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   24-JAN-2024, entry version 153.
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   GlyGen; Q91W39; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q91W39; -.
DR   PhosphoSitePlus; Q91W39; -.
DR   SwissPalm; Q91W39; -.
DR   EPD; Q91W39; -.
DR   jPOST; Q91W39; -.
DR   MaxQB; Q91W39; -.
DR   PaxDb; 10090-ENSMUSP00000046388; -.
DR   PeptideAtlas; Q91W39; -.
DR   ProteomicsDB; 287455; -.
DR   Pumba; Q91W39; -.
DR   Antibodypedia; 27960; 175 antibodies from 24 providers.
DR   DNASU; 228869; -.
DR   Ensembl; ENSMUST00000040381.15; ENSMUSP00000046388.9; ENSMUSG00000039804.16.
DR   GeneID; 228869; -.
DR   KEGG; mmu:228869; -.
DR   UCSC; uc008nwv.1; mouse.
DR   AGR; MGI:2385165; -.
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; PMEEGVR; -.
DR   OrthoDB; 3061812at2759; -.
DR   PhylomeDB; Q91W39; -.
DR   TreeFam; TF324704; -.
DR   BioGRID-ORCS; 228869; 4 hits in 78 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 232 other cell types or tissues.
DR   ExpressionAtlas; Q91W39; baseline and differential.
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; Anticodon-binding domain; 1.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   PANTHER; PTHR23295:SF3; NUCLEAR RECEPTOR COACTIVATOR 5; 1.
DR   PANTHER; PTHR23295; NUCLEAR RECEPTOR COACTIVATOR 5-RELATED; 1.
DR   SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR   Genevisible; Q91W39; MM.
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
//