NRBF2_RAT
ID NRBF2_RAT Reviewed; 287 AA.
AC Q9QYK3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Nuclear receptor-binding factor 2;
DE Short=NRBF-2;
GN Name=Nrbf2;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH PPARA; THRB; RARA AND RXRA, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10786636; DOI=10.1016/s0167-4781(99)00244-4;
RA Yasumo H., Masuda N., Furusawa T., Tsukamoto T., Sadano H., Osumi T.;
RT "Nuclear receptor binding factor-2 (NRBF-2), a possible gene activator
RT protein interacting with nuclear hormone receptors.";
RL Biochim. Biophys. Acta 1490:189-197(2000).
RN [2]
RP DEVELOPMENTAL STAGE.
RX PubMed=18619852; DOI=10.1016/j.mcn.2008.05.013;
RA Larsson J., Forsberg M., Brannvall K., Zhang X.Q., Enarsson M., Hedborg F.,
RA Forsberg-Nilsson K.;
RT "Nuclear receptor binding protein 2 is induced during neural progenitor
RT differentiation and affects cell survival.";
RL Mol. Cell. Neurosci. 39:32-39(2008).
CC -!- FUNCTION: May modulate transcriptional activation by target nuclear
CC receptors. Can act as transcriptional activator (in vitro).
CC {ECO:0000269|PubMed:10786636}.
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 ECO:0000269|PubMed:10786636}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10786636}. Cytoplasm
CC {ECO:0000269|PubMed:10786636}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in spleen, lung, muscle, liver, kidney,
CC heart, testis and brain. {ECO:0000269|PubMed:10786636}.
CC -!- DEVELOPMENTAL STAGE: Expressed at E14.5 in cerebral cortex; expression
CC increases over time in cultured neural stem/progenitor cells.
CC {ECO:0000269|PubMed:18619852}.
CC -!- SIMILARITY: Belongs to the NRBF family. {ECO:0000305}.
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DR EMBL; AB024930; BAA88955.1; -; mRNA.
DR RefSeq; NP_071522.1; NM_022186.1.
DR AlphaFoldDB; Q9QYK3; -.
DR SMR; Q9QYK3; -.
DR BioGRID; 248641; 1.
DR STRING; 10116.ENSRNOP00000000794; -.
DR PhosphoSitePlus; Q9QYK3; -.
DR PaxDb; Q9QYK3; -.
DR PRIDE; Q9QYK3; -.
DR GeneID; 58839; -.
DR KEGG; rno:58839; -.
DR UCSC; RGD:61937; rat.
DR CTD; 29982; -.
DR RGD; 61937; Nrbf2.
DR eggNOG; ENOG502SGH4; Eukaryota.
DR InParanoid; Q9QYK3; -.
DR OrthoDB; 1613014at2759; -.
DR PhylomeDB; Q9QYK3; -.
DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR PRO; PR:Q9QYK3; -.
DR Proteomes; UP000002494; Unplaced.
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; ISO:RGD.
DR GO; GO:0016922; F:nuclear receptor binding; IDA:RGD.
DR GO; GO:0006914; P:autophagy; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0043550; P:regulation of lipid kinase activity; ISO:RGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD.
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 1: Evidence at protein level;
KW Autophagy; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..287
FT /note="Nuclear receptor-binding factor 2"
FT /id="PRO_0000235819"
FT REGION 81..114
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 81..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 112
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; 32558 MW; CD631F4C4327A532 CRC64;
MEVMEGPLNL AHQQSRRADR LLAAGKYEEA ISCHKKATAY LSEAMKLTQS EQAHLSLELQ
RDSHMKQLLL IQERWKRAKR EERLKAQQST DRDGVPHLQA SHRPSEDSEG QSPLLSQTYI
PSTEKRLPEE QGVFDRDPDT LLFLLQQKNE PSEPCIGSKA PKDDKTIIEE QATKIAELKR
HVEFLVAENE RLRKENKQLK AEKARLLKGP AEKELDVDAD FVEKSELWGL PPHSDTATAS
STWQKFAANT GKAKDIPIPN LPPLDFPSPE LPLMELSEDI LKGFMND
