NIF3L_MOUSE
ID NIF3L_MOUSE Reviewed; 376 AA.
AC Q9EQ80; Q6P1B7; Q9D098;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=NIF3-like protein 1 {ECO:0000305|PubMed:12951069};
GN Name=Nif3l1 {ECO:0000312|MGI:MGI:1929485};
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], AND TISSUE SPECIFICITY.
RX PubMed=11124544; DOI=10.1159/000056799;
RA Tascou S., Uedelhoven J., Dixkens C., Nayernia K., Engel W., Burfeind P.;
RT "Isolation and characterization of a novel human gene, NIF3L1, and its
RT mouse ortholog, Nif3l1, highly conserved from bacteria to mammals.";
RL Cytogenet. Cell Genet. 90:330-336(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Visual cortex;
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP INTERACTION WITH THOC7.
RX PubMed=12951069; DOI=10.1016/j.bbrc.2003.07.008;
RA Tascou S., Kang T.W., Trappe R., Engel W., Burfeind P.;
RT "Identification and characterization of NIF3L1 BP1, a novel cytoplasmic
RT interaction partner of the NIF3L1 protein.";
RL Biochem. Biophys. Res. Commun. 309:440-448(2003).
RN [6]
RP FUNCTION, INTERACTION WITH COPS2, REGION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12522100; DOI=10.1074/jbc.m209856200;
RA Akiyama H., Fujisawa N., Tashiro Y., Takanabe N., Sugiyama A., Tashiro F.;
RT "The role of transcriptional corepressor Nif3l1 in early stage of neural
RT differentiation via cooperation with Trip15/CSN2.";
RL J. Biol. Chem. 278:10752-10762(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254 AND SER-258, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: May function as a transcriptional corepressor through its
CC interaction with COPS2, negatively regulating the expression of genes
CC involved in neuronal differentiation. {ECO:0000269|PubMed:12522100}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with COPS2
CC (PubMed:12522100). Interacts with THOC7 (PubMed:12951069).
CC {ECO:0000250|UniProtKB:Q9GZT8, ECO:0000269|PubMed:12522100,
CC ECO:0000269|PubMed:12951069}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12522100}. Nucleus
CC {ECO:0000269|PubMed:12522100}. Note=Interaction with COPS2 may regulate
CC localization to the nucleus. {ECO:0000269|PubMed:12522100}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in all tissues tested with
CC higher expression in cerebellum, heart and kidney and to a lower level
CC in cerebrum, lung, liver, spleen and muscle.
CC {ECO:0000269|PubMed:11124544, ECO:0000269|PubMed:12522100}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing brain from 10.5 dpc
CC until 14.5 dpc. The expression decreases after 16.5 dpc, but an up-
CC regulation is observed at P5 and the expression remains constant
CC thereafter. {ECO:0000269|PubMed:12522100}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC {ECO:0000305}.
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DR EMBL; AF284439; AAG45961.1; -; mRNA.
DR EMBL; AK011670; BAB27769.1; -; mRNA.
DR EMBL; AK154815; BAE32848.1; -; mRNA.
DR EMBL; AK158616; BAE34583.1; -; mRNA.
DR EMBL; CH466548; EDL00082.1; -; Genomic_DNA.
DR EMBL; BC065163; AAH65163.1; -; mRNA.
DR CCDS; CCDS14973.1; -.
DR RefSeq; NP_075364.2; NM_022988.3.
DR RefSeq; XP_006496249.1; XM_006496186.1.
DR AlphaFoldDB; Q9EQ80; -.
DR SMR; Q9EQ80; -.
DR BioGRID; 211128; 13.
DR STRING; 10090.ENSMUSP00000084799; -.
DR iPTMnet; Q9EQ80; -.
DR PhosphoSitePlus; Q9EQ80; -.
DR SwissPalm; Q9EQ80; -.
DR EPD; Q9EQ80; -.
DR MaxQB; Q9EQ80; -.
DR PaxDb; Q9EQ80; -.
DR PeptideAtlas; Q9EQ80; -.
DR PRIDE; Q9EQ80; -.
DR ProteomicsDB; 293657; -.
DR Antibodypedia; 34126; 322 antibodies from 31 providers.
DR DNASU; 65102; -.
DR Ensembl; ENSMUST00000087521; ENSMUSP00000084799; ENSMUSG00000026036.
DR Ensembl; ENSMUST00000171597; ENSMUSP00000127501; ENSMUSG00000026036.
DR GeneID; 65102; -.
DR KEGG; mmu:65102; -.
DR UCSC; uc007bbz.1; mouse.
DR CTD; 60491; -.
DR MGI; MGI:1929485; Nif3l1.
DR VEuPathDB; HostDB:ENSMUSG00000026036; -.
DR eggNOG; KOG4131; Eukaryota.
DR GeneTree; ENSGT00390000003590; -.
DR HOGENOM; CLU_037423_0_0_1; -.
DR InParanoid; Q9EQ80; -.
DR OMA; EVAYDIY; -.
DR OrthoDB; 1293706at2759; -.
DR PhylomeDB; Q9EQ80; -.
DR TreeFam; TF324125; -.
DR BioGRID-ORCS; 65102; 1 hit in 58 CRISPR screens.
DR ChiTaRS; Nif3l1; mouse.
DR PRO; PR:Q9EQ80; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9EQ80; protein.
DR Bgee; ENSMUSG00000026036; Expressed in ear vesicle and 253 other tissues.
DR ExpressionAtlas; Q9EQ80; baseline and differential.
DR Genevisible; Q9EQ80; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:1903507; P:negative regulation of nucleic acid-templated transcription; IDA:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR InterPro; IPR002678; DUF34/NIF3.
DR InterPro; IPR017222; DUF34/NIF3_animal.
DR InterPro; IPR036069; DUF34/NIF3_sf.
DR PANTHER; PTHR13799; PTHR13799; 1.
DR Pfam; PF01784; NIF3; 1.
DR PIRSF; PIRSF037490; UCP037490_NIF3_euk; 1.
DR SUPFAM; SSF102705; SSF102705; 1.
DR TIGRFAMs; TIGR00486; YbgI_SA1388; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..376
FT /note="NIF3-like protein 1"
FT /id="PRO_0000147354"
FT REGION 243..376
FT /note="Mediates interaction with COPS2"
FT /evidence="ECO:0000269|PubMed:12522100"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZT8"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 7
FT /note="L -> I (in Ref. 1; AAG45961)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="G -> S (in Ref. 2; BAB27769)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="E -> K (in Ref. 2; BAB27769)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="L -> F (in Ref. 2; BAB27769)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="L -> Q (in Ref. 2; BAB27769)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="L -> F (in Ref. 2; BAB27769)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="T -> I (in Ref. 2; BAB27769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 41746 MW; 5B8693C5C621DC3D CRC64;
MLSSAHLVPT SVQRAQSWIC RSSRSFMDLK ALLSSLNDFA SLSFAESWDN VGLLVEPSPP
HTVNTLFLTN DLTEEVMDEA LQKKADFILS YHPPIFRPMK HITWKTWKEC LVIRALENRV
AVYSPHTAYD AAPQGVNSWL AKGLGTCTTR PIHPSRAPDY PTEGAHRLEF SVNRSQDLDK
VMSTLRGVGG VSVTSFPARC DGEEQTRISL NCTQKTLMQV LAFLSQDRQL YQKTEILSLE
KPLLLHTGMG RLCTLDESVS LAIMIERIKT HLKLSHLRLA LGVGRTLESQ VKVVALCAGS
GGSVLQGVEA DLYLTGEMSH HDVLDAASKG INVILCEHSN TERGFLSELQ EMLGVHFENK
INIILSETDR DPLRVV
