ID H0WAG7_CAVPO Unreviewed; 597 AA.
AC H0WAG7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Establishment of sister chromatid cohesion N-acetyltransferase 2 {ECO:0000313|Ensembl:ENSCPOP00000019979.2};
GN Name=ESCO2 {ECO:0000313|Ensembl:ENSCPOP00000019979.2};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000019979.2, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000019979.2}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000019979.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000636};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC {ECO:0000256|ARBA:ARBA00005816}.
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DR EMBL; AAKN02003310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0WAG7; -.
DR STRING; 10141.ENSCPOP00000019979; -.
DR Ensembl; ENSCPOT00000026955.2; ENSCPOP00000019979.2; ENSCPOG00000024189.2.
DR VEuPathDB; HostDB:ENSCPOG00000024189; -.
DR eggNOG; KOG3014; Eukaryota.
DR GeneTree; ENSGT00940000158598; -.
DR HOGENOM; CLU_031546_1_0_1; -.
DR InParanoid; H0WAG7; -.
DR OMA; HIQYHHR; -.
DR TreeFam; TF314027; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000024189; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR GO; GO:0010369; C:chromocenter; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0001741; C:XY body; IEA:Ensembl.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:Ensembl.
DR GO; GO:0006302; P:double-strand break repair; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0071168; P:protein localization to chromatin; IEA:Ensembl.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:Ensembl.
DR InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR InterPro; IPR028009; ESCO_Acetyltransf_dom.
DR PANTHER; PTHR45884; N-ACETYLTRANSFERASE ECO; 1.
DR PANTHER; PTHR45884:SF3; N-ACETYLTRANSFERASE ESCO2; 1.
DR Pfam; PF13880; Acetyltransf_13; 1.
DR Pfam; PF13878; zf-C2H2_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 375..414
FT /note="N-acetyltransferase ESCO zinc-finger"
FT /evidence="ECO:0000259|Pfam:PF13878"
FT DOMAIN 525..593
FT /note="N-acetyltransferase ESCO acetyl-transferase"
FT /evidence="ECO:0000259|Pfam:PF13880"
FT REGION 136..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 67681 MW; 23CE9BE7A68C64F4 CRC64;
KMASFTPKKR KQDSLDSDSL LDIRSKKLIL DIAEDLLPSS NKIHTCKSSE INEENVSCTQ
QSHFTSSPLR TTNKNRLPLA NQSSPFKSAV STVSFYNKPK WYLNPLERKL VRQSRPISLQ
TSNEGKSVPI VAPKMQGKPV CSKKRNKKLQ KSLTTKYQPN HKCIKSVLKN SKNSKKNEMT
YKPAMEKENT CYSTESNLNT PRVLSQKIKP QTTLQSGAAF FISRKKLKRL SLEDKPSVGL
NQKDKSKVIE DCDTKALEQV PKCLLLEKKL NIELSAKSKN EEKLIKDSSI AVVSSKECSL
NKTKDLPSDD SVGENKISPE PLVYPIFSAS SGNTKRSPSE EESSMEPTTY MNFSKQTNTQ
KTVNARDANK ETKDQLIIDA GQKYFGATMC KSCGMIYSAS NPEDEIQHIQ YHHRFLEGIK
YTSWKRERVV AEFWDGKILL VLPRDPSYAT RKVTDVQELV DYELGFQQVV PRCPEKAKTL
LFVSDDKRVV GFLTAEPIKQ AFRVLSEPTG SKECSRAWQC SNVPEPAVCG ISRIWVFKLK
RRKRIARRLV DTLRNCFMFG CFLSTNEIAF SDPTPDGKLF ATKYCNTPNF LVYNFNS
//
