NDUF7_MOUSE
ID NDUF7_MOUSE Reviewed; 436 AA.
AC Q9CWG8; E9QLM6; Q8C1X3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protein arginine methyltransferase NDUFAF7, mitochondrial {ECO:0000250|UniProtKB:Q7L592};
DE EC=2.1.1.320 {ECO:0000250|UniProtKB:Q7L592};
DE AltName: Full=NADH dehydrogenase [ubiquinone] complex I, assembly factor 7 {ECO:0000312|MGI:MGI:1920944};
DE AltName: Full=Protein midA homolog {ECO:0000250|UniProtKB:Q7L592};
DE Flags: Precursor;
GN Name=Ndufaf7 {ECO:0000312|MGI:MGI:1920944};
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] (ISOFORMS 1 AND 2).
RC STRAIN=C3H/HeJ, and C57BL/6J; TISSUE=Brain;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Kidney;
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=Heart;
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).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=24838397; DOI=10.1093/hmg/ddu239;
RA Zurita Rendon O., Silva Neiva L., Sasarman F., Shoubridge E.A.;
RT "The arginine methyltransferase NDUFAF7 is essential for complex I assembly
RT and early vertebrate embryogenesis.";
RL Hum. Mol. Genet. 23:5159-5170(2014).
CC -!- FUNCTION: Arginine methyltransferase involved in the assembly or
CC stability of mitochondrial NADH:ubiquinone oxidoreductase complex
CC (complex I). Acts by mediating symmetric dimethylation of 'Arg-118' of
CC NDUFS2 after it assembles into the complex I, stabilizing the early
CC intermediate complex. {ECO:0000250|UniProtKB:Q7L592}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320;
CC Evidence={ECO:0000250|UniProtKB:Q7L592};
CC -!- SUBUNIT: Interacts with NDUFS2. {ECO:0000250|UniProtKB:Q7L592}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q7L592}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CWG8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CWG8-2; Sequence=VSP_030608;
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality.
CC {ECO:0000269|PubMed:24838397}.
CC -!- SIMILARITY: Belongs to the NDUFAF7 family. {ECO:0000305}.
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DR EMBL; AK010752; BAB27158.2; -; mRNA.
DR EMBL; AK090097; BAC41089.1; -; mRNA.
DR EMBL; AC154274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC108350; AAI08351.1; -; mRNA.
DR CCDS; CCDS28982.1; -. [Q9CWG8-1]
DR RefSeq; NP_082887.2; NM_028611.3. [Q9CWG8-1]
DR AlphaFoldDB; Q9CWG8; -.
DR SMR; Q9CWG8; -.
DR STRING; 10090.ENSMUSP00000024887; -.
DR PhosphoSitePlus; Q9CWG8; -.
DR EPD; Q9CWG8; -.
DR MaxQB; Q9CWG8; -.
DR PaxDb; Q9CWG8; -.
DR PeptideAtlas; Q9CWG8; -.
DR PRIDE; Q9CWG8; -.
DR ProteomicsDB; 293645; -. [Q9CWG8-1]
DR ProteomicsDB; 293646; -. [Q9CWG8-2]
DR Antibodypedia; 52425; 127 antibodies from 16 providers.
DR DNASU; 73694; -.
DR Ensembl; ENSMUST00000024887; ENSMUSP00000024887; ENSMUSG00000024082. [Q9CWG8-1]
DR Ensembl; ENSMUST00000233068; ENSMUSP00000156412; ENSMUSG00000024082. [Q9CWG8-2]
DR GeneID; 73694; -.
DR KEGG; mmu:73694; -.
DR UCSC; uc008dpm.2; mouse. [Q9CWG8-2]
DR UCSC; uc008dpn.2; mouse. [Q9CWG8-1]
DR CTD; 55471; -.
DR MGI; MGI:1920944; Ndufaf7.
DR VEuPathDB; HostDB:ENSMUSG00000024082; -.
DR eggNOG; KOG2901; Eukaryota.
DR GeneTree; ENSGT00390000001588; -.
DR HOGENOM; CLU_024840_3_1_1; -.
DR InParanoid; Q9CWG8; -.
DR OMA; YYHPQRN; -.
DR OrthoDB; 491869at2759; -.
DR PhylomeDB; Q9CWG8; -.
DR TreeFam; TF314312; -.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 73694; 18 hits in 72 CRISPR screens.
DR ChiTaRS; Ndufaf7; mouse.
DR PRO; PR:Q9CWG8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9CWG8; protein.
DR Bgee; ENSMUSG00000024082; Expressed in right kidney and 255 other tissues.
DR ExpressionAtlas; Q9CWG8; baseline and differential.
DR Genevisible; Q9CWG8; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR GO; GO:0019918; P:peptidyl-arginine methylation, to symmetrical-dimethyl arginine; ISS:UniProtKB.
DR Gene3D; 3.40.50.12710; -; 1.
DR InterPro; IPR003788; NDUFAF7.
DR InterPro; IPR038375; NDUFAF7_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12049; PTHR12049; 1.
DR Pfam; PF02636; Methyltransf_28; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; Mitochondrion; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..436
FT /note="Protein arginine methyltransferase NDUFAF7,
FT mitochondrial"
FT /id="PRO_0000315673"
FT REGION 411..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 367..436
FT /note="LLDKAGEPSAKQQLLGGYDMLMNPQKMGERFHFFALLPHQRLHGGSQERNAC
FT QSKTPSSSVAGFDELVWQ -> VVYLSNTKPLNFGNYLN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_030608"
FT CONFLICT 2
FT /note="N -> T (in Ref. 1; BAB27158)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="E -> D (in Ref. 1; BAB27158)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="V -> I (in Ref. 1; BAC41089 and 3; AAI08351)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="R -> H (in Ref. 1; BAC41089 and 3; AAI08351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 48385 MW; 33945F146ED2902E CRC64;
MNALVRRCVA RAGLPCIWRG KCYSSGNEPA ESNQVTPMLR HLMYKIKSTG PITVAEYMKE
VLTNPAKGYY VHQDMLGEKG DFITSPEISQ IFGELLGVWF VSEWIASGKS PAFQLVELGP
GRGTLTADIL RVFSQLGSVL KTCAISIHLV EVSQKLSEIQ ALTLAEEKVP LERDAESLVY
MKGVTKSGIP VSWYRDLKDV PEGYSLYLAH EFFDVLPVHK FQKTPRGWRE VFVDVDPQAS
DKLRFVLAPC ATPAEAFIQR DERREHVEVC PDAGVIIQEL SQRIASTGGA ALIADYGHDG
TKTDTLRGFY GHQLHDVLIA PGTADLTADV DFSYLRRMAQ GKVASLGPVE QRTFLKNMGI
DVRLKVLLDK AGEPSAKQQL LGGYDMLMNP QKMGERFHFF ALLPHQRLHG GSQERNACQS
KTPSSSVAGF DELVWQ
