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RYA_DROME
ID   RYA_DROME               Reviewed;         109 AA.
AC   G5CKU5; A8Y508; V9I0I4;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=RYamide neuropeptides {ECO:0000303|PubMed:21704020, ECO:0000303|PubMed:21843505};
DE   AltName: Full=Neuropeptide Y-like receptor ligand {ECO:0000303|PubMed:21704020, ECO:0000303|PubMed:21843505};
DE   Contains:
DE     RecName: Full=RYamide-1 {ECO:0000303|PubMed:21704020, ECO:0000303|PubMed:21843505};
DE   Contains:
DE     RecName: Full=RYamide-2 {ECO:0000303|PubMed:21704020, ECO:0000303|PubMed:21843505};
DE   Flags: Precursor;
GN   Name=RYa {ECO:0000303|PubMed:21704020, ECO:0000303|PubMed:21843505};
GN   Synonyms=NepYr {ECO:0000303|PubMed:21704020};
GN   ORFNames=CG40733 {ECO:0000312|FlyBase:FBgn0085512};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN   [1] {ECO:0000312|EMBL:AEP22449.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF RYAMIDE-1 AND RYAMIDE-2, FUNCTION,
RP   SUBCELLULAR LOCATION, AND AMIDATION AT TYR-33 AND TYR-63.
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|EMBL:BAM66571.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-33 AND 54-63, SYNTHESIS
RP   OF RYAMIDE-1 AND RYAMIDE-2, FUNCTION, SUBCELLULAR LOCATION, AND AMIDATION
RP   AT TYR-33 AND TYR-63.
RX   PubMed=21704020; DOI=10.1016/j.bbrc.2011.06.081;
RA   Ida T., Takahashi T., Tominaga H., Sato T., Kume K., Ozaki M.,
RA   Hiraguchi T., Maeda T., Shiotani H., Terajima S., Sano H., Mori K.,
RA   Yoshida M., Miyazato M., Kato J., Murakami N., Kangawa K., Kojima M.;
RT   "Identification of the novel bioactive peptides dRYamide-1 and dRYamide-2,
RT   ligands for a neuropeptide Y-like receptor in Drosophila.";
RL   Biochem. Biophys. Res. Commun. 410:872-877(2011).
RN   [3] {ECO:0000312|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4] {ECO:0000312|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
CC   -!- FUNCTION: Neuropeptides RYamide-1 and RYamide-2 are ligands for the G-
CC       protein coupled receptor RYa-R (PubMed:21843505, PubMed:21704020). May
CC       suppress feeding behavior (PubMed:21704020).
CC       {ECO:0000269|PubMed:21704020, ECO:0000269|PubMed:21843505}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21704020,
CC       ECO:0000305|PubMed:21843505}.
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DR   EMBL; HQ698845; ADZ15313.1; -; mRNA.
DR   EMBL; JN222358; AEP22449.1; -; mRNA.
DR   EMBL; AB638268; BAM66571.1; -; mRNA.
DR   EMBL; AE013599; EDP28140.3; -; Genomic_DNA.
DR   RefSeq; NP_001104382.3; NM_001110912.3.
DR   AlphaFoldDB; G5CKU5; -.
DR   STRING; 7227.FBpp0302660; -.
DR   PaxDb; G5CKU5; -.
DR   EnsemblMetazoa; FBtr0310523; FBpp0302660; FBgn0085512.
DR   GeneID; 5740597; -.
DR   KEGG; dme:Dmel_CG40733; -.
DR   CTD; 5740597; -.
DR   FlyBase; FBgn0085512; RYa.
DR   VEuPathDB; VectorBase:FBgn0085512; -.
DR   HOGENOM; CLU_2186633_0_0_1; -.
DR   OrthoDB; 1590016at2759; -.
DR   ChiTaRS; RYa-R; fly.
DR   GenomeRNAi; 5740597; -.
DR   PRO; PR:G5CKU5; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0085512; Expressed in midgut and 11 other tissues.
DR   GO; GO:0005576; C:extracellular region; IC:FlyBase.
DR   GO; GO:0005615; C:extracellular space; IC:FlyBase.
DR   GO; GO:0048018; F:receptor ligand activity; IPI:FlyBase.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR   GO; GO:2000252; P:negative regulation of feeding behavior; IDA:FlyBase.
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; Direct protein sequencing;
KW   Neuropeptide; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000305|PubMed:21704020"
FT   PEPTIDE         25..33
FT                   /note="RYamide-1"
FT                   /evidence="ECO:0000269|PubMed:21704020,
FT                   ECO:0000305|PubMed:21843505"
FT                   /id="PRO_0000439148"
FT   PROPEP          36..53
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000439149"
FT   PEPTIDE         54..63
FT                   /note="RYamide-2"
FT                   /evidence="ECO:0000269|PubMed:21704020,
FT                   ECO:0000305|PubMed:21843505"
FT                   /id="PRO_0000439150"
FT   PROPEP          67..109
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000439151"
FT   MOD_RES         33
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000305|PubMed:21704020,
FT                   ECO:0000305|PubMed:21843505"
FT   MOD_RES         63
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000305|PubMed:21704020,
FT                   ECO:0000305|PubMed:21843505"
SQ   SEQUENCE   109 AA;  13167 MW;  5C22387ECBEB53D4 CRC64;
     MNECVNKLLH LKFLFYFILG IQKRPVFFVA SRYGRSTTYD ESLKSRRIFI VPRNEHFFLG
     SRYGKRSGKY LCLSREINKL IVRKRLRNND KERTPTLSFI TKHFLMRNT
 
 
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