ECO1_YEAST
ID ECO1_YEAST Reviewed; 281 AA.
AC P43605; D6VTQ7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=N-acetyltransferase ECO1;
DE EC=2.3.1.-;
DE AltName: Full=Chromosome transmission fidelity protein 7;
DE AltName: Full=Establishment of cohesion protein 1;
GN Name=ECO1; Synonyms=CTF7; OrderedLocusNames=YFR027W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9990855; DOI=10.1101/gad.13.3.307;
RA Skibbens R.V., Corson L.B., Koshland D., Hieter P.;
RT "Ctf7p is essential for sister chromatid cohesion and links mitotic
RT chromosome structure to the DNA replication machinery.";
RL Genes Dev. 13:307-319(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=9990856; DOI=10.1101/gad.13.3.320;
RA Toth A., Ciosk R., Uhlmann F., Galova M., Schleiffer A., Nasmyth K.;
RT "Yeast cohesin complex requires a conserved protein, Eco1p(Ctf7), to
RT establish cohesion between sister chromatids during DNA replication.";
RL Genes Dev. 13:320-333(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8686381;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<177::aid-yea896>3.0.co;2-a;
RA Eki T., Naitou M., Hagiwara H., Abe M., Ozawa M., Sasanuma S., Sasanuma M.,
RA Tsuchiya Y., Shibata T., Watanabe K., Ono A., Yamazaki M., Tashiro H.,
RA Hanaoka F., Murakami Y.;
RT "Fifteen open reading frames in a 30.8 kb region of the right arm of
RT chromosome VI from Saccharomyces cerevisiae.";
RL Yeast 12:177-190(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP ACETYLATION AT LYS-223, ENZYME ACTIVITY, AND MUTAGENESIS OF GLY-211;
RP 222-ARG-LYS-223; GLY-225 AND ASP-232.
RX PubMed=11864574; DOI=10.1016/s0960-9822(02)00681-4;
RA Ivanov D., Schleiffer A., Eisenhaber F., Mechtler K., Haering C.H.,
RA Nasmyth K.;
RT "Eco1 is a novel acetyltransferase that can acetylate proteins involved in
RT cohesion.";
RL Curr. Biol. 12:323-328(2002).
RN [7]
RP FUNCTION, AND INTERACTION WITH CHL12; RFC1; RFC2; RFC3; RFC4; RFC5 AND
RP RAD24.
RX PubMed=12665596; DOI=10.1128/mcb.23.8.2999-3007.2003;
RA Kenna M.A., Skibbens R.V.;
RT "Mechanical link between cohesion establishment and DNA replication:
RT Ctf7p/Eco1p, a cohesion establishment factor, associates with three
RT different replication factor C complexes.";
RL Mol. Cell. Biol. 23:2999-3007(2003).
RN [8]
RP INTERACTION WITH CHL1.
RX PubMed=15020404; DOI=10.1534/genetics.166.1.33;
RA Skibbens R.V.;
RT "Chl1p, a DNA helicase-like protein in budding yeast, functions in sister-
RT chromatid cohesion.";
RL Genetics 166:33-42(2004).
RN [9]
RP INTERACTION WITH MPS3.
RX PubMed=15355977; DOI=10.1074/jbc.m404324200;
RA Antoniacci L.M., Kenna M.A., Uetz P., Fields S., Skibbens R.V.;
RT "The spindle pole body assembly component Mps3p/Nep98p functions in sister
RT chromatid cohesion.";
RL J. Biol. Chem. 279:49542-49550(2004).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF CYS-35 AND HIS-53.
RX PubMed=15668154; DOI=10.1016/j.cub.2004.12.052;
RA Brands A., Skibbens R.V.;
RT "Ctf7p/Eco1p exhibits acetyltransferase activity -- but does it matter?";
RL Curr. Biol. 15:R50-R51(2005).
RN [11]
RP CATALYTIC ACTIVITY, AUTOACETYLATION, AND INTERACTION WITH SMC3.
RX PubMed=18614053; DOI=10.1016/j.molcel.2008.06.006;
RA Zhang J., Shi X., Li Y., Kim B.J., Jia J., Huang Z., Yang T., Fu X.,
RA Jung S.Y., Wang Y., Zhang P., Kim S.T., Pan X., Qin J.;
RT "Acetylation of Smc3 by Eco1 is required for S phase sister chromatid
RT cohesion in both human and yeast.";
RL Mol. Cell 31:143-151(2008).
CC -!- FUNCTION: Required for establishment of sister chromatid cohesion
CC during S phase but not for its further maintenance during G2 or M
CC phases or for loading the cohesin complex onto DNA. Interacts with the
CC three known alternate replication factor C (RFC) complexes, suggesting
CC that these complexes have essential but redundant activity in cohesion
CC establishment. Acts by acetylating the cohesin complex component SMC3.
CC In vitro, possesses acetyltransferase activity where it can acetylate
CC itself and components of the cohesin complex (MCD1, IRR1 and PDS5), but
CC is unable to acetylate histones. {ECO:0000269|PubMed:12665596,
CC ECO:0000269|PubMed:15668154, ECO:0000269|PubMed:9990855,
CC ECO:0000269|PubMed:9990856}.
CC -!- SUBUNIT: Binds specifically to CHL12, RFC1, RFC2, RFC3, RFC4, RFC5 and
CC RAD24 when members of an RFC complex. Interacts with CHL1 and MPS3.
CC {ECO:0000269|PubMed:12665596, ECO:0000269|PubMed:15020404,
CC ECO:0000269|PubMed:15355977, ECO:0000269|PubMed:18614053}.
CC -!- INTERACTION:
CC P43605; P22516: CHL1; NbExp=2; IntAct=EBI-22988, EBI-4600;
CC P43605; P49956: CTF18; NbExp=2; IntAct=EBI-22988, EBI-4560;
CC P43605; P47069: MPS3; NbExp=5; IntAct=EBI-22988, EBI-25811;
CC P43605; P15873: POL30; NbExp=2; IntAct=EBI-22988, EBI-12993;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9990855,
CC ECO:0000269|PubMed:9990856}. Note=Associated with chromatin.
CC -!- PTM: Autoacetylates in vitro.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC {ECO:0000305}.
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DR EMBL; D50617; BAA09266.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12467.1; -; Genomic_DNA.
DR PIR; S56282; S56282.
DR RefSeq; NP_116683.1; NM_001179992.1.
DR AlphaFoldDB; P43605; -.
DR SMR; P43605; -.
DR BioGRID; 31181; 142.
DR DIP; DIP-5602N; -.
DR IntAct; P43605; 14.
DR STRING; 4932.YFR027W; -.
DR iPTMnet; P43605; -.
DR MaxQB; P43605; -.
DR PaxDb; P43605; -.
DR PRIDE; P43605; -.
DR EnsemblFungi; YFR027W_mRNA; YFR027W; YFR027W.
DR GeneID; 850584; -.
DR KEGG; sce:YFR027W; -.
DR SGD; S000001923; ECO1.
DR VEuPathDB; FungiDB:YFR027W; -.
DR eggNOG; KOG3014; Eukaryota.
DR GeneTree; ENSGT00940000175408; -.
DR HOGENOM; CLU_039183_2_1_1; -.
DR InParanoid; P43605; -.
DR OMA; RIWVCRT; -.
DR BioCyc; YEAST:G3O-30476-MON; -.
DR Reactome; R-SCE-2468052; Establishment of Sister Chromatid Cohesion.
DR PRO; PR:P43605; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43605; protein.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0043596; C:nuclear replication fork; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA: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:0140588; P:chromatin looping; IMP:SGD.
DR GO; GO:0051276; P:chromosome organization; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IDA:SGD.
DR GO; GO:0006260; P:DNA replication; IMP:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IDA:SGD.
DR GO; GO:0045132; P:meiotic chromosome segregation; IEA:InterPro.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:UniProtKB.
DR GO; GO:0032200; P:telomere organization; IMP:SGD.
DR GO; GO:0070058; P:tRNA gene clustering; IMP:SGD.
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 PANTHER; PTHR45884:SF2; PTHR45884:SF2; 1.
DR Pfam; PF13880; Acetyltransf_13; 1.
DR Pfam; PF13878; zf-C2H2_3; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Cell cycle; DNA replication; Metal-binding;
KW Nucleus; Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..281
FT /note="N-acetyltransferase ECO1"
FT /id="PRO_0000074550"
FT ZN_FING 33..57
FT /note="CCHH-type"
FT REGION 86..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 223
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:11864574"
FT MUTAGEN 35
FT /note="C->Y: In ctf7-109; loss of function."
FT /evidence="ECO:0000269|PubMed:15668154"
FT MUTAGEN 53
FT /note="H->Y: In ctf7-108; loss of function."
FT /evidence="ECO:0000269|PubMed:15668154"
FT MUTAGEN 211
FT /note="G->D: Abolishes acetyltransferase activity; but not
FT chromatid cohesion activity."
FT /evidence="ECO:0000269|PubMed:11864574"
FT MUTAGEN 222..223
FT /note="RK->GG: Abolishes acetyltransferase activity; but
FT not chromatid cohesion activity."
FT /evidence="ECO:0000269|PubMed:11864574"
FT MUTAGEN 225
FT /note="G->D: Abolishes acetyltransferase activity; but not
FT chromatid cohesion activity."
FT /evidence="ECO:0000269|PubMed:11864574"
FT MUTAGEN 232
FT /note="D->G: Abolishes acetyltransferase activity; but not
FT chromatid cohesion activity."
FT /evidence="ECO:0000269|PubMed:11864574"
SQ SEQUENCE 281 AA; 31845 MW; 0AF1B59BE9E71818 CRC64;
MKARKSQRKA GSKPNLIQSK LQVNNGSKSN KIVKCDKCEM SYSSTSIEDR AIHEKYHTLQ
LHGRKWSPNW GSIVYTERNH SRTVHLSRST GTITPLNSSP LKKSSPSITH QEEKIVYVRP
DKSNGEVRAM TEIMTLVNNE LNAPHDENVI WNSTTEEKGK AFVYIRNDRA VGIIIIENLY
GGNGKTSSRG RWMVYDSRRL VQNVYPDFKI GISRIWVCRT ARKLGIATKL IDVARENIVY
GEVIPRYQVA WSQPTDSGGK LASKYNGIMH KSGKLLLPVY I
