NDUF5_MOUSE
ID NDUF5_MOUSE Reviewed; 343 AA.
AC A2APY7; Q9D7L6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Arginine-hydroxylase NDUFAF5, mitochondrial;
DE EC=1.-.-.- {ECO:0000250|UniProtKB:Q5TEU4};
DE AltName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 5 {ECO:0000312|MGI:MGI:1916737};
DE AltName: Full=Putative methyltransferase NDUFAF5 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=Ndufaf5 {ECO:0000312|MGI:MGI:1916737};
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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] OF 24-343 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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, Brown adipose tissue, and 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).
CC -!- FUNCTION: Arginine hydroxylase involved in the assembly of
CC mitochondrial NADH:ubiquinone oxidoreductase complex (complex I, MT-
CC ND1) at early stages. Acts by mediating hydroxylation of 'Arg-111' of
CC NDUFS7. May also have methyltransferase activity.
CC {ECO:0000250|UniProtKB:Q5TEU4}.
CC -!- SUBUNIT: Interacts with NDUFAF8, leading to stabilize NDUFAF5.
CC Interacts with NDUFS7. {ECO:0000250|UniProtKB:Q5TEU4}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q5TEU4}. Note=Peripherally localized on the
CC matrix face of the mitochondrial inner membrane.
CC {ECO:0000250|UniProtKB:Q5TEU4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2APY7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2APY7-2; Sequence=VSP_028638;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05630.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK009123; BAB26088.1; -; mRNA.
DR EMBL; AL844528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005630; AAH05630.1; ALT_INIT; mRNA.
DR CCDS; CCDS16804.2; -. [A2APY7-1]
DR RefSeq; NP_081369.2; NM_027093.4. [A2APY7-1]
DR AlphaFoldDB; A2APY7; -.
DR SMR; A2APY7; -.
DR STRING; 10090.ENSMUSP00000035325; -.
DR iPTMnet; A2APY7; -.
DR PhosphoSitePlus; A2APY7; -.
DR EPD; A2APY7; -.
DR MaxQB; A2APY7; -.
DR PaxDb; A2APY7; -.
DR PeptideAtlas; A2APY7; -.
DR PRIDE; A2APY7; -.
DR ProteomicsDB; 286168; -. [A2APY7-1]
DR ProteomicsDB; 286169; -. [A2APY7-2]
DR Antibodypedia; 24277; 127 antibodies from 21 providers.
DR DNASU; 69487; -.
DR Ensembl; ENSMUST00000044825; ENSMUSP00000035325; ENSMUSG00000027384. [A2APY7-1]
DR GeneID; 69487; -.
DR KEGG; mmu:69487; -.
DR UCSC; uc008mpo.2; mouse. [A2APY7-1]
DR UCSC; uc008mpp.2; mouse. [A2APY7-2]
DR CTD; 79133; -.
DR MGI; MGI:1916737; Ndufaf5.
DR VEuPathDB; HostDB:ENSMUSG00000027384; -.
DR eggNOG; KOG2940; Eukaryota.
DR GeneTree; ENSGT00390000014687; -.
DR HOGENOM; CLU_046586_0_2_1; -.
DR InParanoid; A2APY7; -.
DR OMA; PSMWELM; -.
DR OrthoDB; 691814at2759; -.
DR PhylomeDB; A2APY7; -.
DR TreeFam; TF315222; -.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 69487; 24 hits in 76 CRISPR screens.
DR PRO; PR:A2APY7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2APY7; protein.
DR Bgee; ENSMUSG00000027384; Expressed in hindlimb stylopod muscle and 250 other tissues.
DR Genevisible; A2APY7; MM.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR GO; GO:0030961; P:peptidyl-arginine hydroxylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Methyltransferase; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..343
FT /note="Arginine-hydroxylase NDUFAF5, mitochondrial"
FT /id="PRO_0000307214"
FT VAR_SEQ 1..187
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028638"
SQ SEQUENCE 343 AA; 38405 MW; 5B9766C0840643A0 CRC64;
MLRKVVLLRL CPLLGRPAVS ASSGSRREVA SGVPPSGSTS PRALNIFDRE LKRKQKNWAA
RQPDPMKFDY LKEEVGSRIA DRVYDIARDF PLALDIGCGR GYIAQHLDKE TVGKIFQTDI
AEHALKNSLE TDIPTVNILA DEEFLPFQEN TFDLVVSSLS LHWVNDLPRA LEQIHYVLKP
DGVFVGAMFG GDTLYELRCS LQLAETEREG GFSPHISPFT AVNDLGHLLG RAGFNTLTVD
TDEIQVNYPG MFELMEDLKG MGESNCSWNR KALLHRDTML AAAAVYREMY RNEDGSIPAT
FQIYHMIGWK YHDSQARPAE RGSATVSFGE LAKLNDVMSH EKK
