NRF1_MOUSE
ID NRF1_MOUSE Reviewed; 503 AA.
AC Q9WU00; Q9CXE4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Nuclear respiratory factor 1;
DE Short=NRF-1;
DE AltName: Full=Alpha palindromic-binding protein;
DE Short=Alpha-pal;
GN Name=Nrf1;
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] (ISOFORMS LONG AND SHORT).
RX PubMed=10656923; DOI=10.1007/s003350010021;
RA Schaefer L., Engman H., Miller J.B.;
RT "Coding sequence, chromosomal localization, and expression pattern of Nrf1:
RT the mouse homolog of Drosophila erect wing.";
RL Mamm. Genome 11:104-110(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, and Skin;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor that activates the expression of the
CC EIF2S1 (EIF2-alpha) gene. Links the transcriptional modulation of key
CC metabolic genes to cellular growth and development. Implicated in the
CC control of nuclear genes required for respiration, heme biosynthesis,
CC and mitochondrial DNA transcription and replication (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Binds DNA as a dimer. Interacts with PPRC1 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9WU00; P56558: Ogt; Xeno; NbExp=2; IntAct=EBI-11291138, EBI-7614183;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q9WU00-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q9WU00-2; Sequence=VSP_003599;
CC -!- TISSUE SPECIFICITY: Widely expressed in embryonic, fetal, and adult
CC tissues.
CC -!- PTM: Phosphorylation enhances DNA binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NRF1/Ewg family. {ECO:0000305}.
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DR EMBL; AF098077; AAD21938.1; -; mRNA.
DR EMBL; AK014494; BAB29394.1; -; mRNA.
DR EMBL; AK029034; BAC26256.1; -; mRNA.
DR EMBL; CH466533; EDL13755.1; -; Genomic_DNA.
DR EMBL; CH466533; EDL13757.1; -; Genomic_DNA.
DR CCDS; CCDS19968.1; -. [Q9WU00-1]
DR RefSeq; NP_001157698.1; NM_001164226.1. [Q9WU00-1]
DR RefSeq; NP_035068.3; NM_010938.4. [Q9WU00-1]
DR RefSeq; XP_017176933.1; XM_017321444.1.
DR RefSeq; XP_017176934.1; XM_017321445.1.
DR AlphaFoldDB; Q9WU00; -.
DR BioGRID; 201845; 1.
DR DIP; DIP-61236N; -.
DR IntAct; Q9WU00; 2.
DR MINT; Q9WU00; -.
DR STRING; 10090.ENSMUSP00000110860; -.
DR iPTMnet; Q9WU00; -.
DR PhosphoSitePlus; Q9WU00; -.
DR EPD; Q9WU00; -.
DR jPOST; Q9WU00; -.
DR MaxQB; Q9WU00; -.
DR PaxDb; Q9WU00; -.
DR PeptideAtlas; Q9WU00; -.
DR PRIDE; Q9WU00; -.
DR ProteomicsDB; 293730; -. [Q9WU00-1]
DR ProteomicsDB; 293731; -. [Q9WU00-2]
DR Antibodypedia; 17908; 477 antibodies from 37 providers.
DR DNASU; 18181; -.
DR Ensembl; ENSMUST00000115209; ENSMUSP00000110864; ENSMUSG00000058440. [Q9WU00-1]
DR Ensembl; ENSMUST00000115211; ENSMUSP00000110866; ENSMUSG00000058440. [Q9WU00-1]
DR Ensembl; ENSMUST00000115212; ENSMUSP00000110867; ENSMUSG00000058440. [Q9WU00-1]
DR Ensembl; ENSMUST00000167972; ENSMUSP00000130108; ENSMUSG00000058440. [Q9WU00-1]
DR GeneID; 18181; -.
DR KEGG; mmu:18181; -.
DR UCSC; uc009bev.1; mouse. [Q9WU00-1]
DR CTD; 4899; -.
DR MGI; MGI:1332235; Nrf1.
DR VEuPathDB; HostDB:ENSMUSG00000058440; -.
DR eggNOG; KOG1491; Eukaryota.
DR GeneTree; ENSGT00390000006835; -.
DR HOGENOM; CLU_018156_3_1_1; -.
DR InParanoid; Q9WU00; -.
DR OMA; EVEPSWA; -.
DR OrthoDB; 858632at2759; -.
DR BioGRID-ORCS; 18181; 28 hits in 75 CRISPR screens.
DR ChiTaRS; Nrf1; mouse.
DR PRO; PR:Q9WU00; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9WU00; protein.
DR Bgee; ENSMUSG00000058440; Expressed in animal zygote and 232 other tissues.
DR ExpressionAtlas; Q9WU00; baseline and differential.
DR Genevisible; Q9WU00; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0005667; C:transcription regulator complex; TAS:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:AgBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:AgBase.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051602; P:response to electrical stimulus; ISO:MGI.
DR InterPro; IPR039142; NRF1/Ewg.
DR InterPro; IPR019526; Nrf1_activation-bd.
DR InterPro; IPR019525; Nrf1_NLS/DNA-bd_dimer.
DR PANTHER; PTHR20338; PTHR20338; 1.
DR Pfam; PF10492; Nrf1_activ_bdg; 1.
DR Pfam; PF10491; Nrf1_DNA-bind; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..503
FT /note="Nuclear respiratory factor 1"
FT /id="PRO_0000100209"
FT DNA_BIND 109..305
FT /evidence="ECO:0000250"
FT REGION 1..78
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT REGION 36..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..476
FT /note="Required for transcriptional activation"
FT /evidence="ECO:0000250"
FT MOTIF 88..116
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOD_RES 39
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q16656"
FT MOD_RES 44
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q16656"
FT MOD_RES 46
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q16656"
FT MOD_RES 47
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q16656"
FT MOD_RES 52
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q16656"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16656"
FT VAR_SEQ 256..321
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:10656923"
FT /id="VSP_003599"
FT CONFLICT 92
FT /note="K -> N (in Ref. 1; AAD21938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 53571 MW; 6C3D6B8C83C3B227 CRC64;
MEEHGVTQTE HMATIEAHAV AQQVQQVHVA TYTEHSMLSA DEDSPSSPED TSYDDSDILN
STAADEVTAH LAAAGPVGMA AAAAVATGKK RKRPHVFESN PSIRKRQQTR LLRKLRATLD
EYTTRVGQQA IVLCISPSKP NPVFKVFGAA PLENVVRKYK SMILEDLESA LAEHAPAPQE
VNSELPPLTI DGIPVSVDKM TQAQLRAFIP EMLKYSTGRG KPGWGKESCK PIWWPEDIPW
ANVRSDVRTE EQKQRVSWTQ ALRTIVKNCY KQHGREDLLY AFEDQQTQTQ ATTTHSIAHL
VPSQTVVQTF SNPDGTVSLI QVGTGATVAT LADASELPTT VTVAQVNYSA VADGEVEQNW
ATLQGGEMTI QTTQASEATQ AVASLAEAAV AASQEMQQGA TVTMALNSEA AAHAVATLAE
ATLQGGGQIV LSGETAAAVG ALTGVQDANG LVQIPVSMYQ TVVTSLAQGN GPVQVAMAPV
TTRISDSAVT MDGQAVEVVT LEQ
