CHMP5_DROME
ID CHMP5_DROME Reviewed; 226 AA.
AC Q9VVI9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Charged multivesicular body protein 5;
DE AltName: Full=Vacuolar protein-sorting-associated protein 60 {ECO:0000312|FlyBase:FBgn0036740};
GN Name=Vps60 {ECO:0000312|FlyBase:FBgn0036740};
GN ORFNames=CG6259 {ECO:0000312|FlyBase:FBgn0036740};
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=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-226, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24762813; DOI=10.1242/jcs.144519;
RA Berns N., Woichansky I., Friedrichsen S., Kraft N., Riechmann V.;
RT "A genome-scale in vivo RNAi analysis of epithelial development in
RT Drosophila identifies new proliferation domains outside of the stem cell
RT niche.";
RL J. Cell Sci. 127:2736-2748(2014).
CC -!- FUNCTION: Probable peripherally associated component of the endosomal
CC sorting required for transport complex III (ESCRT-III) which is
CC involved in multivesicular bodies (MVBs) formation and sorting of
CC endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles
CC (ILVs) that are generated by invagination and scission from the
CC limiting membrane of the endosome and are delivered to lysosomes
CC enabling degradation of membrane proteins (By similarity). Specifically
CC down-regulates Notch signaling activity in the germarium, probably by
CC facilitating Notch endocytosis (PubMed:24762813).
CC {ECO:0000250|UniProtKB:Q9BY43, ECO:0000269|PubMed:24762813}.
CC -!- SUBUNIT: Probable peripherally associated component of the endosomal
CC sorting required for transport complex III (ESCRT-III). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Homozygous lethal. RNAi-mediated knockdown in
CC ovarian follicle epithelium results in cell proliferation in the
CC germarium epithelium. Stalks between adjacent egg chambers/ follicles
CC become elongated due to increased number of cells and the linear
CC arrangement of germline cysts is also disturbed.
CC {ECO:0000269|PubMed:24762813}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; AE014296; AAF49322.2; -; Genomic_DNA.
DR EMBL; AY071206; AAL48828.1; -; mRNA.
DR RefSeq; NP_001261994.1; NM_001275065.1.
DR RefSeq; NP_648997.1; NM_140740.4.
DR AlphaFoldDB; Q9VVI9; -.
DR SMR; Q9VVI9; -.
DR BioGRID; 65251; 18.
DR IntAct; Q9VVI9; 2.
DR STRING; 7227.FBpp0305334; -.
DR iPTMnet; Q9VVI9; -.
DR PaxDb; Q9VVI9; -.
DR PRIDE; Q9VVI9; -.
DR DNASU; 39964; -.
DR EnsemblMetazoa; FBtr0075201; FBpp0074964; FBgn0036740.
DR EnsemblMetazoa; FBtr0333123; FBpp0305334; FBgn0036740.
DR GeneID; 39964; -.
DR KEGG; dme:Dmel_CG6259; -.
DR UCSC; CG6259-RA; d. melanogaster.
DR CTD; 39964; -.
DR FlyBase; FBgn0036740; Vps60.
DR VEuPathDB; VectorBase:FBgn0036740; -.
DR eggNOG; KOG1655; Eukaryota.
DR GeneTree; ENSGT00550000074817; -.
DR HOGENOM; CLU_079409_1_0_1; -.
DR InParanoid; Q9VVI9; -.
DR OMA; MEQAQTM; -.
DR OrthoDB; 1301560at2759; -.
DR PhylomeDB; Q9VVI9; -.
DR SignaLink; Q9VVI9; -.
DR BioGRID-ORCS; 39964; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39964; -.
DR PRO; PR:Q9VVI9; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036740; Expressed in saliva-secreting gland and 10 other tissues.
DR ExpressionAtlas; Q9VVI9; baseline and differential.
DR Genevisible; Q9VVI9; DM.
DR GO; GO:0000815; C:ESCRT III complex; NAS:FlyBase.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; ISS:FlyBase.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR GO; GO:0046718; P:viral entry into host cell; HMP:FlyBase.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR22761; PTHR22761; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endosome; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..226
FT /note="Charged multivesicular body protein 5"
FT /id="PRO_0000372645"
FT REGION 188..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 21..93
FT /evidence="ECO:0000255"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 226
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 226 AA; 25151 MW; B7D3AEA5EAF824F4 CRC64;
MNRLFGRGKP KEPGPSLNDC IAGVDARATN IEEKISNLEA ELRKYREQMS KMREGPAKNS
VKQKALRVLK QKKAYEQQAE SLRNQSFNME QANYAAQSLK DTQATVAAMK DGVKQMKTEY
KKINIDQIED IQDDMADMFE QADEVQEALG RTYGMPEVDD DDLQAELDAL GDEIALDDDT
SYLDDVVKAP EAPSREPGAD SIVPGKSTIE TDEFGLPKIP TSLKTT
