ECO_DROME
ID ECO_DROME Reviewed; 1052 AA.
AC Q9VS50; A4V1K9; Q6AWN5; Q95RU6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=N-acetyltransferase eco;
DE EC=2.3.1.-;
DE AltName: Full=Establishment of cohesion 1 homolog;
DE Short=ECO1 homolog;
GN Name=eco; ORFNames=CG8598;
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., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 489-1052.
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14653991; DOI=10.1016/j.cub.2003.11.018;
RA Williams B.C., Garrett-Engele C.M., Li Z., Williams E.V., Rosenman E.D.,
RA Goldberg M.L.;
RT "Two putative acetyltransferases, san and deco, are required for
RT establishing sister chromatid cohesion in Drosophila.";
RL Curr. Biol. 13:2025-2036(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-177; SER-310;
RP SER-312 AND SER-314, AND 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: Acetyltransferase required for the establishment of sister
CC chromatid cohesion and couple the processes of cohesion and DNA
CC replication to ensure that only sister chromatids become paired
CC together. In contrast to the structural cohesins, the deposition and
CC establishment factors are required only during S phase.
CC {ECO:0000269|PubMed:14653991}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Flies display disrupt centromeric sister
CC chromatid cohesion very early in division. This failure of sister
CC chromatid cohesion does not require separase and is correlated with a
CC failure of the cohesin component Scc1 to accumulate in centromeric
CC regions. {ECO:0000269|PubMed:14653991}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28680.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014296; AAF50579.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12052.2; -; Genomic_DNA.
DR EMBL; BT015213; AAT94442.1; -; mRNA.
DR EMBL; AY061132; AAL28680.1; ALT_INIT; mRNA.
DR RefSeq; NP_648106.1; NM_139849.3.
DR RefSeq; NP_729236.2; NM_168201.2.
DR AlphaFoldDB; Q9VS50; -.
DR SMR; Q9VS50; -.
DR BioGRID; 64252; 12.
DR IntAct; Q9VS50; 6.
DR STRING; 7227.FBpp0076592; -.
DR iPTMnet; Q9VS50; -.
DR PaxDb; Q9VS50; -.
DR PRIDE; Q9VS50; -.
DR DNASU; 38812; -.
DR EnsemblMetazoa; FBtr0076882; FBpp0076592; FBgn0035766.
DR EnsemblMetazoa; FBtr0100278; FBpp0099670; FBgn0035766.
DR GeneID; 38812; -.
DR KEGG; dme:Dmel_CG8598; -.
DR CTD; 38812; -.
DR FlyBase; FBgn0035766; eco.
DR VEuPathDB; VectorBase:FBgn0035766; -.
DR eggNOG; KOG3014; Eukaryota.
DR GeneTree; ENSGT00940000156667; -.
DR HOGENOM; CLU_016671_0_0_1; -.
DR InParanoid; Q9VS50; -.
DR OMA; HKIRKRH; -.
DR OrthoDB; 241722at2759; -.
DR PhylomeDB; Q9VS50; -.
DR Reactome; R-DME-2468052; Establishment of Sister Chromatid Cohesion.
DR SignaLink; Q9VS50; -.
DR BioGRID-ORCS; 38812; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 38812; -.
DR PRO; PR:Q9VS50; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035766; Expressed in ovary and 17 other tissues.
DR ExpressionAtlas; Q9VS50; baseline and differential.
DR Genevisible; Q9VS50; DM.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016407; F:acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IMP:FlyBase.
DR GO; GO:0045132; P:meiotic chromosome segregation; IEA:InterPro.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:FlyBase.
DR InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR033257; Eco1/CTF7.
DR InterPro; IPR028009; ESCO_Acetyltransf_dom.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR45884:SF2; PTHR45884:SF2; 1.
DR Pfam; PF13880; Acetyltransf_13; 1.
DR Pfam; PF13878; zf-C2H2_3; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell cycle; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1052
FT /note="N-acetyltransferase eco"
FT /id="PRO_0000074544"
FT DOMAIN 906..1052
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT ZN_FING 852..876
FT /note="CCHH-type"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 264
FT /note="K -> E (in Ref. 3; AAT94442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1052 AA; 117414 MW; 5D4AE81BB3B12580 CRC64;
METPTGSGRP SRMATPRLSE RKRQLFGSPR SRLRQINDDE DDADVDSLGV LPLKTHVAAN
RKGRSLFAAV PGKSSSSANS SPETNKENKK TRGGVMTATA EQLPQLFTAT MRLNSNSSSN
SRNSSPRQTR VQRKRADSSM SSPTSSSEGT PSSRARNSIR RSPRTFSAQK DPDAFSSPES
FQTRLSKVAA MLMKGQDSRS MLEKSKKKHN HSLKTTAQVH TTKPKKTSPA EESQSDDEKP
SSSKNSRKNT EVRETRSSQI ISPKTRNRRR PFTSADINCK TLKAAAHLHE NMRSYDEEKT
AAVKLENSRS RSKSPVEVFK SNDDAVKRNT GNTNNKTAKS SEVATAKRPE SPGSSMKIDV
EVPESDEEAS NHKPQKRQHP ETSTPVAPSA DADSGSPQSK MRKVTLSSSI PTMAFYSHSG
EAVTKSRRRP SISKNSLKQP TKISPTSRPL LGINKGVHHK IRKRHGFANR LPATDMDNIL
NSLSNERLKN LITTKREERA KVEEVHQILR NAKDPIKMAK PLSVIEADDA NNNNNLPATA
WQETSADFSD LSDVEDIDPI IEVEPIIPII RHEPVQKSPT AEPADLSKRK FFKSGRRSST
CMEVRITDNI RASVSQGKIE LVQTIRRKPR QVRVKSATIF SAEQATVDAI LKNLDDTVVD
EIVEANPVVQ ATPIDAEETT METESLPDII EYAPEANDVE IDPFAEFRQR LPYQTDDPNV
VEQQQILLEF LISNNICTEK NFEIFIANPD DYKDEANQIV DNLYMVVNSE EAAQLAQMET
VENTAVAIAP KQDAPAVEEV QPKLFPIFTQ RLQPVVQKSL RRRPDTSMRL LTAAGGSNQY
QIDAGQKAFG ARQCQQCGLV YTVHEPEEEL LHREYHNSIH VLRFKGWIDE DIVSVYPEWA
SDGRIIRINE RAPTARLDRL RDLIGVVDKE LGYSSYIVPK IFVAFIAVRK QQIVGFCLVQ
PLSQAHRFIQ VDGTDYFSEE SYPASCGVSR IWVSPLQRRS GIASKLLRVV QCHTVLGQEI
ARECIAFSTP TDDGRALARQ FTGLDNFLTY DQ
