NRIP2_MOUSE
ID NRIP2_MOUSE Reviewed; 270 AA.
AC Q9JHR9; Q14BZ2; Q3U0V7; Q3UYH0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Nuclear receptor-interacting protein 2;
DE AltName: Full=Neuronal-interacting factor X 1;
GN Name=Nrip2; Synonyms=Nix1;
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 [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH NR1F2; RARA AND THRB, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10860982; DOI=10.1073/pnas.97.13.7160;
RA Greiner E.F., Kirfel J., Greschik H., Huang D., Becker P., Kapfhammer J.P.,
RA Schuele R.;
RT "Differential ligand-dependent protein-protein interactions between nuclear
RT receptors and a neuronal-specific cofactor.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:7160-7165(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Medulla oblongata, and Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Down-regulates transcriptional activation by nuclear
CC receptors, such as NR1F2. {ECO:0000269|PubMed:10860982}.
CC -!- SUBUNIT: Interacts with NR1F2, RARA and THRB in a ligand-dependent
CC manner. {ECO:0000269|PubMed:10860982}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10860982}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JHR9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JHR9-2; Sequence=VSP_022275;
CC -!- TISSUE SPECIFICITY: Expression is restricted to the central nervous
CC system (neurons in the dentate gyrus of the hippocampus, the amygdala,
CC thalamic and hypothalamic regions). {ECO:0000269|PubMed:10860982}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE22242.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ278170; CAB95737.1; -; mRNA.
DR EMBL; AK134689; BAE22242.1; ALT_FRAME; mRNA.
DR EMBL; AK156526; BAE33744.1; -; mRNA.
DR EMBL; BC115523; AAI15524.1; -; mRNA.
DR CCDS; CCDS20571.1; -. [Q9JHR9-2]
DR CCDS; CCDS51917.1; -. [Q9JHR9-1]
DR RefSeq; NP_001156330.1; NM_001162858.1. [Q9JHR9-1]
DR RefSeq; NP_068363.2; NM_021717.2. [Q9JHR9-2]
DR AlphaFoldDB; Q9JHR9; -.
DR SMR; Q9JHR9; -.
DR BioGRID; 208553; 4.
DR IntAct; Q9JHR9; 2.
DR STRING; 10090.ENSMUSP00000113317; -.
DR MEROPS; A28.002; -.
DR PhosphoSitePlus; Q9JHR9; -.
DR MaxQB; Q9JHR9; -.
DR PaxDb; Q9JHR9; -.
DR PRIDE; Q9JHR9; -.
DR ProteomicsDB; 252856; -. [Q9JHR9-1]
DR ProteomicsDB; 252857; -. [Q9JHR9-2]
DR DNASU; 60345; -.
DR Ensembl; ENSMUST00000001561; ENSMUSP00000001561; ENSMUSG00000001520. [Q9JHR9-2]
DR Ensembl; ENSMUST00000120405; ENSMUSP00000113317; ENSMUSG00000001520. [Q9JHR9-1]
DR GeneID; 60345; -.
DR KEGG; mmu:60345; -.
DR UCSC; uc009edn.2; mouse. [Q9JHR9-2]
DR UCSC; uc012etb.1; mouse. [Q9JHR9-1]
DR CTD; 83714; -.
DR MGI; MGI:1891884; Nrip2.
DR VEuPathDB; HostDB:ENSMUSG00000001520; -.
DR eggNOG; KOG0012; Eukaryota.
DR GeneTree; ENSGT00950000182999; -.
DR HOGENOM; CLU_087166_0_0_1; -.
DR InParanoid; Q9JHR9; -.
DR OMA; WKESCST; -.
DR OrthoDB; 1182441at2759; -.
DR PhylomeDB; Q9JHR9; -.
DR TreeFam; TF333421; -.
DR BioGRID-ORCS; 60345; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q9JHR9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9JHR9; protein.
DR Bgee; ENSMUSG00000001520; Expressed in hypothalamus and 73 other tissues.
DR ExpressionAtlas; Q9JHR9; baseline and differential.
DR Genevisible; Q9JHR9; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.70.10; -; 1.
DR InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR Pfam; PF09668; Asp_protease; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..270
FT /note="Nuclear receptor-interacting protein 2"
FT /id="PRO_0000271057"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..99
FT /note="Interaction with NR1F2"
FT /evidence="ECO:0000269|PubMed:10860982"
FT MOTIF 192..196
FT /note="LXXLL motif"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 200..270
FT /note="LATSLSASSLLPSALGIPTESICDSEALVPHSLLSLPKCTTKSLTEKDLQQM
FT GSRLHPGCRGQSYLLPPLA -> CCIDLDRGVLRLKAPFSELPFLPLYQEPGQ (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10860982,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_022275"
FT CONFLICT 32
FT /note="R -> L (in Ref. 2; BAE22242)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="Q -> R (in Ref. 2; BAE33744)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="L -> P (in Ref. 1; CAB95737)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="P -> T (in Ref. 2; BAE22242)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="P -> S (in Ref. 2; BAE33744)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="E -> Q (in Ref. 2; BAE22242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 29284 MW; EC001C2E290F5CCE CRC64;
MSTGQEARRD EGDSRKEQEA SLRDRAHLSQ QRQLKQATQF LHKDSADLLP LDSLKRLGTS
KDLQPHSVIQ RRLVEGNQRR LQGESPLLQA LIRGHDSSRT SATQVPALLV NCKCQDQMLR
VAVDTGTQHN QISAGCLRRL GLGKRVPKAP GGDVAPEPPT QVEQLELELG QETVACSAQV
VDVDSPEFCL GLQTLLSLKL ATSLSASSLL PSALGIPTES ICDSEALVPH SLLSLPKCTT
KSLTEKDLQQ MGSRLHPGCR GQSYLLPPLA
