VPS72_DROME
ID VPS72_DROME Reviewed; 351 AA.
AC Q9VKM6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Vacuolar protein sorting-associated protein 72 homolog;
DE AltName: Full=Protein YL-1;
GN Name=YL-1; ORFNames=CG4621;
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 IDENTIFICATION IN THE TIP60 COMPLEX, AND FUNCTION.
RX PubMed=15528408; DOI=10.1126/science.1103455;
RA Kusch T., Florens L., Macdonald W.H., Swanson S.K., Glaser R.L.,
RA Yates J.R. III, Abmayr S.M., Washburn M.P., Workman J.L.;
RT "Acetylation by Tip60 is required for selective histone variant exchange at
RT DNA lesions.";
RL Science 306:2084-2087(2004).
RN [5]
RP FUNCTION, AND PROBABLE INTERACTION WITH HIS2AV.
RX PubMed=16299513; DOI=10.1038/nsmb1023;
RA Wu W.-H., Alami S., Luk E., Wu C.-H., Sen S., Mizuguchi G., Wei D., Wu C.;
RT "Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent
RT histone exchange.";
RL Nat. Struct. Mol. Biol. 12:1064-1071(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-59 AND SER-68, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Part of the Tip60 chromatin-remodeling complex which is
CC involved in DNA repair. Upon induction of DNA double-strand breaks,
CC this complex acetylates phosphorylated H2AV in nucleosomes and
CC exchanges it with unmodified H2AV. {ECO:0000269|PubMed:15528408,
CC ECO:0000269|PubMed:16299513}.
CC -!- SUBUNIT: Interacts with H2AV (Probable). Component of the Tip60
CC chromatin-remodeling complex which contains the catalytic subunit Tip60
CC and the subunits Domino, Tra1, Brd8, E(Pc), DMAP1, Pontin, Reptin,
CC Ing3, Act87E, BAP55, Mrg15, MrgBP, Gas41 and YL-1.
CC {ECO:0000269|PubMed:15528408, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VPS72/YL1 family. {ECO:0000305}.
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DR EMBL; AE014134; AAF53038.1; -; Genomic_DNA.
DR EMBL; AY122237; AAM52749.1; -; mRNA.
DR RefSeq; NP_001285823.1; NM_001298894.1.
DR RefSeq; NP_609475.1; NM_135631.4.
DR PDB; 5CHL; X-ray; 1.89 A; A=2-75.
DR PDBsum; 5CHL; -.
DR AlphaFoldDB; Q9VKM6; -.
DR SMR; Q9VKM6; -.
DR BioGRID; 60585; 20.
DR IntAct; Q9VKM6; 13.
DR STRING; 7227.FBpp0079735; -.
DR iPTMnet; Q9VKM6; -.
DR PaxDb; Q9VKM6; -.
DR DNASU; 34516; -.
DR EnsemblMetazoa; FBtr0080146; FBpp0079735; FBgn0032321.
DR EnsemblMetazoa; FBtr0340549; FBpp0309447; FBgn0032321.
DR GeneID; 34516; -.
DR KEGG; dme:Dmel_CG4621; -.
DR UCSC; CG4621-RA; d. melanogaster.
DR CTD; 34516; -.
DR FlyBase; FBgn0032321; YL-1.
DR VEuPathDB; VectorBase:FBgn0032321; -.
DR eggNOG; KOG2897; Eukaryota.
DR HOGENOM; CLU_040862_0_0_1; -.
DR InParanoid; Q9VKM6; -.
DR OMA; VNTKAYK; -.
DR OrthoDB; 1468037at2759; -.
DR PhylomeDB; Q9VKM6; -.
DR BioGRID-ORCS; 34516; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34516; -.
DR PRO; PR:Q9VKM6; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032321; Expressed in eye disc (Drosophila) and 25 other tissues.
DR ExpressionAtlas; Q9VKM6; baseline and differential.
DR Genevisible; Q9VKM6; DM.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IPI:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
DR GO; GO:0043486; P:histone exchange; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR008895; Vps72/YL1.
DR InterPro; IPR013272; Vps72/YL1_C.
DR PANTHER; PTHR13275; PTHR13275; 1.
DR Pfam; PF05764; YL1; 1.
DR Pfam; PF08265; YL1_C; 1.
DR SMART; SM00993; YL1_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Coiled coil; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..351
FT /note="Vacuolar protein sorting-associated protein 72
FT homolog"
FT /id="PRO_0000239006"
FT DNA_BIND 156..208
FT /evidence="ECO:0000255"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 142..202
FT /evidence="ECO:0000255"
FT COMPBIAS 17..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..69
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT TURN 9..14
FT /evidence="ECO:0007829|PDB:5CHL"
FT HELIX 15..30
FT /evidence="ECO:0007829|PDB:5CHL"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:5CHL"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:5CHL"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:5CHL"
SQ SEQUENCE 351 AA; 40442 MW; CB2D4B48CD09BDDE CRC64;
MAASRSRRNN AGNKIAHLLN EEEEDDFYKT SYGGFQEDEE DKEYEQKDEE EDVVDSDFSI
DENDEPVSDQ EEAPEKKRKR GVVNTKAYKE TKPAVKKETK ATPALHKKRP GGGVTKRRPR
PRFTVLDSGR KSIRTSTAIK TQATKIRLKE LDDARKRKKK KVRVEDYMPT QEELLEEAKI
TEEENTKSLE KFQKMELEKK KSRPTKRTFS GPTIRYHSLT MPAMRKPTRG ANPAVDSKDL
AGKCERTFVT IENDFNDKVF QSLFRHKAPP KASNGICPIT RLPARYFDPI TQQPYYSIQA
FKILREAYYM QLEQQGGGSE QPELAKWLEW RKLVKENRLK ASAAASKNGD N
