ID   PNRC2_MOUSE             Reviewed;         140 AA.
AC   Q9CR73; B1AV48; B1AV49; Q9CXC6;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 136.
DE   RecName: Full=Proline-rich nuclear receptor coactivator 2;
GN   Name=Pnrc2;
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 MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Head, Lung, and Small intestine;
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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=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).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=16181749; DOI=10.1016/j.gene.2005.07.012;
RA   Zhou D., Masri S., Ye J.J., Chen S.;
RT   "Transcriptional regulation of the mouse PNRC2 promoter by the nuclear
RT   factor Y (NFY) and E2F1.";
RL   Gene 361:89-100(2005).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17971453; DOI=10.1074/jbc.m703234200;
RA   Zhou D., Shen R., Ye J.J., Li Y., Tsark W., Isbell D., Tso P., Chen S.;
RT   "Nuclear receptor coactivator PNRC2 regulates energy expenditure and
RT   adiposity.";
RL   J. Biol. Chem. 283:541-553(2008).
CC   -!- FUNCTION: Involved in nonsense-mediated mRNA decay (NMD) by acting as a
CC       bridge between the mRNA decapping complex and the NMD machinery (By
CC       similarity). May act by targeting the NMD machinery to the P-body and
CC       recruiting the decapping machinery to aberrant mRNAs (By similarity).
CC       Required for UPF1/RENT1 localization to the P-body (By similarity).
CC       Plays a role in glucocorticoid receptor-mediated mRNA degradation by
CC       interacting with the glucocorticoid receptor NR3C1 in a ligand-
CC       dependent manner when it is bound to the 5' UTR of target mRNAs and
CC       recruiting the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A,
CC       leading to RNA decay (By similarity). Also acts as a nuclear receptor
CC       coactivator. May play a role in controlling the energy balance between
CC       energy storage and energy expenditure (PubMed:17971453).
CC       {ECO:0000250|UniProtKB:Q9NPJ4, ECO:0000269|PubMed:17971453}.
CC   -!- SUBUNIT: Interacts with UPF1/RENT1; preferentially interacts with
CC       hyperphosphorylated form. Interacts with DCP1A. Interacts with many
CC       nuclear receptors including ESR1, ESRRA, ESRRG, NR3C1/GR, NR5A1, PGR,
CC       TR, RAR and RXR. {ECO:0000250|UniProtKB:Q9NPJ4}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, P-body
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Strong expression is detected in lung, spleen,
CC       ovary, thymus, and colon. {ECO:0000269|PubMed:16181749}.
CC   -!- DOMAIN: The interaction between PNRC2 and nuclear receptors is
CC       dependent on the SH3 binding motif. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice are lean, resistant to high fat diet-induced
CC       obesity but without the induction of insulin resistance and have a
CC       higher metabolic rate than wild-type mice.
CC       {ECO:0000269|PubMed:17971453}.
CC   -!- SIMILARITY: Belongs to the PNRC family. PNRC2 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM15897.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AK011192; BAB27457.1; -; mRNA.
DR   EMBL; AK012073; BAB28010.1; -; mRNA.
DR   EMBL; AK013163; BAB28686.1; -; mRNA.
DR   EMBL; AK018384; BAB31186.1; -; mRNA.
DR   EMBL; AK075816; BAC35983.1; -; mRNA.
DR   EMBL; AK077403; BAC36786.1; -; mRNA.
DR   EMBL; AL672076; CAM15896.1; -; Genomic_DNA.
DR   EMBL; AL672076; CAM15897.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH466552; EDL29966.1; -; Genomic_DNA.
DR   EMBL; BC006598; AAH06598.1; -; mRNA.
DR   CCDS; CCDS18792.1; -.
DR   RefSeq; NP_080659.1; NM_026383.3.
DR   RefSeq; XP_006539101.1; XM_006539038.1.
DR   RefSeq; XP_006539102.1; XM_006539039.1.
DR   AlphaFoldDB; Q9CR73; -.
DR   STRING; 10090.ENSMUSP00000030436; -.
DR   iPTMnet; Q9CR73; -.
DR   PhosphoSitePlus; Q9CR73; -.
DR   PaxDb; 10090-ENSMUSP00000030436; -.
DR   ProteomicsDB; 289467; -.
DR   Antibodypedia; 49958; 130 antibodies from 20 providers.
DR   DNASU; 52830; -.
DR   Ensembl; ENSMUST00000030436.12; ENSMUSP00000030436.6; ENSMUSG00000028675.13.
DR   GeneID; 52830; -.
DR   KEGG; mmu:52830; -.
DR   UCSC; uc008vhf.2; mouse.
DR   AGR; MGI:106512; -.
DR   CTD; 55629; -.
DR   MGI; MGI:106512; Pnrc2.
DR   VEuPathDB; HostDB:ENSMUSG00000028675; -.
DR   eggNOG; ENOG502RZZX; Eukaryota.
DR   GeneTree; ENSGT00530000063881; -.
DR   HOGENOM; CLU_086541_1_0_1; -.
DR   InParanoid; Q9CR73; -.
DR   OMA; RNTTKNH; -.
DR   OrthoDB; 5353336at2759; -.
DR   PhylomeDB; Q9CR73; -.
DR   Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   BioGRID-ORCS; 52830; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; Pnrc2; mouse.
DR   PRO; PR:Q9CR73; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q9CR73; Protein.
DR   Bgee; ENSMUSG00000028675; Expressed in optic fissure and 269 other cell types or tissues.
DR   ExpressionAtlas; Q9CR73; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
DR   InterPro; IPR026780; PNRC1/2.
DR   PANTHER; PTHR15405; PROLINE-RICH NUCLEAR RECEPTOR COACTIVATOR; 1.
DR   PANTHER; PTHR15405:SF6; PROLINE-RICH NUCLEAR RECEPTOR COACTIVATOR 2; 1.
DR   Pfam; PF15365; PNRC; 1.
DR   Genevisible; Q9CR73; MM.
PE   2: Evidence at transcript level;
KW   Activator; Cytoplasm; Nonsense-mediated mRNA decay; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..140
FT                   /note="Proline-rich nuclear receptor coactivator 2"
FT                   /id="PRO_0000058486"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           100..106
FT                   /note="SH3-binding"
FT   COMPBIAS        11..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        98
FT                   /note="K -> Q (in Ref. 1; BAB31186)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   140 AA;  15401 MW;  17321057158B36B3 CRC64;
     MGGGERYNIP DPQSRNASKN QEQQNRQKSK DQNSSQTKIA HKKKERGHGY NPAAAAWQAM
     QNGGKTKSLS NNSNWNAGLS SPSLLFKSQA SQNYAGAKFS EPPSPSVLPK PPSHWVHVSL
     NPSDKETMTF QLKTLLKVQV
//