2 are ligands for the G-
CC protein coupled receptor RYa-R. RYamide-2 is the most potent activator
CC of RYa-R. {ECO:0000269|PubMed:21843505}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21843505}.
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DR EMBL; JN200817; AEP22448.1; -; mRNA.
DR EMBL; KQ971354; EFA05855.1; -; Genomic_DNA.
DR RefSeq; NP_001280530.1; NM_001293601.1.
DR AlphaFoldDB; D6WT67; -.
DR STRING; 7070.TC008650-PA; -.
DR EnsemblMetazoa; TC008650_001; TC008650_001; TC008650.
DR GeneID; 100750223; -.
DR KEGG; tca:100750223; -.
DR eggNOG; ENOG502SGHQ; Eukaryota.
DR HOGENOM; CLU_1817660_0_0_1; -.
DR InParanoid; D6WT67; -.
DR OrthoDB; 1634058at2759; -.
DR PhylomeDB; D6WT67; -.
DR Proteomes; UP000007266; Linkage group 7.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Neuropeptide;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 26..29
FT /evidence="ECO:0000305"
FT /id="PRO_0000439152"
FT PEPTIDE 32..44
FT /note="RYamide-1"
FT /evidence="ECO:0000305|PubMed:21843505"
FT /id="PRO_0000439153"
FT PROPEP 47..63
FT /evidence="ECO:0000305"
FT /id="PRO_0000439154"
FT PEPTIDE 64..73
FT /note="RYamide-2"
FT /evidence="ECO:0000305|PubMed:21843505"
FT /id="PRO_0000439155"
FT PROPEP 77..128
FT /evidence="ECO:0000305"
FT /id="PRO_0000439156"
FT MOD_RES 44
FT /note="Tyrosine amide"
FT /evidence="ECO:0000305|PubMed:21843505"
FT MOD_RES 73
FT /note="Tyrosine amide"
FT /evidence="ECO:0000305|PubMed:21843505"
SQ SEQUENCE 128 AA; 14298 MW; 62DD396A2679FE5C CRC64;
MHARKLIVVL VYILTVLVSV AVSKRYTSEK RVQNLATFKT MMRYGRGGPS PNNKENKVNI
RPRADAFFLG PRYGKRSGWS PNASLVYPVS TPLCGLDEDL SCAYTGISDL YRCTPRKGES
EEFTTSSN
