NCOA5_MOUSE
ID NCOA5_MOUSE Reviewed; 579 AA.
AC Q91W39; A2A5L2;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Nuclear receptor coactivator 5;
DE Short=NCoA-5;
DE AltName: Full=Coactivator independent of AF-2;
DE Short=CIA;
GN Name=Ncoa5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=11113208; DOI=10.1128/mcb.21.1.343-353.2001;
RA Sauve F., McBroom L.D.B., Gallant J., Moraitis A.N., Labrie F., Giguere V.;
RT "CIA, a novel estrogen receptor coactivator with a bifunctional nuclear
RT receptor interacting determinant.";
RL Mol. Cell. Biol. 21:343-353(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378 AND SER-381, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=24268775; DOI=10.1016/j.celrep.2013.10.035;
RA Boeser A., Drexler H.C., Reuter H., Schmitz H., Wu G., Schoeler H.R.,
RA Gentile L., Bartscherer K.;
RT "SILAC proteomics of planarians identifies Ncoa5 as a conserved component
RT of pluripotent stem cells.";
RL Cell Rep. 5:1142-1155(2013).
CC -!- FUNCTION: Nuclear receptor coregulator that can have both coactivator
CC and corepressor functions. Interacts with nuclear receptors for
CC steroids (ESR1 and ESR2) independently of the steroid binding domain
CC (AF-2) of the ESR receptors, and with the orphan nuclear receptor
CC NR1D2. Involved in the coactivation of nuclear steroid receptors (ER)
CC as well as the corepression of MYC in response to 17-beta-estradiol
CC (E2) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds HTATIP2/TIP30. Interacts with YLPM1. Forms a complex
CC with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and PPP1CA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24268775}.
CC -!- DEVELOPMENTAL STAGE: Expressed in both unfertilized and fertilized eggs
CC during preimplantation development (at protein level)
CC (PubMed:24268775). Detected in all blastmeres of morulae at 3 days
CC post-coitum (dpc) (at protein level) (PubMed:24268775). Localizes to
CC the pluripotent inner cell mass (ICM) of blastocysts at 4 dpc (at
CC protein level) (PubMed:24268775). Expressed in many fetal tissues
CC (PubMed:11113208). High expression in fetal heart and kidney
CC (PubMed:11113208). Weak expression in fetal liver (PubMed:11113208).
CC {ECO:0000269|PubMed:11113208, ECO:0000269|PubMed:24268775}.
CC -!- DOMAIN: Contains one Leu-Xaa-Xaa-Leu-Leu (LxxLL) motif that is
CC essential for the association with nuclear receptors. {ECO:0000250}.
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DR EMBL; AL591495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017152; AAH17152.1; -; mRNA.
DR CCDS; CCDS17068.1; -.
DR RefSeq; NP_659141.1; NM_144892.1.
DR AlphaFoldDB; Q91W39; -.
DR BMRB; Q91W39; -.
DR SMR; Q91W39; -.
DR BioGRID; 230788; 8.
DR IntAct; Q91W39; 6.
DR MINT; Q91W39; -.
DR STRING; 10090.ENSMUSP00000046388; -.
DR iPTMnet; Q91W39; -.
DR PhosphoSitePlus; Q91W39; -.
DR EPD; Q91W39; -.
DR jPOST; Q91W39; -.
DR MaxQB; Q91W39; -.
DR PaxDb; Q91W39; -.
DR PeptideAtlas; Q91W39; -.
DR PRIDE; Q91W39; -.
DR ProteomicsDB; 287455; -.
DR Antibodypedia; 27960; 148 antibodies from 24 providers.
DR DNASU; 228869; -.
DR Ensembl; ENSMUST00000040381; ENSMUSP00000046388; ENSMUSG00000039804.
DR GeneID; 228869; -.
DR KEGG; mmu:228869; -.
DR UCSC; uc008nwv.1; mouse.
DR CTD; 57727; -.
DR MGI; MGI:2385165; Ncoa5.
DR VEuPathDB; HostDB:ENSMUSG00000039804; -.
DR eggNOG; KOG0845; Eukaryota.
DR GeneTree; ENSGT00530000064134; -.
DR HOGENOM; CLU_030807_1_1_1; -.
DR InParanoid; Q91W39; -.
DR OMA; ERRNMNK; -.
DR OrthoDB; 994112at2759; -.
DR PhylomeDB; Q91W39; -.
DR TreeFam; TF324704; -.
DR BioGRID-ORCS; 228869; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Ncoa5; mouse.
DR PRO; PR:Q91W39; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91W39; protein.
DR Bgee; ENSMUSG00000039804; Expressed in embryonic brain and 229 other tissues.
DR ExpressionAtlas; Q91W39; baseline and differential.
DR Genevisible; Q91W39; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IMP:MGI.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:MGI.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR Gene3D; 3.40.50.800; -; 1.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
PE 1: Evidence at protein level;
KW Acetylation; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..579
FT /note="Nuclear receptor coactivator 5"
FT /id="PRO_0000094412"
FT REGION 1..158
FT /note="Transcription repression"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..579
FT /note="Transcription activation"
FT MOTIF 345..349
FT /note="LXXLL motif"
FT COMPBIAS 16..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD5"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD5"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD5"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD5"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD5"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD5"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD5"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD5"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD5"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD5"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD5"
FT MOD_RES 274
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD5"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 579 AA; 65319 MW; 145A34199FB02D33 CRC64;
MNTAPSRPSP TRRDPYSFGD SRDTRRDRSP IRGSPRREPR DGRNGRDARD SRDIRDPRDL
RDRRDSRDIR DHRDSRSVRE ARDLRDFRDF RDLRDSRDFR DHRDPVYDRY RDIRDSRDPL
YRREGSYDRY LRVDDYCRRK DDSYFDRYRD SFDGRGPPGP ESQSRAKERL KREERRREEL
YRRYFEEIQR RFDAERPVDC SVIVVNKQTK DYAESVGRKV RDLGMVVDLI FLNTEVSLSQ
ALEDVSRGGS PFAIVITQQH QIHRSCTVNI MFGTPQEHRN MPQADAMVLV ARNYERYKND
CREKEREEIA RQAAKMANDA ILQERDRGGP EEGGRGGHPP AIQSLINLLA DNRYLTAEET
DKIINYLRER KERLLRSSAD SLPGPISRQP LGAASGSSLK SQPSSQPLQS GQVLPSATPT
PAAPPTSQQE LQAKILSLFN SGAVAANSSS ASPSVATGSS QNQNFSTAAN SQPQQRPQAS
GNQPPNIVGQ AGSARNMGPR PGAPSQGLFG QPSSRLAPAS TMASQRPVSS TGINFDNPSV
QKALDTLIQS GPALSHLVSQ TAAQVGRPQA PMGSYQRHY
