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F120B_MOUSE
ID   F120B_MOUSE             Reviewed;         786 AA.
AC   Q6RI63; Q5DTU5; Q8BK59; Q8BVH5; Q8BWQ3; Q8C158; Q99LL4; Q9DAC3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Constitutive coactivator of peroxisome proliferator-activated receptor gamma;
DE            Short=Constitutive coactivator of PPAR-gamma;
DE            Short=Constitutive coactivator of PPARG;
DE   AltName: Full=Protein FAM120B;
GN   Name=Fam120b; Synonyms=Ccpg, Kiaa1838;
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 [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ESR1;
RP   PPARG AND RXRA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND INDUCTION.
RC   TISSUE=Lung;
RX   PubMed=17595322; DOI=10.1210/me.2006-0520;
RA   Li D., Kang Q., Wang D.-M.;
RT   "Constitutive coactivator of peroxisome proliferator-activated receptor
RT   (PPARgamma), a novel coactivator of PPARgamma that promotes adipogenesis.";
RL   Mol. Endocrinol. 21:2320-2333(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Liver, Olfactory bulb, Skin, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RA   Nagaraja R., Waeltz P., Brathwaite M.E.;
RT   "Genomic sequence analysis in the mouse T-complex region.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 255-786 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
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).
CC   -!- FUNCTION: Functions as a transactivator of PPARG and ESR1. Functions in
CC       adipogenesis through PPARG activation. {ECO:0000269|PubMed:17595322}.
CC   -!- SUBUNIT: Interacts with ESR1 and RXRA. Interacts with PPARG; in a
CC       ligand-independent manner. {ECO:0000269|PubMed:17595322}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17595322}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6RI63-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6RI63-2; Sequence=VSP_033417, VSP_033418;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level).
CC       {ECO:0000269|PubMed:17595322}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout the embryonic developmental
CC       stages from 5 dpc to 19 dpc (at protein level).
CC       {ECO:0000269|PubMed:17595322}.
CC   -!- INDUCTION: Up-regulated in differentiating adipocytes (at protein
CC       level). {ECO:0000269|PubMed:17595322}.
CC   -!- SIMILARITY: Belongs to the constitutive coactivator of PPAR-gamma
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH03200.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB24339.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAD90470.1; Type=Erroneous translation; Evidence={ECO:0000305};
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DR   EMBL; DQ873694; ABH09085.1; -; mRNA.
DR   EMBL; AK005957; BAB24339.1; ALT_INIT; mRNA.
DR   EMBL; AK028911; BAC26191.1; -; mRNA.
DR   EMBL; AK050319; BAC34186.1; -; mRNA.
DR   EMBL; AK076185; BAC36239.1; -; mRNA.
DR   EMBL; AK078215; BAC37177.1; -; mRNA.
DR   EMBL; AK132211; BAE21035.1; -; mRNA.
DR   EMBL; AK220425; BAD90470.1; ALT_SEQ; Transcribed_RNA.
DR   EMBL; AY497019; AAR30868.1; -; Genomic_DNA.
DR   EMBL; BC003200; AAH03200.1; ALT_INIT; mRNA.
DR   EMBL; BC085163; AAH85163.1; -; mRNA.
DR   CCDS; CCDS37453.1; -. [Q6RI63-1]
DR   RefSeq; NP_077165.2; NM_024203.3. [Q6RI63-1]
DR   RefSeq; XP_006524890.1; XM_006524827.3.
DR   AlphaFoldDB; Q6RI63; -.
DR   BioGRID; 212265; 2.
DR   STRING; 10090.ENSMUSP00000054420; -.
DR   iPTMnet; Q6RI63; -.
DR   PhosphoSitePlus; Q6RI63; -.
DR   EPD; Q6RI63; -.
DR   MaxQB; Q6RI63; -.
DR   PaxDb; Q6RI63; -.
DR   PeptideAtlas; Q6RI63; -.
DR   PRIDE; Q6RI63; -.
DR   ProteomicsDB; 275495; -. [Q6RI63-1]
DR   ProteomicsDB; 275496; -. [Q6RI63-2]
DR   Antibodypedia; 33580; 91 antibodies from 23 providers.
DR   Ensembl; ENSMUST00000055352; ENSMUSP00000054420; ENSMUSG00000014763. [Q6RI63-1]
DR   GeneID; 67544; -.
DR   KEGG; mmu:67544; -.
DR   UCSC; uc008aoj.2; mouse. [Q6RI63-1]
DR   CTD; 84498; -.
DR   MGI; MGI:1914794; Fam120b.
DR   VEuPathDB; HostDB:ENSMUSG00000014763; -.
DR   eggNOG; ENOG502QRMW; Eukaryota.
DR   GeneTree; ENSGT00530000063168; -.
DR   HOGENOM; CLU_007639_0_0_1; -.
DR   InParanoid; Q6RI63; -.
DR   OMA; TCPHVCT; -.
DR   OrthoDB; 203269at2759; -.
DR   PhylomeDB; Q6RI63; -.
DR   TreeFam; TF331093; -.
DR   BioGRID-ORCS; 67544; 5 hits in 71 CRISPR screens.
DR   ChiTaRS; Fam120b; mouse.
DR   PRO; PR:Q6RI63; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q6RI63; protein.
DR   Bgee; ENSMUSG00000014763; Expressed in substantia nigra and 242 other tissues.
DR   Genevisible; Q6RI63; MM.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0045444; P:fat cell differentiation; IMP:MGI.
DR   GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IPI:MGI.
DR   InterPro; IPR026784; Coact_PPARg.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   PANTHER; PTHR15976; PTHR15976; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Differentiation; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..786
FT                   /note="Constitutive coactivator of peroxisome proliferator-
FT                   activated receptor gamma"
FT                   /id="PRO_0000332991"
FT   REGION          1..561
FT                   /note="Mediates transactivation of PPARG"
FT   REGION          371..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        743..774
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         457..493
FT                   /note="VARMHHVHSESYLVYNILSSGEIECSNTLEDELDQAL -> ASDCASPTSVH
FT                   NVVIESVPTNGFDREKRTVGGCRRETS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT                   /id="VSP_033417"
FT   VAR_SEQ         494..786
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT                   /id="VSP_033418"
FT   CONFLICT        41
FT                   /note="I -> N (in Ref. 2; BAC36239)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        178
FT                   /note="E -> K (in Ref. 2; BAC34186)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        549
FT                   /note="V -> I (in Ref. 5; AAH03200)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   786 AA;  89313 MW;  A9B6EEFD99275D4C CRC64;
     MGVRGLQGFV GSTCPHICTI VNIHELAERH RNKYPGCTPT IVVDAMCCLR YWYTAESWVC
     GGQWREYYCA LRNFVAAFTS AGIKLIFFFD GMVEPGKRDE WVKRRLKNNR EISKIFHYIK
     SKRDQPGRNM FFIPSGLAIF TRFALKTLGQ ETFCSLQEAD YEVASYGLQH NCLGILGEDT
     DYLIYDTCPY FSIGDLCLES LQTIMLCREK LCESLGLRVA DLPLLACLLG NDITPESMFE
     SFRYKCLSSY ASVKENAGKK GNIILAVSDY ISKVLHLYQG EKKIEEMLPL GPNKALFYKG
     VTSYLLPGQK SPWLVQKPKG MITDKQQMVS LNPESKQEVP MCIDPEFKQE VPVCTNPESM
     QEVPMCMDPE PNQEASMCTD PESKQEVPMC TDSESKPEVS QYTNPESKQK LPSGIDTEFN
     LEALMCTHPE FKQEDVMDME PEIKQVTMVS ESEILKVARM HHVHSESYLV YNILSSGEIE
     CSNTLEDELD QALPSQAFIY RPVRQRVYAL LLGDWKDGAS TGPVVKEWFV YPGNSLKHPD
     LVRPLQMTVQ GGTPSLEVLW LSQEPAVQAQ RLDTLLACFN LSSSREELQA VESPLRALCC
     LLIYLFVQVD TLSLEDLHAF IAQALCLQGK STSQLMHLQL DYINSRAVQL GSLLVRGLTT
     LVLVNSACGF PWTTSEFMPW NVFDGKLFHQ KYLQSEKGYA VEVLLEQNRS WLTKFHNLKA
     VVCKACSKEN RRIVGRTHWD SPYTGRQGRQ GYSSYRTDST HGHSGQSWRN QGSGGRQHER
     NHWRRY
 
 
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