ID   NRBF2_PONAB             Reviewed;         287 AA.
AC   Q5R4C9;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Nuclear receptor-binding factor 2;
DE            Short=NRBF-2;
GN   Name=NRBF2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May modulate transcriptional activation by target nuclear
CC       receptors. Can act as transcriptional activator (in vitro) (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: Involved in starvation-induced autophagy probably by its
CC       association with PI3K complex I (PI3KC3-C1). However, effects has been
CC       described variably. Involved in the induction of starvation-induced
CC       autophagy. Stabilzes PI3KC3-C1 assembly and enhances ATG14-linked lipid
CC       kinase activity of PIK3C3. Proposed to negatively regulate basal and
CC       starvation-induced autophagy and to inhibit PIK3C3 activity by
CC       modulating interactions in PI3KC3-C1. May be involved in autophagosome
CC       biogenesis. May play a role in neural progenitor cell survival during
CC       differentiation (By similarity). {ECO:0000250|UniProtKB:Q8VCQ3,
CC       ECO:0000250|UniProtKB:Q96F24}.
CC   -!- SUBUNIT: Interacts with PPARD and PPARG (By similarity). Interacts with
CC       SCOC (By similarity). Interacts with PPARA. Interacts with THRB, RARA,
CC       RARG and RXRA in the presence of bound ligand. Associates with the PI3K
CC       complex I (PI3KC3-C1); the direct binding partner in the complex is
CC       reported variably as PIK3R4 or ATG14 (By similarity).
CC       {ECO:0000250|UniProtKB:Q8VCQ3, ECO:0000250|UniProtKB:Q96F24}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9QYK3}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9QYK3}. Cytoplasmic vesicle, autophagosome
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the NRBF family. {ECO:0000305}.
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DR   EMBL; CR861322; CAH93387.1; -; mRNA.
DR   RefSeq; NP_001126988.1; NM_001133516.1.
DR   AlphaFoldDB; Q5R4C9; -.
DR   SMR; Q5R4C9; -.
DR   STRING; 9601.ENSPPYP00000002795; -.
DR   PRIDE; Q5R4C9; -.
DR   Ensembl; ENSPPYT00000002893; ENSPPYP00000002795; ENSPPYG00000002411.
DR   GeneID; 100174011; -.
DR   KEGG; pon:100174011; -.
DR   CTD; 29982; -.
DR   eggNOG; ENOG502QRE0; Eukaryota.
DR   GeneTree; ENSGT00390000000984; -.
DR   HOGENOM; CLU_098323_0_0_1; -.
DR   InParanoid; Q5R4C9; -.
DR   OMA; CEAMKLT; -.
DR   OrthoDB; 1613014at2759; -.
DR   TreeFam; TF328627; -.
DR   Proteomes; UP000001595; Chromosome 10.
DR   GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0035032; C:phosphatidylinositol 3-kinase complex, class III; IEA:Ensembl.
DR   GO; GO:0006914; P:autophagy; IEA:Ensembl.
DR   GO; GO:0043550; P:regulation of lipid kinase activity; IEA:Ensembl.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR   InterPro; IPR039679; NRBF2.
DR   InterPro; IPR015056; NRBF2_C.
DR   InterPro; IPR033393; NRBF2_MIT.
DR   PANTHER; PTHR14964; PTHR14964; 1.
DR   Pfam; PF08961; NRBF2; 1.
DR   Pfam; PF17169; NRBF2_MIT; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Cytoplasmic vesicle; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..287
FT                   /note="Nuclear receptor-binding factor 2"
FT                   /id="PRO_0000235818"
FT   REGION          99..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          168..209
FT                   /evidence="ECO:0000255"
FT   MOTIF           141..145
FT                   /note="Nuclear receptor interaction motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        105..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96F24"
FT   MOD_RES         268
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96F24"
SQ   SEQUENCE   287 AA;  32422 MW;  9178801A7C89EC16 CRC64;
     MEVMEGPLNL AHQQSRRADR LLAAGKYEEA ISCHKKAAAY LSEAMKLTQS EQAHLSLELQ
     RDSHMKQLLL IQERWKRAQR EERLKAQQNT DKDVAAHLQT SHKPSAEDAE GQSPLSQKYS
     PSTEKCLPEI QGIFDRDPDT LLYLLQQKSE PAEPCIGSKA PKDDKTIIEE QATKIADLKR
     HVEFLVAENE RLRKENKQLK AEKARLLKGP IEKELDVDAD FVETSELWSL PPHSETATAS
     STWQKFAANT GKAKDIPIPN LPPLDFPSPE LPLMELSEDI LKGFMNN