ID SUN_DROME Reviewed; 61 AA.
AC Q9VXN2; Q8IR24;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-NOV-2024, entry version 176.
DE RecName: Full=Protein stunted {ECO:0000305};
GN Name=sun {ECO:0000312|FlyBase:FBgn0014391};
GN ORFNames=CG9032 {ECO:0000312|FlyBase:FBgn0014391};
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|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 [2] {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).
RN [3] {ECO:0000312|EMBL:AAL48780.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL48780.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL48780.1}, and
RC Head {ECO:0000312|EMBL:AAL49366.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000312|EMBL:ACV82452.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:ACV82452.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:ANY27747.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:ANY27747.1};
RA Wan K., Booth B., Spirohn K., Hao T., Hu Y., Calderwood M., Hill D.,
RA Mohr S., Vidal M., Celniker S., Perrimon N.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND IDENTIFICATION BY MASS SPECTROMETRY
RP (ISOFORMS A AND B).
RX PubMed=15133470; DOI=10.1038/ncb1133;
RA Cvejic S., Zhu Z., Felice S.J., Berman Y., Huang X.Y.;
RT "The endogenous ligand Stunted of the GPCR Methuselah extends lifespan in
RT Drosophila.";
RL Nat. Cell Biol. 6:540-546(2004).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF ALA-3; TRP-4 AND ALA-6.
RX PubMed=19672878; DOI=10.1002/pro.221;
RA Ja W.W., Carvalho G.B., Madrigal M., Roberts R.W., Benzer S.;
RT "The Drosophila G protein-coupled receptor, Methuselah, exhibits a
RT promiscuous response to peptides.";
RL Protein Sci. 18:2203-2208(2009).
CC -!- FUNCTION: Activates the G-protein coupled receptor mth in vitro,
CC leading to increased intracellular calcium ion levels.
CC {ECO:0000269|PubMed:15133470, ECO:0000269|PubMed:19672878}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000312|FlyBase:FBgn0014391};
CC IsoId=Q9VXN2-1; Sequence=Displayed;
CC Name=B {ECO:0000312|FlyBase:FBgn0014391};
CC IsoId=Q9VXN2-2; Sequence=VSP_058581;
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. Heterozygotes show increased
CC lifespan and enhanced resistance to oxidative stress. ATP levels are
CC normal. {ECO:0000269|PubMed:15133470}.
CC -!- SIMILARITY: Belongs to the eukaryotic ATPase epsilon family.
CC {ECO:0000305}.
CC -!- CAUTION: Although related to the eukaryotic ATPase epsilon family,
CC there is no evidence for a function in the ATP synthase complex.
CC {ECO:0000269|PubMed:15133470}.
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DR EMBL; AE014298; AAF48526.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09369.1; -; Genomic_DNA.
DR EMBL; AY071158; AAL48780.1; -; mRNA.
DR EMBL; AY071744; AAL49366.1; -; mRNA.
DR EMBL; BT099753; ACV82452.1; -; mRNA.
DR EMBL; KX531597; ANY27747.1; -; mRNA.
DR RefSeq; NP_524682.1; NM_079943.4. [Q9VXN2-1]
DR RefSeq; NP_727905.1; NM_167468.3. [Q9VXN2-2]
DR AlphaFoldDB; Q9VXN2; -.
DR SMR; Q9VXN2; -.
DR ComplexPortal; CPX-8618; Mitochondrial proton-transporting ATP synthase complex.
DR IntAct; Q9VXN2; 3.
DR STRING; 7227.FBpp0073963; -.
DR PaxDb; 7227-FBpp0073963; -.
DR DNASU; 44046; -.
DR EnsemblMetazoa; FBtr0074176; FBpp0073963; FBgn0014391. [Q9VXN2-1]
DR EnsemblMetazoa; FBtr0074177; FBpp0073964; FBgn0014391. [Q9VXN2-2]
DR GeneID; 44046; -.
DR KEGG; dme:Dmel_CG9032; -.
DR UCSC; CG9032-RA; d. melanogaster. [Q9VXN2-1]
DR UCSC; CG9032-RB; d. melanogaster.
DR AGR; FB:FBgn0014391; -.
DR CTD; 44046; -.
DR FlyBase; FBgn0014391; sun.
DR VEuPathDB; VectorBase:FBgn0014391; -.
DR eggNOG; KOG3495; Eukaryota.
DR GeneTree; ENSGT00700000106200; -.
DR HOGENOM; CLU_187039_3_1_1; -.
DR InParanoid; Q9VXN2; -.
DR OMA; HIRITKW; -.
DR OrthoDB; 740at2759; -.
DR PhylomeDB; Q9VXN2; -.
DR Reactome; R-DME-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-DME-8949613; Cristae formation.
DR BioGRID-ORCS; 44046; 0 hits in 3 CRISPR screens.
DR ChiTaRS; sun; fly.
DR GenomeRNAi; 44046; -.
DR PRO; PR:Q9VXN2; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0014391; Expressed in male reproductive gland and 29 other cell types or tissues.
DR ExpressionAtlas; Q9VXN2; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); ISS:FlyBase.
DR GO; GO:0045269; C:proton-transporting ATP synthase, central stalk; ISS:FlyBase.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:FlyBase.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; ISS:FlyBase.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; ISS:FlyBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
DR CDD; cd12153; F1-ATPase_epsilon; 1.
DR FunFam; 1.10.1620.20:FF:000005; Uncharacterized protein, isoform A; 1.
DR Gene3D; 1.10.1620.20; ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial; 1.
DR InterPro; IPR006721; ATP_synth_F1_esu_mt.
DR InterPro; IPR036742; ATP_synth_F1_esu_sf_mt.
DR PANTHER; PTHR12448; ATP SYNTHASE EPSILON CHAIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12448:SF0; ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL; 1.
DR Pfam; PF04627; ATP-synt_Eps; 1.
DR SUPFAM; SSF48690; Epsilon subunit of mitochondrial F1F0-ATP synthase; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Reference proteome.
FT CHAIN 1..61
FT /note="Protein stunted"
FT /id="PRO_0000437960"
FT REGION 3..15
FT /note="Sufficient for mth activation"
FT /evidence="ECO:0000269|PubMed:19672878"
FT VAR_SEQ 54..61
FT /note="QRQTQSES -> HERA (in isoform B)"
FT /id="VSP_058581"
FT MUTAGEN 3
FT /note="A->S: Abolishes ability to activate mth."
FT /evidence="ECO:0000269|PubMed:19672878"
FT MUTAGEN 4
FT /note="W->A: Abolishes ability to activate mth."
FT /evidence="ECO:0000269|PubMed:19672878"
FT MUTAGEN 6
FT /note="A->S: Strongly reduces ability to activate mth."
FT /evidence="ECO:0000269|PubMed:19672878"
SQ SEQUENCE 61 AA; 6791 MW; FFCB824BC4612FED CRC64;
MTAWRAAGIT YIQYSNIAAR ILRESLKTGL RADAAKRDAS HVKFTPWANG KPAQRQTQSE
S
//
