ID   PNRC2_RAT               Reviewed;         134 AA.
AC   Q66HE1;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Proline-rich nuclear receptor coactivator 2;
GN   Name=Pnrc2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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: Involved in nonsense-mediated mRNA decay (NMD) by acting as a
CC       bridge between the mRNA decapping complex and the NMD machinery. May
CC       act by targeting the NMD machinery to the P-body and recruiting the
CC       decapping machinery to aberrant mRNAs. Required for UPF1/RENT1
CC       localization to the P-body. Plays a role in glucocorticoid receptor-
CC       mediated mRNA degradation by interacting with the glucocorticoid
CC       receptor NR3C1 in a ligand-dependent manner when it is bound to the 5'
CC       UTR of target mRNAs and recruiting the RNA helicase UPF1 and the mRNA-
CC       decapping enzyme DCP1A, leading to RNA decay. Also acts as a nuclear
CC       receptor coactivator. May play a role in controlling the energy balance
CC       between energy storage and energy expenditure.
CC       {ECO:0000250|UniProtKB:Q9CR73, ECO:0000250|UniProtKB:Q9NPJ4}.
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   -!- DOMAIN: The interaction between PNRC2 and nuclear receptors is
CC       dependent on the SH3 binding motif. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PNRC family. PNRC2 subfamily. {ECO:0000305}.
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DR   EMBL; BC081903; AAH81903.1; -; mRNA.
DR   RefSeq; NP_001096830.1; NM_001103360.1.
DR   AlphaFoldDB; Q66HE1; -.
DR   STRING; 10116.ENSRNOP00000012258; -.
DR   PhosphoSitePlus; Q66HE1; -.
DR   PaxDb; Q66HE1; -.
DR   Ensembl; ENSRNOT00000012258; ENSRNOP00000012258; ENSRNOG00000070268.
DR   Ensembl; ENSRNOT00000104557; ENSRNOP00000084836; ENSRNOG00000070268.
DR   GeneID; 100125373; -.
DR   KEGG; rno:100125373; -.
DR   CTD; 55629; -.
DR   RGD; 1642418; Pnrc2.
DR   eggNOG; ENOG502RZZX; Eukaryota.
DR   GeneTree; ENSGT00530000063881; -.
DR   HOGENOM; CLU_086541_1_0_1; -.
DR   InParanoid; Q66HE1; -.
DR   OrthoDB; 1570409at2759; -.
DR   PhylomeDB; Q66HE1; -.
DR   Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   PRO; PR:Q66HE1; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000009248; Expressed in thymus and 20 other tissues.
DR   ExpressionAtlas; Q66HE1; baseline and differential.
DR   Genevisible; Q66HE1; RN.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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   InterPro; IPR026781; PNRC2.
DR   PANTHER; PTHR15405; PTHR15405; 1.
DR   PANTHER; PTHR15405:SF6; PTHR15405:SF6; 1.
PE   2: Evidence at transcript level;
KW   Activator; Cytoplasm; Nonsense-mediated mRNA decay; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..134
FT                   /note="Proline-rich nuclear receptor coactivator 2"
FT                   /id="PRO_0000058487"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           94..100
FT                   /note="SH3-binding"
FT   COMPBIAS        24..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   134 AA;  14881 MW;  F46E7E873299F5F9 CRC64;
     MGGGERYNIP DPQSRNASKN QQQHNRQKTK DQNSQMKIVH KKKERGHGYN PSAVQNGGKT
     KSLSNNSNWN ASLSSPSLLF KSQASQNYAG AKFSEPPSPS VLPKPPSHWV HVSLNPSDKE
     TMTFQLKTLL KVQV