VPS28_DROME
ID VPS28_DROME Reviewed; 210 AA.
AC Q9V359;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Vacuolar protein sorting-associated protein 28 homolog;
DE AltName: Full=ESCRT-I complex subunit VPS28;
GN Name=Vps28; Synonyms=l(2)k16503; ORFNames=CG12770;
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 TSG101, AND DISRUPTION PHENOTYPE.
RX PubMed=15728719; DOI=10.1091/mbc.e04-11-1013;
RA Sevrioukov E.A., Moghrabi N., Kuhn M., Kramer H.;
RT "A mutation in dVps28 reveals a link between a subunit of the endosomal
RT sorting complex required for transport-I complex and the actin cytoskeleton
RT in Drosophila.";
RL Mol. Biol. Cell 16:2301-2312(2005).
CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular
CC trafficking process. {ECO:0000250}.
CC -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Death at the transition from the first to second
CC instar. Morphological changes in MVBs and developmental defects in the
CC compound eye. However, for the ligands and receptors tested, changes in
CC their cell surface levels or their delivery to lysosomes have not been
CC detected. In early embryos and during sperm individualization defects
CC in actin cytoskeleton organization ocurr.
CC {ECO:0000269|PubMed:15728719}.
CC -!- SIMILARITY: Belongs to the VPS28 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00642, ECO:0000255|PROSITE-ProRule:PRU00645}.
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DR EMBL; AE013599; AAF59143.1; -; Genomic_DNA.
DR EMBL; AY060620; AAL28168.1; -; mRNA.
DR RefSeq; NP_001260796.1; NM_001273867.2.
DR RefSeq; NP_652053.1; NM_143796.4.
DR AlphaFoldDB; Q9V359; -.
DR SMR; Q9V359; -.
DR BioGRID; 70793; 9.
DR DIP; DIP-20897N; -.
DR IntAct; Q9V359; 27.
DR STRING; 7227.FBpp0302051; -.
DR PaxDb; Q9V359; -.
DR PRIDE; Q9V359; -.
DR DNASU; 47408; -.
DR EnsemblMetazoa; FBtr0088825; FBpp0087901; FBgn0021814.
DR EnsemblMetazoa; FBtr0310370; FBpp0302051; FBgn0021814.
DR GeneID; 47408; -.
DR KEGG; dme:Dmel_CG12770; -.
DR UCSC; CG12770-RA; d. melanogaster.
DR CTD; 51160; -.
DR FlyBase; FBgn0021814; Vps28.
DR VEuPathDB; VectorBase:FBgn0021814; -.
DR eggNOG; KOG3284; Eukaryota.
DR GeneTree; ENSGT00390000007486; -.
DR HOGENOM; CLU_076417_2_0_1; -.
DR InParanoid; Q9V359; -.
DR OMA; CDEFPTV; -.
DR OrthoDB; 1281819at2759; -.
DR PhylomeDB; Q9V359; -.
DR Reactome; R-DME-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR SignaLink; Q9V359; -.
DR BioGRID-ORCS; 47408; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Vps28; fly.
DR GenomeRNAi; 47408; -.
DR PRO; PR:Q9V359; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0021814; Expressed in testis and 23 other tissues.
DR ExpressionAtlas; Q9V359; baseline and differential.
DR Genevisible; Q9V359; DM.
DR GO; GO:0000813; C:ESCRT I complex; IDA:FlyBase.
DR GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR GO; GO:0097352; P:autophagosome maturation; IMP:FlyBase.
DR GO; GO:0006914; P:autophagy; IMP:FlyBase.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IMP:FlyBase.
DR GO; GO:0036257; P:multivesicular body organization; IMP:FlyBase.
DR GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
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:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:FlyBase.
DR Gene3D; 1.20.120.1130; -; 1.
DR Gene3D; 1.20.1440.200; -; 1.
DR InterPro; IPR037202; ESCRT_assembly_dom.
DR InterPro; IPR007143; Vps28.
DR InterPro; IPR017899; VPS28_C.
DR InterPro; IPR037206; VPS28_C_sf.
DR InterPro; IPR017898; VPS28_N.
DR InterPro; IPR038358; VPS28_N_sf.
DR PANTHER; PTHR12937; PTHR12937; 1.
DR Pfam; PF03997; VPS28; 1.
DR PIRSF; PIRSF017535; VPS28; 1.
DR SUPFAM; SSF140111; SSF140111; 1.
DR SUPFAM; SSF140427; SSF140427; 1.
DR PROSITE; PS51310; VPS28_C; 1.
DR PROSITE; PS51313; VPS28_N; 1.
PE 1: Evidence at protein level;
KW Endosome; Protein transport; Reference proteome; Transport.
FT CHAIN 1..210
FT /note="Vacuolar protein sorting-associated protein 28
FT homolog"
FT /id="PRO_0000120954"
FT DOMAIN 1..108
FT /note="VPS28 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00645"
FT DOMAIN 112..208
FT /note="VPS28 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00642"
SQ SEQUENCE 210 AA; 24512 MW; 843DB9820ADE9D96 CRC64;
MQEQSPELYE EVKLFRNARE REKYDNMADL YAIINTIQQL EKAYIRDCIT PQEYTAACSK
YLVQYKVAFK QVQCDEFPSV ETFVKKFRLD CPAALERIRE DRPITIRDDK GNTSKCIAEI
VSLFITIMDK LRLQINTMDA LQPDVKDLAD NMNRLSLIPE DFDAKLKVEK WLGSLNEMQA
SDELSEGQVR QFLFDLESAY ADFNKLLHSQ
