VPS25_DROME
ID VPS25_DROME Reviewed; 174 AA.
AC Q7JXV9;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Vacuolar protein-sorting-associated protein 25;
DE AltName: Full=ESCRT-II complex subunit VPS25;
DE AltName: Full=Vacuolar protein sorting 25;
GN Name=Vps25; Synonyms=l(2)44Db; ORFNames=CG14750;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
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]
RP INTERACTION WITH LSN/SNF8/VPS22.
RX PubMed=14605208; DOI=10.1126/science.1090289;
RA Giot L., Bader J.S., Brouwer C., Chaudhuri A., Kuang B., Li Y., Hao Y.L.,
RA Ooi C.E., Godwin B., Vitols E., Vijayadamodar G., Pochart P., Machineni H.,
RA Welsh M., Kong Y., Zerhusen B., Malcolm R., Varrone Z., Collis A.,
RA Minto M., Burgess S., McDaniel L., Stimpson E., Spriggs F., Williams J.,
RA Neurath K., Ioime N., Agee M., Voss E., Furtak K., Renzulli R.,
RA Aanensen N., Carrolla S., Bickelhaupt E., Lazovatsky Y., DaSilva A.,
RA Zhong J., Stanyon C.A., Finley R.L. Jr., White K.P., Braverman M.,
RA Jarvie T., Gold S., Leach M., Knight J., Shimkets R.A., McKenna M.P.,
RA Chant J., Rothberg J.M.;
RT "A protein interaction map of Drosophila melanogaster.";
RL Science 302:1727-1736(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16256743; DOI=10.1016/j.devcel.2005.09.019;
RA Vaccari T., Bilder D.;
RT "The Drosophila tumor suppressor vps25 prevents nonautonomous
RT overproliferation by regulating notch trafficking.";
RL Dev. Cell 9:687-698(2005).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16256745; DOI=10.1016/j.devcel.2005.09.020;
RA Thompson B.J., Mathieu J., Sung H.H., Loeser E., Rorth P., Cohen S.M.;
RT "Tumor suppressor properties of the ESCRT-II complex component Vps25 in
RT Drosophila.";
RL Dev. Cell 9:711-720(2005).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=17088062; DOI=10.1016/j.cub.2006.09.031;
RA Childress J.L., Acar M., Tao C., Halder G.;
RT "Lethal giant discs, a novel C2-domain protein, restricts notch activation
RT during endocytosis.";
RL Curr. Biol. 16:2228-2233(2006).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=16611691; DOI=10.1242/dev.02356;
RA Herz H.M., Chen Z., Scherr H., Lackey M., Bolduc C., Bergmann A.;
RT "vps25 mosaics display non-autonomous cell survival and overgrowth, and
RT autonomous apoptosis.";
RL Development 133:1871-1880(2006).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17935992; DOI=10.1016/j.cub.2007.09.032;
RA Rusten T.E., Vaccari T., Lindmo K., Rodahl L.M., Nezis I.P.,
RA Sem-Jacobsen C., Wendler F., Vincent J.P., Brech A., Bilder D.,
RA Stenmark H.;
RT "ESCRTs and Fab1 regulate distinct steps of autophagy.";
RL Curr. Biol. 17:1817-1825(2007).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17268469; DOI=10.1038/nature05503;
RA Irion U., St Johnston D.;
RT "bicoid RNA localization requires specific binding of an endosomal sorting
RT complex.";
RL Nature 445:554-558(2007).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19132102; DOI=10.1371/journal.pone.0004165;
RA Herz H.M., Woodfield S.E., Chen Z., Bolduc C., Bergmann A.;
RT "Common and distinct genetic properties of ESCRT-II components in
RT Drosophila.";
RL PLoS ONE 4:E4165-E4165(2009).
CC -!- FUNCTION: Component of the ESCRT-II complex (endosomal sorting complex
CC required for transport II), which is required for multivesicular body
CC (MVB) formation and sorting of endosomal cargo proteins into MVBs. The
CC MVB pathway mediates delivery of transmembrane proteins into the lumen
CC of the lysosome for degradation. The ESCRT-II complex is probably
CC involved in the recruitment of the ESCRT-III complex (By similarity).
CC Seems to function as a tumor suppressor by regulating Notch
CC trafficking, hence preventing non-autonomous overproliferation. May be
CC involved in the regulation of autophagy. ESCRT-II interacts with bicoid
CC mRNA, which is required for the anterior localization of bicoid mRNA in
CC the developing egg. {ECO:0000250, ECO:0000269|PubMed:16256743,
CC ECO:0000269|PubMed:16256745, ECO:0000269|PubMed:17268469,
CC ECO:0000269|PubMed:17935992, ECO:0000269|PubMed:19132102}.
CC -!- SUBUNIT: Component of the endosomal sorting complex required for
CC transport II (ESCRT-II) (By similarity). Interacts with Lsn/Snf8/Vps22
CC (Probable). {ECO:0000250, ECO:0000305}.
CC -!- INTERACTION:
CC Q7JXV9; Q9VD72: lsn; NbExp=3; IntAct=EBI-98834, EBI-104459;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome membrane
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Vps25 mutant cells exhibit multivesicular body
CC sorting defects, with large amounts of ubiquitinated proteins detected
CC on endosomes. This leads to activation of signals (through Notch and
CC Dpp receptors) that drive cell proliferation, non-autonomous
CC overgrowth, loss of epithelial organization, and render cells sensitive
CC to apoptosis. Vps25 mutant cells display accumulation of
CC autophagosomes. Bicoid mRNA is mislocalized in developing eggs.
CC {ECO:0000269|PubMed:16256743, ECO:0000269|PubMed:16256745,
CC ECO:0000269|PubMed:16611691, ECO:0000269|PubMed:17088062,
CC ECO:0000269|PubMed:17268469, ECO:0000269|PubMed:17935992,
CC ECO:0000269|PubMed:19132102}.
CC -!- SIMILARITY: Belongs to the VPS25 family. {ECO:0000305}.
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DR EMBL; AE013599; AAF59066.1; -; Genomic_DNA.
DR EMBL; AY089657; AAL90395.1; -; mRNA.
DR RefSeq; NP_610398.1; NM_136554.3.
DR AlphaFoldDB; Q7JXV9; -.
DR SMR; Q7JXV9; -.
DR BioGRID; 61697; 17.
DR IntAct; Q7JXV9; 7.
DR STRING; 7227.FBpp0087774; -.
DR MoonProt; Q7JXV9; -.
DR PaxDb; Q7JXV9; -.
DR PRIDE; Q7JXV9; -.
DR DNASU; 35847; -.
DR EnsemblMetazoa; FBtr0088694; FBpp0087774; FBgn0022027.
DR GeneID; 35847; -.
DR KEGG; dme:Dmel_CG14750; -.
DR UCSC; CG14750-RA; d. melanogaster.
DR CTD; 84313; -.
DR FlyBase; FBgn0022027; Vps25.
DR VEuPathDB; VectorBase:FBgn0022027; -.
DR eggNOG; KOG4068; Eukaryota.
DR GeneTree; ENSGT00390000014892; -.
DR HOGENOM; CLU_087657_0_1_1; -.
DR InParanoid; Q7JXV9; -.
DR OMA; SQEFHGM; -.
DR OrthoDB; 1094121at2759; -.
DR PhylomeDB; Q7JXV9; -.
DR Reactome; R-DME-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR BioGRID-ORCS; 35847; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35847; -.
DR PRO; PR:Q7JXV9; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0022027; Expressed in saliva-secreting gland and 12 other tissues.
DR Genevisible; Q7JXV9; DM.
DR GO; GO:0000814; C:ESCRT II complex; ISS:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; ISS:FlyBase.
DR GO; GO:0097352; P:autophagosome maturation; IMP:FlyBase.
DR GO; GO:0045450; P:bicoid mRNA localization; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IMP:FlyBase.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IMP:FlyBase.
DR GO; GO:0010669; P:epithelial structure maintenance; IMP:FlyBase.
DR GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IMP:FlyBase.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IMP:FlyBase.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0070086; P:ubiquitin-dependent endocytosis; IMP:FlyBase.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:FlyBase.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.10.570; -; 1.
DR InterPro; IPR008570; ESCRT-II_cplx_Vps25-sub.
DR InterPro; IPR014041; ESCRT-II_cplx_Vps25-sub_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13149; PTHR13149; 1.
DR Pfam; PF05871; ESCRT-II; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Endosome; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..174
FT /note="Vacuolar protein-sorting-associated protein 25"
FT /id="PRO_0000386527"
SQ SEQUENCE 174 AA; 20608 MW; 0711584CC2727233 CRC64;
MAEFQWPWEY TFPPFFTLQP HEETRQQQLK VWTDLFLKYL RHTNRFTLSI GDQNSPLFHN
EALKRRLSPE LVLAILGELE RSGHANPLDK RRQEWQVYWF TLEEYGNMVY DWVQETGQTN
TICTLYEIAS GENTSHLDFY GVDEAVLLSA LRLLEEKGRC ELIEMDGSHG VKFF
