VP33A_DROME
ID VP33A_DROME Reviewed; 617 AA.
AC Q9Y1I2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Vacuolar protein sorting-associated protein 33A;
DE AltName: Full=Protein carnation;
GN Name=car; ORFNames=CG12230;
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|EMBL:AAL39643.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DOR, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=10549280; DOI=10.1016/s1097-2765(00)80199-9;
RA Sevrioukov E.A., He J.-P., Moghrabi N., Sunio A., Kraemer H.;
RT "A role for the deep orange and carnation eye color genes in lysosomal
RT delivery in Drosophila.";
RL Mol. Cell 4:479-486(1999).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [3]
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 [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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 [5]
RP INTERACTION WITH EMA.
RX PubMed=20194640; DOI=10.1083/jcb.200911126;
RA Kim S., Wairkar Y.P., Daniels R.W., DiAntonio A.;
RT "The novel endosomal membrane protein Ema interacts with the class C Vps-
RT HOPS complex to promote endosomal maturation.";
RL J. Cell Biol. 188:717-734(2010).
RN [6]
RP MUTAGENESIS OF LEU-26 AND GLY-249, AND FUNCTION.
RX PubMed=22160599; DOI=10.1091/mbc.e11-02-0154;
RA Gailite I., Egger-Adam D., Wodarz A.;
RT "The phosphoinositide-associated protein Rush hour regulates endosomal
RT trafficking in Drosophila.";
RL Mol. Biol. Cell 23:433-447(2012).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE CORVET COMPLEX, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=27253064; DOI=10.7554/elife.14226;
RA Lorincz P., Lakatos Z., Varga A., Maruzs T., Simon-Vecsei Z., Darula Z.,
RA Benko P., Csordas G., Lippai M., Ando I., Hegedus K., Medzihradszky K.F.,
RA Takats S., Juhasz G.;
RT "MiniCORVET is a Vps8-containing early endosomal tether in Drosophila.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Required for the biogenesis of eye pigment granules
CC (PubMed:10549280). Plays a role in vesicle-mediated protein trafficking
CC to lysosomal compartments and in membrane docking/fusion reactions of
CC late endosomes/lysosomes probably as part of the class C core
CC vacuole/endosome tethering (CORVET) complex (PubMed:10549280,
CC PubMed:22160599, PubMed:27253064). {ECO:0000269|PubMed:10549280,
CC ECO:0000269|PubMed:22160599, ECO:0000305|PubMed:27253064}.
CC -!- SUBUNIT: Component of the class C core vacuole/endosome tethering
CC (CORVET) complex composed of at least dor/Vps18, Vps16A, Vps8 and
CC car/Vps33A; unlike in other species, Vps11 is not part of the
CC Drosophila complex (PubMed:27253064). Interacts with dor
CC (PubMed:10549280). Interacts with ema (PubMed:20194640).
CC {ECO:0000269|PubMed:10549280, ECO:0000269|PubMed:20194640,
CC ECO:0000269|PubMed:27253064}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000305|PubMed:27253064}.
CC Late endosome membrane {ECO:0000269|PubMed:10549280}; Peripheral
CC membrane protein {ECO:0000269|PubMed:10549280}; Cytoplasmic side
CC {ECO:0000269|PubMed:10549280}. Lysosome membrane
CC {ECO:0000269|PubMed:10549280}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10549280}; Cytoplasmic side
CC {ECO:0000269|PubMed:10549280}. Note=Cytoplasmic, peripheral membrane
CC protein associated with late endosomes/lysosomes.
CC -!- DEVELOPMENTAL STAGE: Expressed in larva and adult (at protein level).
CC {ECO:0000269|PubMed:27253064}.
CC -!- DISRUPTION PHENOTYPE: Flies display impaired deposition of pigment
CC granules (PubMed:10549280). Member of the 'granule group' of eye color
CC genes as mutants affect deposition in pigment granules of two types of
CC pigments, the ommochromes and drosopterins (PubMed:10549280). RNAi-
CC mediated knockdown results in late endosome fragmentation
CC (PubMed:27253064). {ECO:0000269|PubMed:10549280,
CC ECO:0000269|PubMed:27253064}.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR EMBL; AF133260; AAD38513.1; -; mRNA.
DR EMBL; AE014298; AAF48972.1; -; Genomic_DNA.
DR EMBL; AY069498; AAL39643.1; -; mRNA.
DR RefSeq; NP_523410.1; NM_078686.5.
DR RefSeq; NP_728266.1; NM_167664.2.
DR AlphaFoldDB; Q9Y1I2; -.
DR SMR; Q9Y1I2; -.
DR BioGRID; 59247; 16.
DR IntAct; Q9Y1I2; 1.
DR STRING; 7227.FBpp0074496; -.
DR PaxDb; Q9Y1I2; -.
DR PRIDE; Q9Y1I2; -.
DR DNASU; 32947; -.
DR EnsemblMetazoa; FBtr0074727; FBpp0074496; FBgn0000257.
DR EnsemblMetazoa; FBtr0074728; FBpp0074497; FBgn0000257.
DR GeneID; 32947; -.
DR KEGG; dme:Dmel_CG12230; -.
DR CTD; 32947; -.
DR FlyBase; FBgn0000257; car.
DR VEuPathDB; VectorBase:FBgn0000257; -.
DR eggNOG; KOG1302; Eukaryota.
DR GeneTree; ENSGT00940000155165; -.
DR HOGENOM; CLU_016678_3_0_1; -.
DR InParanoid; Q9Y1I2; -.
DR OMA; FHIFFVP; -.
DR OrthoDB; 406738at2759; -.
DR PhylomeDB; Q9Y1I2; -.
DR SignaLink; Q9Y1I2; -.
DR BioGRID-ORCS; 32947; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32947; -.
DR PRO; PR:Q9Y1I2; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000257; Expressed in head capsule and 45 other tissues.
DR ExpressionAtlas; Q9Y1I2; baseline and differential.
DR Genevisible; Q9Y1I2; DM.
DR GO; GO:0033263; C:CORVET complex; ISS:FlyBase.
DR GO; GO:0005829; C:cytosol; TAS:FlyBase.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030897; C:HOPS complex; IDA:FlyBase.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; TAS:FlyBase.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; ISS:FlyBase.
DR GO; GO:0019905; F:syntaxin binding; IPI:FlyBase.
DR GO; GO:0097352; P:autophagosome maturation; IMP:FlyBase.
DR GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
DR GO; GO:0048072; P:compound eye pigmentation; IMP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0006897; P:endocytosis; IMP:FlyBase.
DR GO; GO:0016197; P:endosomal transport; ISS:FlyBase.
DR GO; GO:0007032; P:endosome organization; IMP:FlyBase.
DR GO; GO:0008333; P:endosome to lysosome transport; IMP:FlyBase.
DR GO; GO:0008057; P:eye pigment granule organization; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0046907; P:intracellular transport; TAS:FlyBase.
DR GO; GO:0007220; P:Notch receptor processing; IMP:FlyBase.
DR GO; GO:0006727; P:ommochrome biosynthetic process; IMP:FlyBase.
DR GO; GO:0006622; P:protein targeting to lysosome; IMP:UniProtKB.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IMP:FlyBase.
DR GO; GO:0035542; P:regulation of SNARE complex assembly; ISS:FlyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:FlyBase.
DR Gene3D; 1.25.40.850; -; 1.
DR Gene3D; 3.40.50.1910; -; 2.
DR Gene3D; 3.40.50.2060; -; 1.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR InterPro; IPR027121; VPS33.
DR InterPro; IPR043155; VPS33_dom3b.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR PANTHER; PTHR11679:SF1; PTHR11679:SF1; 1.
DR Pfam; PF00995; Sec1; 1.
DR PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 1: Evidence at protein level;
KW Endosome; Lysosome; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..617
FT /note="Vacuolar protein sorting-associated protein 33A"
FT /id="PRO_0000206308"
FT REGION 268..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 26
FT /note="L->V: In car-1; irregular clustering of early
FT endosomes; when associated with V-249."
FT /evidence="ECO:0000269|PubMed:22160599"
FT MUTAGEN 249
FT /note="G->V: In car-1; irregular clustering of early
FT endosomes; when associated with V-26."
FT /evidence="ECO:0000269|PubMed:22160599"
SQ SEQUENCE 617 AA; 68766 MW; 81B806965D7330FF CRC64;
MFPHLKGHGQ RVNLQLLQEA ACRELLQQLD RIEGSKVIVL DETMIGPLDL VTRPKLFADR
GIRLLALKPE LHLPREVANV VYVMRPRVAL MEQLAAHVKA GGRAAAGRQY HILFAPRRSC
LCVSQLEVSG VLGSFGNIEE LAWNYLPLDV DLVSMEMPNA FRDVSVDGDT SSLYQAAVGL
VQLQRLYGRI PKIYGKGEFA HRVWEHAKQL GRDERTLYNG DKGVVDQLIL LDRSIDLLSP
LATQLTYEGL IDEFYGIRQN KLTLPAENFP SDGALPGGGG SGPRVEESQS LLGDTEKKTI
LLHSGEQLYA ELRNKHFNEV TKLLARKARE IHVQMHATSQ DKSVQEIKSF VENLLPQLMA
QKKATSEHTA IAGLLHEQVN AVRFADDLAA EQEFMVCADI DKPSAYIEDL IACRVELNRV
LRLICMQCHA ASGFKEKLLN HYKRELVHVY GLEVLLTISN LEKSGLLHLQ TESRAYSVLR
KTLHLTVDDN VEIEPKDISY VHSFYAPLTA RIVEHSLKPL GWQTLKSQIN NLPGPTFEDF
QAQLVGIGGR HTVTTVSEGS LLNVPRVVLV CFVGGCTFAE IAALRFLAAQ EDNNVEFLIA
TTKVVNKHSF LDSLMSS
