ID   COPRS_BOVIN             Reviewed;         185 AA.
AC   A5PJD3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Coordinator of PRMT5 and differentiation stimulator;
DE   AltName: Full=Cooperator of PRMT5;
GN   Name=COPRS; Synonyms=COPR5;
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=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone-binding protein required for histone H4
CC       methyltransferase activity of PRMT5. Specifically required for histone
CC       H4 'Arg-3' methylation mediated by PRMT5, but not histone H3 'Arg-8'
CC       methylation, suggesting that it modulates the substrate specificity of
CC       PRMT5. Specifically interacts with the N-terminus of histone H4 but not
CC       with histone H3, suggesting that it acts by promoting the association
CC       between histone H4 and PRMT5. Involved in CCNE1 promoter repression (By
CC       similarity). Plays a role in muscle cell differentiation by modulating
CC       the recruitment of PRMT5 to the promoter of genes involved in the
CC       coordination between cell cycle exit and muscle differentiation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with PRMT5. Interacts with histone H4; specifically
CC       interacts with the N-terminus of histone H4 but not with histone H3.
CC       Interacts with CBFB. Found in a complex with PRMT5, RUNX1 and CBFB.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR   EMBL; BC142058; AAI42059.1; -; mRNA.
DR   RefSeq; NP_001092364.1; NM_001098894.2.
DR   RefSeq; XP_010814057.1; XM_010815755.2.
DR   AlphaFoldDB; A5PJD3; -.
DR   STRING; 9913.ENSBTAP00000002453; -.
DR   PaxDb; A5PJD3; -.
DR   PRIDE; A5PJD3; -.
DR   Ensembl; ENSBTAT00000074870; ENSBTAP00000060660; ENSBTAG00000049483.
DR   GeneID; 506999; -.
DR   KEGG; bta:506999; -.
DR   CTD; 55352; -.
DR   VEuPathDB; HostDB:ENSBTAG00000049483; -.
DR   VGNC; VGNC:27598; COPRS.
DR   eggNOG; ENOG502ST7I; Eukaryota.
DR   GeneTree; ENSGT00390000007384; -.
DR   HOGENOM; CLU_126074_0_0_1; -.
DR   InParanoid; A5PJD3; -.
DR   OMA; NDIPTHG; -.
DR   OrthoDB; 1312667at2759; -.
DR   TreeFam; TF338109; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000049483; Expressed in semen and 104 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0043985; P:histone H4-R3 methylation; ISS:UniProtKB.
DR   GO; GO:0007517; P:muscle organ development; ISS:UniProtKB.
DR   InterPro; IPR029289; COPR5.
DR   PANTHER; PTHR36461; PTHR36461; 1.
DR   Pfam; PF15340; COPR5; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chromatin regulator; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..185
FT                   /note="Coordinator of PRMT5 and differentiation stimulator"
FT                   /id="PRO_0000336076"
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..92
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQ92"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQ92"
SQ   SEQUENCE   185 AA;  19950 MW;  04D77EB1D63B3B24 CRC64;
     MDPPTAGAQS LGAAEQPRGL QLPSGREAPP SPGTAFAPAD HSSQEKATEN ATDRLANGAQ
     SIPHDSPAHG EGTHCEEEGF AEDDEDSDGE PSPWELSEGM SGCLPKEQAG DLFHEDWDLE
     LKADQGNPYD ADDIQGCLSQ EVRPWVCCAP QGDMIYDPSW HHPPPLIPHY SKMVFETGQF
     DDAED