ESCO2_DANRE
ID ESCO2_DANRE Reviewed; 609 AA.
AC Q5SPR8; Q4V9K9; Q6DRF5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=N-acetyltransferase ESCO2;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q56NI9};
DE AltName: Full=Establishment of cohesion 1 homolog 2;
DE Short=ECO1 homolog 2;
GN Name=esco2; ORFNames=si:dkey-217m5.6, zgc:111795;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND FUNCTION.
RX PubMed=15256591; DOI=10.1073/pnas.0403929101;
RA Amsterdam A., Nissen R.M., Sun Z., Swindell E.C., Farrington S.,
RA Hopkins N.;
RT "Identification of 315 genes essential for early zebrafish development.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12792-12797(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acetyltransferase required for the establishment of sister
CC chromatid cohesion. Couples the processes of cohesion and DNA
CC replication to ensure that only sister chromatids become paired
CC together (By similarity). Essential for early development
CC (PubMed:15256591). {ECO:0000250|UniProtKB:Q56NI9,
CC ECO:0000269|PubMed:15256591}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC Evidence={ECO:0000250|UniProtKB:Q56NI9};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q56NI9}.
CC Chromosome {ECO:0000250|UniProtKB:Q56NI9}.
CC -!- DOMAIN: The N-terminal region seems to be responsible for association
CC with chromosomes, thus excluding any involvement of the Zn finger in
CC this process. {ECO:0000250|UniProtKB:Q56NI9}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC {ECO:0000305}.
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DR EMBL; AY648804; AAT68122.1; -; mRNA.
DR EMBL; AL845306; CAI20931.1; -; Genomic_DNA.
DR EMBL; BC096847; AAH96847.1; -; mRNA.
DR RefSeq; NP_001003872.1; NM_001003872.1.
DR AlphaFoldDB; Q5SPR8; -.
DR SMR; Q5SPR8; -.
DR STRING; 7955.ENSDARP00000002535; -.
DR PaxDb; Q5SPR8; -.
DR PRIDE; Q5SPR8; -.
DR Ensembl; ENSDART00000009164; ENSDARP00000002535; ENSDARG00000014685.
DR GeneID; 445395; -.
DR KEGG; dre:445395; -.
DR CTD; 157570; -.
DR ZFIN; ZDB-GENE-050913-156; esco2.
DR eggNOG; KOG3014; Eukaryota.
DR GeneTree; ENSGT00940000158598; -.
DR HOGENOM; CLU_031546_1_0_1; -.
DR InParanoid; Q5SPR8; -.
DR OMA; PTDWMDS; -.
DR OrthoDB; 1024179at2759; -.
DR PhylomeDB; Q5SPR8; -.
DR TreeFam; TF314027; -.
DR Reactome; R-DRE-2468052; Establishment of Sister Chromatid Cohesion.
DR PRO; PR:Q5SPR8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000014685; Expressed in testis and 36 other tissues.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; 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:1990523; P:bone regeneration; IMP:ZFIN.
DR GO; GO:0031101; P:fin regeneration; IMP:ZFIN.
DR GO; GO:0007507; P:heart development; IMP:ZFIN.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:ZFIN.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:ZFIN.
DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; IMP:ZFIN.
DR InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR InterPro; IPR028009; ESCO_Acetyltransf_dom.
DR Pfam; PF13880; Acetyltransf_13; 1.
DR Pfam; PF13878; zf-C2H2_3; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cell cycle; Chromosome; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..609
FT /note="N-acetyltransferase ESCO2"
FT /id="PRO_0000074541"
FT ZN_FING 392..416
FT /note="CCHH-type"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 34
FT /note="R -> Q (in Ref. 3; AAH96847)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="R -> Q (in Ref. 3; AAH96847)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="P -> L (in Ref. 3; AAH96847)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="K -> N (in Ref. 3; AAH96847)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="T -> K (in Ref. 3; AAH96847)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="S -> P (in Ref. 3; AAH96847)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="K -> N (in Ref. 3; AAH96847)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="A -> T (in Ref. 3; AAH96847)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="T -> A (in Ref. 3; AAH96847)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="L -> V (in Ref. 3; AAH96847)"
FT /evidence="ECO:0000305"
FT CONFLICT 256..258
FT /note="HDK -> RDI (in Ref. 3; AAH96847)"
FT /evidence="ECO:0000305"
FT CONFLICT 335..336
FT /note="RP -> IF (in Ref. 1; AAT68122)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="P -> H (in Ref. 3; AAH96847)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="A -> T (in Ref. 3; AAH96847)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="A -> P (in Ref. 3; AAH96847)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 609 AA; 68360 MW; AEF6C1122726D8B5 CRC64;
MLSRKRKHGS PDAESNPSKK QITSLRSSPR RTTRQKENIP ISLNSPQKIP STPKKTQRAF
LLESPPKRVS PRKAVLGAGT FYSKQKPLYL TPLERKVLKE AKSPPSVTNK EPSRPPLTAA
NQVVKPAKKV QKKPRASAPQ SNLKGYFTAK PKATKSSSDK QTDQVLKSTM APISFSSMKS
KGKPKLVVGA AFFNTGKKPT SMYKKSAQNT KPKPTYEKPS IRKPVREKEL VTAPGQRSPV
RRAVFLKKQP EVEVSHDKRE STQAPMSPQV LADVHGITKE LRVVLRRSVS PETGSQDAPS
EADSVFDVSD LLLPDHDSSH DEEESSVYPI FGTKRPQKKG KLSPPLNSST PSALTATPAL
KAKERSMLRR EMKKQTDNQL IIDAGQKQFG ATTCASCGML YSTDSPEDNF QHTQFHQRFL
DTIKFVGWKK ERVVAEFWDG KIILVLPDDP KYATRKAEDV RRIADSELGF QQITLSSPSS
AKTYLFINTD RMVVGCLVAE NIRQAYRVLE QQEKQKDMSK EDFMEHHRTW CCSTVPEKAL
CGVSRIWVFS LMRRKSVATR LLDTARNTFM YGSHLTKEEI AFSDPTPQGK LFATKYCQTP
TFLVYNFIS
