ID   PNRC2_BOVIN             Reviewed;         139 AA.
AC   Q0VCW6;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Proline-rich nuclear receptor coactivator 2;
GN   Name=PNRC2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; BC119962; AAI19963.1; -; mRNA.
DR   RefSeq; NP_001070425.1; NM_001076957.1.
DR   AlphaFoldDB; Q0VCW6; -.
DR   STRING; 9913.ENSBTAP00000040573; -.
DR   PaxDb; Q0VCW6; -.
DR   PRIDE; Q0VCW6; -.
DR   Ensembl; ENSBTAT00000042971; ENSBTAP00000040573; ENSBTAG00000030435.
DR   GeneID; 767836; -.
DR   KEGG; bta:767836; -.
DR   CTD; 55629; -.
DR   VEuPathDB; HostDB:ENSBTAG00000030435; -.
DR   VGNC; VGNC:33099; PNRC2.
DR   eggNOG; ENOG502RZZX; Eukaryota.
DR   GeneTree; ENSGT00530000063881; -.
DR   HOGENOM; CLU_086541_1_0_1; -.
DR   InParanoid; Q0VCW6; -.
DR   OMA; KERGHGC; -.
DR   OrthoDB; 1570409at2759; -.
DR   TreeFam; TF333211; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000030435; Expressed in abdominal lymph node and 107 other tissues.
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..139
FT                   /note="Proline-rich nuclear receptor coactivator 2"
FT                   /id="PRO_0000350624"
FT   REGION          1..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           99..105
FT                   /note="SH3-binding"
FT   COMPBIAS        11..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   139 AA;  15656 MW;  1A3E68059DAFAA73 CRC64;
     MGGGERYNIP APQTRNVSKN QQQLSRQKTK DQNSQMKIVH KKKERGHTYN SSSAAWQAMQ
     NGGKNKNFPN NQNWNSSLSS PTLLFKSQTN QNYAGAKFSE PPSPSVLPKP PSHWVPVSFN
     PSDKEIMTFQ LKTLLKVQV