ID   IN80E_BOVIN             Reviewed;         244 AA.
AC   Q29RS4;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=INO80 complex subunit E;
DE   AltName: Full=Coiled-coil domain-containing protein 95;
GN   Name=INO80E; Synonyms=CCDC95;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Putative regulatory component of the chromatin remodeling
CC       INO80 complex which is involved in transcriptional regulation, DNA
CC       replication and probably DNA repair.
CC   -!- SUBUNIT: Component of the chromatin remodeling INO80 complex;
CC       specifically part of a complex module associated with the N-terminus of
CC       INO80.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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DR   EMBL; BC114048; AAI14049.1; -; mRNA.
DR   RefSeq; NP_001040009.1; NM_001046544.1.
DR   AlphaFoldDB; Q29RS4; -.
DR   STRING; 9913.ENSBTAP00000006625; -.
DR   PaxDb; Q29RS4; -.
DR   Ensembl; ENSBTAT00000006625; ENSBTAP00000006625; ENSBTAG00000005030.
DR   GeneID; 614852; -.
DR   KEGG; bta:614852; -.
DR   CTD; 283899; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005030; -.
DR   VGNC; VGNC:30207; INO80E.
DR   eggNOG; ENOG502RZ5F; Eukaryota.
DR   GeneTree; ENSGT00390000011918; -.
DR   InParanoid; Q29RS4; -.
DR   OMA; EMNGQTD; -.
DR   OrthoDB; 1299948at2759; -.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000005030; Expressed in spermatocyte and 106 other tissues.
DR   ExpressionAtlas; Q29RS4; baseline and differential.
DR   GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:Ensembl.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0045739; P:positive regulation of DNA repair; IEA:Ensembl.
DR   GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:Ensembl.
DR   GO; GO:0060382; P:regulation of DNA strand elongation; IEA:Ensembl.
DR   GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR   GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
DR   InterPro; IPR026678; INO80E.
DR   PANTHER; PTHR21812; PTHR21812; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; DNA damage; DNA recombination; DNA repair; Isopeptide bond;
KW   Nucleus; Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..244
FT                   /note="INO80 complex subunit E"
FT                   /id="PRO_0000234291"
FT   REGION          59..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          10..54
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        72..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..244
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        159
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBZ0"
FT   CROSSLNK        171
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBZ0"
SQ   SEQUENCE   244 AA;  26384 MW;  20E0868F68E03930 CRC64;
     MNGPADGEVD YKKKYRNLKR KLKFLIYEHE CFQEELRKAQ RKLLKVSRDK SFLLDRLLQY
     ENVDEDSSDS DATASSDNSE TEGTPKLSDT PAPKRKRSPP LGGAPSPSSL SLPPSTGFPL
     QASRAPSPYL SSLASPTYPP FPSDYLALQL PEPSPLRPKR EKRPRLPRKL KMAVGPPDCP
     VGGPLTFPGR GSGAGVGAAL APLPPPKMPP PTILSAVPRQ MFSDAGSGDD ALDGDDDLVI
     DIPE