VPS36_DROME
ID VPS36_DROME Reviewed; 399 AA.
AC Q9VU87; Q8MSB7;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Vacuolar protein-sorting-associated protein 36;
DE AltName: Full=ESCRT-II complex subunit VPS36;
GN Name=Vps36; ORFNames=CG10711;
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;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DOMAIN, 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 [6]
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).
RN [7]
RP FUNCTION.
RX PubMed=29307555; DOI=10.1016/j.cub.2017.11.064;
RA Anding A.L., Wang C., Chang T.K., Sliter D.A., Powers C.M., Hofmann K.,
RA Youle R.J., Baehrecke E.H.;
RT "Vps13D Encodes a Ubiquitin-Binding Protein that Is Required for the
RT Regulation of Mitochondrial Size and Clearance.";
RL Curr. Biol. 28:287-295(2018).
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
CC (PubMed:19132102). The MVB pathway mediates delivery of transmembrane
CC proteins into the lumen of the lysosome for degradation
CC (PubMed:19132102). The ESCRT-II complex is probably involved in the
CC recruitment of the ESCRT-III complex (By similarity). ESCRT-II
CC interacts, through the Vps36 subunit, with bicoid mRNA
CC (PubMed:17268469). This interaction is required for the anterior
CC localization of bicoid mRNA in the developing egg (PubMed:17268469).
CC Plays a role in promoting mitochondrial autophagy (mitophagy)
CC (PubMed:29307555). {ECO:0000250|UniProtKB:Q06696,
CC ECO:0000269|PubMed:17268469, ECO:0000269|PubMed:19132102,
CC ECO:0000269|PubMed:29307555}.
CC -!- SUBUNIT: Component of the endosomal sorting complex required for
CC transport II (ESCRT-II). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17268469}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in the ovary.
CC {ECO:0000269|PubMed:17268469}.
CC -!- DEVELOPMENTAL STAGE: Localizes to the anterior cortex of the oocyte in
CC the same region as bicoid mRNA from stage 10B/11 of oogenesis.
CC {ECO:0000269|PubMed:17268469}.
CC -!- DOMAIN: The GLUE domain (GRAM-like ubiquitin-binding in EAP45) mediates
CC the binding to the 3' UTR of bicoid mRNA.
CC {ECO:0000269|PubMed:17268469}.
CC -!- DISRUPTION PHENOTYPE: Multivesicular body sorting defects, with large
CC amounts of ubiquitinated proteins detected on endosomes
CC (PubMed:19132102). Bicoid mRNA is mislocalized in developing eggs
CC (PubMed:17268469). {ECO:0000269|PubMed:17268469,
CC ECO:0000269|PubMed:19132102}.
CC -!- SIMILARITY: Belongs to the VPS36 family. {ECO:0000305}.
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DR EMBL; AE014296; AAF49802.2; -; Genomic_DNA.
DR EMBL; AY118941; AAM50801.1; -; mRNA.
DR EMBL; BT044237; ACH92302.1; -; mRNA.
DR RefSeq; NP_648660.1; NM_140403.2.
DR AlphaFoldDB; Q9VU87; -.
DR SMR; Q9VU87; -.
DR BioGRID; 64866; 9.
DR STRING; 7227.FBpp0075560; -.
DR MoonProt; Q9VU87; -.
DR PaxDb; Q9VU87; -.
DR PRIDE; Q9VU87; -.
DR DNASU; 39523; -.
DR EnsemblMetazoa; FBtr0075818; FBpp0075560; FBgn0086785.
DR GeneID; 39523; -.
DR KEGG; dme:Dmel_CG10711; -.
DR UCSC; CG10711-RA; d. melanogaster.
DR CTD; 51028; -.
DR FlyBase; FBgn0086785; Vps36.
DR VEuPathDB; VectorBase:FBgn0086785; -.
DR eggNOG; KOG2760; Eukaryota.
DR GeneTree; ENSGT00390000017209; -.
DR HOGENOM; CLU_015433_0_0_1; -.
DR InParanoid; Q9VU87; -.
DR OMA; TLNARVW; -.
DR OrthoDB; 981902at2759; -.
DR PhylomeDB; Q9VU87; -.
DR Reactome; R-DME-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR BioGRID-ORCS; 39523; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 39523; -.
DR PRO; PR:Q9VU87; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0086785; Expressed in eye disc (Drosophila) and 22 other tissues.
DR Genevisible; Q9VU87; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0000814; C:ESCRT II complex; ISS:FlyBase.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:FlyBase.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; ISS:FlyBase.
DR GO; GO:0045450; P:bicoid mRNA localization; IMP:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:FlyBase.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR021648; GLUE_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR040608; Snf8/Vps36.
DR InterPro; IPR037855; Vps36.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13128; PTHR13128; 1.
DR Pfam; PF04157; EAP30; 1.
DR Pfam; PF11605; Vps36_ESCRT-II; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
DR PROSITE; PS51495; GLUE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; mRNA transport; Protein transport; Reference proteome;
KW RNA-binding; Transport.
FT CHAIN 1..399
FT /note="Vacuolar protein-sorting-associated protein 36"
FT /id="PRO_0000390363"
FT DOMAIN 1..94
FT /note="GLUE N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00828"
FT DOMAIN 111..144
FT /note="GLUE C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00828"
SQ SEQUENCE 399 AA; 44214 MW; 6E04D5E3B7E69CEE CRC64;
MNRFAYVEAR LSPNESFVSR DNRVKIYDGD QKTDFEDGEV VLTTHRLFWG RPGEIARAAV
TLCLPLSYVI SVSEETTASN FFGRKTRIIM HLHPPTSDKG PGPLDTSRAT HIKLSGKNGL
SVEFHSALRE TLNARVWEIL LTSEIIINGV ASSPTLEPAN DRLARIQKRT GIGGIERHLE
AKAKATDENI ALAFQDLSVL MAMAKDMVGV SKTISSKIRK QKGEISDDET VRFKSYLMSL
GIDDPVTRDN FTSNSAYFSS LARQICEMLL DPIEEQGGMM SLADVYCRVN RARGLELLSP
EDLLHACEQL SGPIRLRSFP SGARVLQLES HDDALIAVDT LEKVEAAESL AVEELAKQLG
ISLLLAKERL LVAERLGKVC RDESVEGLRF YPNLLLGRD
