NDUF7_HUMAN
ID NDUF7_HUMAN Reviewed; 441 AA.
AC Q7L592; Q7Z399; Q9P1G3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein arginine methyltransferase NDUFAF7, mitochondrial {ECO:0000305};
DE EC=2.1.1.320 {ECO:0000269|PubMed:24089531};
DE AltName: Full=NADH dehydrogenase [ubiquinone] complex I, assembly factor 7;
DE AltName: Full=Protein midA homolog {ECO:0000303|PubMed:20406883};
DE Flags: Precursor;
GN Name=NDUFAF7 {ECO:0000312|HGNC:HGNC:28816};
GN Synonyms=C2orf56 {ECO:0000312|HGNC:HGNC:28816}; ORFNames=PRO1853;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Endometrial adenocarcinoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-441 (ISOFORM 1).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 121 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH NDUFS2.
RX PubMed=20406883; DOI=10.1242/jcs.066076;
RA Carilla-Latorre S., Gallardo M.E., Annesley S.J., Calvo-Garrido J.,
RA Grana O., Accari S.L., Smith P.K., Valencia A., Garesse R., Fisher P.R.,
RA Escalante R.;
RT "MidA is a putative methyltransferase that is required for mitochondrial
RT complex I function.";
RL J. Cell Sci. 123:1674-1683(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP NDUFS2.
RX PubMed=24089531; DOI=10.1074/jbc.m113.518803;
RA Rhein V.F., Carroll J., Ding S., Fearnley I.M., Walker J.E.;
RT "NDUFAF7 methylates arginine 85 in the NDUFS2 subunit of human complex I.";
RL J. Biol. Chem. 288:33016-33026(2013).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-124.
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).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP SUBCELLULAR LOCATION, INVOLVEMENT IN SUSCEPTIBILITY TO PATHOLOGIC MYOPIA,
RP VARIANT GLU-266, AND CHARACTERIZATION OF VARIANT GLU-266.
RX PubMed=28837730; DOI=10.1167/iovs.16-20941;
RA Wang B., Liu Y., Chen S., Wu Y., Lin S., Duan Y., Zheng K., Zhang L.,
RA Gu X., Hong W., Shao H., Zeng X., Sun B., Duan S.;
RT "A novel potentially causative variant of NDUFAF7 revealed by mutation
RT screening in a chinese family with pathologic myopia.";
RL Invest. Ophthalmol. Vis. Sci. 58:4182-4192(2017).
CC -!- FUNCTION: Arginine methyltransferase involved in the assembly or
CC stability of mitochondrial NADH:ubiquinone oxidoreductase complex
CC (complex I) (PubMed:20406883, PubMed:24089531, PubMed:24838397). Acts
CC by mediating symmetric dimethylation of 'Arg-118' of NDUFS2 after it
CC assembles into the complex I, stabilizing the early intermediate
CC complex (PubMed:24089531). {ECO:0000269|PubMed:20406883,
CC ECO:0000269|PubMed:24089531, ECO:0000269|PubMed:24838397}.
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:0000269|PubMed:24089531};
CC -!- SUBUNIT: Interacts with NDUFS2 (PubMed:20406883, PubMed:24089531).
CC {ECO:0000269|PubMed:24089531}.
CC -!- INTERACTION:
CC Q7L592; Q5S007: LRRK2; NbExp=2; IntAct=EBI-2555519, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20406883,
CC ECO:0000269|PubMed:24089531, ECO:0000269|PubMed:24838397,
CC ECO:0000269|PubMed:28837730}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7L592-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7L592-2; Sequence=VSP_030606, VSP_030607;
CC -!- DISEASE: Note=Defects in NDUFAF7 may be a cause of susceptibility to
CC pathologic myopia, a genetically heterogeneous disorder characterized
CC by extreme, familial, early-onset vision loss and described as myopia
CC accompanied by severe deformation of the eye besides excessive
CC elongation of the eye. {ECO:0000269|PubMed:28837730}.
CC -!- SIMILARITY: Belongs to the NDUFAF7 family. {ECO:0000305}.
CC -!- CAUTION: Stoichiometry of the protein is unclear. According to a
CC report, it forms a homodimer (PubMed:20406883). According to another
CC publication, it is mainly monomeric (PubMed:24838397).
CC {ECO:0000269|PubMed:20406883, ECO:0000269|PubMed:24838397}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF71091.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH12374.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX538031; CAD97976.1; -; mRNA.
DR EMBL; AC007390; AAY14816.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00402.1; -; Genomic_DNA.
DR EMBL; BC004548; AAH04548.2; -; mRNA.
DR EMBL; BC012374; AAH12374.2; ALT_INIT; mRNA.
DR EMBL; AF116671; AAF71091.1; ALT_INIT; mRNA.
DR CCDS; CCDS1788.1; -. [Q7L592-1]
DR CCDS; CCDS42673.1; -. [Q7L592-2]
DR RefSeq; NP_001077415.1; NM_001083946.1. [Q7L592-2]
DR RefSeq; NP_653337.1; NM_144736.4. [Q7L592-1]
DR AlphaFoldDB; Q7L592; -.
DR SMR; Q7L592; -.
DR BioGRID; 120676; 68.
DR IntAct; Q7L592; 32.
DR MINT; Q7L592; -.
DR STRING; 9606.ENSP00000002125; -.
DR iPTMnet; Q7L592; -.
DR PhosphoSitePlus; Q7L592; -.
DR BioMuta; NDUFAF7; -.
DR DMDM; 74749891; -.
DR EPD; Q7L592; -.
DR jPOST; Q7L592; -.
DR MassIVE; Q7L592; -.
DR MaxQB; Q7L592; -.
DR PaxDb; Q7L592; -.
DR PeptideAtlas; Q7L592; -.
DR PRIDE; Q7L592; -.
DR ProteomicsDB; 68801; -. [Q7L592-1]
DR ProteomicsDB; 68802; -. [Q7L592-2]
DR Antibodypedia; 52425; 127 antibodies from 16 providers.
DR DNASU; 55471; -.
DR Ensembl; ENST00000002125.9; ENSP00000002125.4; ENSG00000003509.16. [Q7L592-1]
DR Ensembl; ENST00000336237.10; ENSP00000337431.6; ENSG00000003509.16. [Q7L592-2]
DR GeneID; 55471; -.
DR KEGG; hsa:55471; -.
DR MANE-Select; ENST00000002125.9; ENSP00000002125.4; NM_144736.5; NP_653337.1.
DR UCSC; uc002rqa.6; human. [Q7L592-1]
DR CTD; 55471; -.
DR DisGeNET; 55471; -.
DR GeneCards; NDUFAF7; -.
DR HGNC; HGNC:28816; NDUFAF7.
DR HPA; ENSG00000003509; Tissue enhanced (testis).
DR MIM; 615898; gene.
DR neXtProt; NX_Q7L592; -.
DR OpenTargets; ENSG00000003509; -.
DR PharmGKB; PA162379266; -.
DR VEuPathDB; HostDB:ENSG00000003509; -.
DR eggNOG; KOG2901; Eukaryota.
DR GeneTree; ENSGT00390000001588; -.
DR InParanoid; Q7L592; -.
DR OMA; YYHPQRN; -.
DR OrthoDB; 491869at2759; -.
DR PhylomeDB; Q7L592; -.
DR TreeFam; TF314312; -.
DR PathwayCommons; Q7L592; -.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; Q7L592; -.
DR BioGRID-ORCS; 55471; 178 hits in 1078 CRISPR screens.
DR ChiTaRS; NDUFAF7; human.
DR GenomeRNAi; 55471; -.
DR Pharos; Q7L592; Tbio.
DR PRO; PR:Q7L592; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q7L592; protein.
DR Bgee; ENSG00000003509; Expressed in left testis and 177 other tissues.
DR ExpressionAtlas; Q7L592; baseline and differential.
DR Genevisible; Q7L592; HS.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; NAS:UniProtKB.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR GO; GO:0019918; P:peptidyl-arginine methylation, to symmetrical-dimethyl arginine; IMP: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..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..441
FT /note="Protein arginine methyltransferase NDUFAF7,
FT mitochondrial"
FT /id="PRO_0000315672"
FT VAR_SEQ 73..99
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_030606"
FT VAR_SEQ 157..227
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_030607"
FT VARIANT 39
FT /note="P -> A (in dbSNP:rs2714473)"
FT /id="VAR_038274"
FT VARIANT 266
FT /note="D -> E (probable disease-associated variant found in
FT patients with pathologic myopia; may decrease mitochondrial
FT complex I activity; decreases the production of ATP;
FT decreases reactive oxygen species production)"
FT /evidence="ECO:0000269|PubMed:28837730"
FT /id="VAR_079608"
FT MUTAGEN 124
FT /note="G->V: Loss of function."
FT /evidence="ECO:0000269|PubMed:24838397"
SQ SEQUENCE 441 AA; 49238 MW; 9F3D667CCE470623 CRC64;
MSVLLRSGLG PLCAVARAAI PFIWRGKYFS SGNEPAENPV TPMLRHLMYK IKSTGPITVA
EYMKEVLTNP AKGYYVYRDM LGEKGDFITS PEISQIFGEL LGIWFISEWM ATGKSTAFQL
VELGPGRGTL VGDILRVFTQ LGSVLKNCDI SVHLVEVSQK LSEIQALTLT KEKVPLERNA
GSPVYMKGVT KSGIPISWYR DLHDVPKGYS FYLAHEFFDV LPVHKFQKTP QGWREVFVDI
DPQVSDKLRF VLAPSATPAE AFIQHDETRD HVEVCPDAGV IIEELSQRIA LTGGAALVAD
YGHDGTKTDT FRGFCDHKLH DVLIAPGTAD LTADVDFSYL RRMAQGKVAS LGPIKQHTFL
KNMGIDVRLK VLLDKSNEPS VRQQLLQGYD MLMNPKKMGE RFNFFALLPH QRLQGGRYQR
NARQSKPFAS VVAGFSELAW Q
