NRBF2_MOUSE
ID NRBF2_MOUSE Reviewed; 287 AA.
AC Q8VCQ3; Q9DCG3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Nuclear receptor-binding factor 2;
DE Short=NRBF-2;
GN Name=Nrbf2;
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=Kidney;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND 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).
RN [4]
RP FUNCTION, INTERACTION WITH ATG14, AND SUBUNIT.
RX PubMed=24849286; DOI=10.1038/ncomms4920;
RA Lu J., He L., Behrends C., Araki M., Araki K., Jun Wang Q., Catanzaro J.M.,
RA Friedman S.L., Zong W.X., Fiel M.I., Li M., Yue Z.;
RT "NRBF2 regulates autophagy and prevents liver injury by modulating Atg14L-
RT linked phosphatidylinositol-3 kinase III activity.";
RL Nat. Commun. 5:3920-3920(2014).
RN [5]
RP STRUCTURE BY NMR OF 4-86.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of MIT domain from mouse Nrbf-2.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: May modulate transcriptional activation by target nuclear
CC receptors. Can act as transcriptional activator (in vitro) (By
CC similarity). {ECO:0000250|UniProtKB:Q96F24}.
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 (By similarity). Stabilzes PI3KC3-C1 assembly and enhances
CC ATG14-linked lipid kinase activity of PIK3C3 (PubMed:24849286).
CC Proposed to negatively regulate basal and starvation-induced autophagy
CC and to inhibit PIK3C3 activity by modulating interactions in PI3KC3-C1
CC (By similarity). May be involved in autophagosome biogenesis (By
CC similarity). May play a role in neural progenitor cell survival during
CC differentiation (PubMed:18619852). {ECO:0000250|UniProtKB:Q96F24,
CC ECO:0000269|PubMed:18619852, ECO:0000269|PubMed:24849286}.
CC -!- FUNCTION: Involved in the induction of starvation-induced autophagy.
CC Modulates ATG14-linked lipid kinase activity of PIK3C3 and stabilzes
CC PI3K complex I (PI3KC3-C1) assembly (PubMed:24849286). May play a role
CC in neural progenitor cell survival during differentiation
CC (PubMed:18619852). {ECO:0000250|UniProtKB:Q96F24,
CC ECO:0000269|PubMed:18619852, ECO:0000269|PubMed:24849286}.
CC -!- SUBUNIT: Interacts with RRARA, PPARD and PPARG. Interacts with THRB,
CC RARA, RARG and RXRA in the presence of bound ligand (By similarity).
CC Interacts with SCOC (By similarity). Associates with the PI3K complex I
CC (PI3KC3-C1); the direct binding partner in the complex is reported
CC variably as PIK3R4 or ATG14 (PubMed:24849286).
CC {ECO:0000250|UniProtKB:Q96F24, ECO:0000269|PubMed:24849286}.
CC -!- INTERACTION:
CC Q8VCQ3; Q8CDJ3: Atg14; NbExp=7; IntAct=EBI-2365563, EBI-3506699;
CC Q8VCQ3; O88597: Becn1; NbExp=5; IntAct=EBI-2365563, EBI-643716;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9QYK3}. Cytoplasm
CC {ECO:0000269|PubMed:18619852}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: During embryonic brain development detected in the
CC cerebral cortex at 14 dpc; expressed in the walls of the third and
CC fourth ventricles, and in the hippocampus. In the adult brain,
CC predominantly expressed in Purkinje cells of the cerebellum and neurons
CC in the CA3 region of the hippocampus (PubMed:18619852).
CC {ECO:0000269|PubMed:18619852}.
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DR EMBL; AK002810; BAB22375.1; -; mRNA.
DR EMBL; BC019448; AAH19448.1; -; mRNA.
DR CCDS; CCDS23902.1; -.
DR RefSeq; NP_001031370.1; NM_001036293.2.
DR PDB; 2CRB; NMR; -; A=4-87.
DR PDBsum; 2CRB; -.
DR AlphaFoldDB; Q8VCQ3; -.
DR SMR; Q8VCQ3; -.
DR BioGRID; 565935; 1.
DR IntAct; Q8VCQ3; 8.
DR STRING; 10090.ENSMUSP00000097254; -.
DR iPTMnet; Q8VCQ3; -.
DR PhosphoSitePlus; Q8VCQ3; -.
DR EPD; Q8VCQ3; -.
DR MaxQB; Q8VCQ3; -.
DR PaxDb; Q8VCQ3; -.
DR PeptideAtlas; Q8VCQ3; -.
DR PRIDE; Q8VCQ3; -.
DR ProteomicsDB; 293970; -.
DR Antibodypedia; 28311; 331 antibodies from 30 providers.
DR DNASU; 641340; -.
DR Ensembl; ENSMUST00000077839; ENSMUSP00000097254; ENSMUSG00000075000.
DR GeneID; 641340; -.
DR KEGG; mmu:641340; -.
DR UCSC; uc007flw.1; mouse.
DR CTD; 29982; -.
DR MGI; MGI:1354950; Nrbf2.
DR VEuPathDB; HostDB:ENSMUSG00000075000; -.
DR eggNOG; ENOG502SGH4; Eukaryota.
DR GeneTree; ENSGT00390000000984; -.
DR HOGENOM; CLU_098323_0_0_1; -.
DR InParanoid; Q8VCQ3; -.
DR OMA; CEAMKLT; -.
DR OrthoDB; 1613014at2759; -.
DR PhylomeDB; Q8VCQ3; -.
DR TreeFam; TF328627; -.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR BioGRID-ORCS; 641340; 11 hits in 72 CRISPR screens.
DR ChiTaRS; Nrbf2; mouse.
DR EvolutionaryTrace; Q8VCQ3; -.
DR PRO; PR:Q8VCQ3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8VCQ3; protein.
DR Bgee; ENSMUSG00000075000; Expressed in hindlimb stylopod muscle and 61 other tissues.
DR ExpressionAtlas; Q8VCQ3; baseline and differential.
DR Genevisible; Q8VCQ3; MM.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:MGI.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0006914; P:autophagy; IMP:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0043550; P:regulation of lipid kinase activity; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB.
DR IDEAL; IID50293; -.
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 3D-structure; Autophagy; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..287
FT /note="Nuclear receptor-binding factor 2"
FT /id="PRO_0000235817"
FT REGION 81..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..215
FT /evidence="ECO:0000255"
FT MOTIF 141..145
FT /note="Nuclear receptor interaction motif"
FT /evidence="ECO:0000250"
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"
FT CONFLICT 203
FT /note="K -> E (in Ref. 1; BAB22375)"
FT /evidence="ECO:0000305"
FT CONFLICT 245..264
FT /note="KFAANTGKAKDIPIPNLPPL -> SLQLTRGSQGHSNTQPSSS (in Ref.
FT 1; BAB22375)"
FT /evidence="ECO:0000305"
FT HELIX 7..23
FT /evidence="ECO:0007829|PDB:2CRB"
FT HELIX 27..45
FT /evidence="ECO:0007829|PDB:2CRB"
FT HELIX 51..85
FT /evidence="ECO:0007829|PDB:2CRB"
SQ SEQUENCE 287 AA; 32501 MW; 81B1C0A0CB575D2E CRC64;
MEVMEGPLNL AHQQSRRADR LLAAGKYEEA ISCHRKATTY LSEAMKLTES EQAHLSLELQ
RDSHMKQLLL IQERWKRAKR EERLKAQQST ERDGAPHLQA PPRPSEDAEG QSPLLSQPYI
PSTERRLPEV QGVFDRDPDT LLFLLQQKNE PSEPCIGSKA PKDDKTIIEE QATKIADLKR
HVEFLVAENE RLRKENKQLK AEKARLLKGT AEKELDVDAD FVEKSELWGL PSHSESAAAS
STWQKFAANT GKAKDIPIPN LPPLDFPSPE LPLMELSEDI LKGFMND
