NDUAD_MOUSE
ID NDUAD_MOUSE Reviewed; 144 AA.
AC Q9ERS2; Q9DC98; Q9DCA1;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13;
DE AltName: Full=Cell death regulatory protein GRIM-19;
DE AltName: Full=Complex I-B16.6;
DE Short=CI-B16.6;
DE AltName: Full=Gene associated with retinoic and interferon-induced mortality 19 protein;
DE Short=GRIM-19;
DE Short=Gene associated with retinoic and IFN-induced mortality 19 protein;
DE AltName: Full=NADH-ubiquinone oxidoreductase B16.6 subunit;
GN Name=Ndufa13; Synonyms=Grim19;
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].
RX PubMed=10924506; DOI=10.1074/jbc.m003929200;
RA Angell J.E., Lindner D.J., Shapiro P.S., Hofmann E.R., Kalvakolanu D.V.;
RT "Identification of GRIM-19, a novel cell death-regulatory gene induced by
RT the interferon-beta and retinoic acid combination, using a genetic
RT approach.";
RL J. Biol. Chem. 275:33416-33426(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
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 MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Colon, and Thymus;
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 PROTEIN SEQUENCE OF 6-22; 59-81; 89-99 AND 106-128, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH STAT3, AND SUBCELLULAR LOCATION.
RX PubMed=12628925; DOI=10.1093/emboj/cdg135;
RA Lufei C., Ma J., Huang G., Zhang T., Novotny-Diermayr V., Ong C.T., Cao X.;
RT "GRIM-19, a death-regulatory gene product, suppresses Stat3 activity via
RT functional interaction.";
RL EMBO J. 22:1325-1335(2003).
RN [6]
RP INTERACTION WITH STAT3.
RX PubMed=12867595; DOI=10.1073/pnas.1633516100;
RA Zhang J., Yang J., Roy S.K., Tininini S., Hu J., Bromberg J.F., Poli V.,
RA Stark G.R., Kalvakolanu D.V.;
RT "The cell death regulator GRIM-19 is an inhibitor of signal transducer and
RT activator of transcription 3.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9342-9347(2003).
RN [7]
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: Accessory subunit of the mitochondrial membrane respiratory
CC chain NADH dehydrogenase (Complex I), that is believed not to be
CC involved in catalysis. Complex I functions in the transfer of electrons
CC from NADH to the respiratory chain. The immediate electron acceptor for
CC the enzyme is believed to be ubiquinone. Involved in the
CC interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This
CC apoptotic activity is inhibited by interaction with viral IRF1.
CC Prevents the transactivation of STAT3 target genes. May play a role in
CC CARD15-mediated innate mucosal responses and serve to regulate
CC intestinal epithelial cell responses to microbes.
CC {ECO:0000250|UniProtKB:Q9P0J0}.
CC -!- SUBUNIT: Complex I is composed of 45 different subunits. Interacts with
CC CARD15, but not with CARD4. Interacts with STAT3, but not with STAT1,
CC STAT2 and STAT5A. Interacts with OLFM4. {ECO:0000250|UniProtKB:Q9P0J0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:12628925}; Single-pass membrane protein
CC {ECO:0000305|PubMed:12628925}; Matrix side
CC {ECO:0000305|PubMed:12628925}. Nucleus {ECO:0000269|PubMed:12628925}.
CC Note=Localizes mainly in the mitochondrion. May be translocated into
CC the nucleus upon IFN/RA treatment. {ECO:0000250|UniProtKB:Q9P0J0}.
CC -!- SIMILARITY: Belongs to the complex I NDUFA13 subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB22505.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF286698; AAG28168.1; -; mRNA.
DR EMBL; AK012422; BAB28227.1; -; mRNA.
DR EMBL; AK010517; BAB26999.1; -; mRNA.
DR EMBL; AK002999; BAB22505.1; ALT_INIT; mRNA.
DR EMBL; AK003012; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC034899; AAH34899.1; -; mRNA.
DR EMBL; BC037149; AAH37149.1; -; mRNA.
DR EMBL; BC055435; AAH55435.1; -; mRNA.
DR CCDS; CCDS22353.1; -.
DR RefSeq; NP_075801.1; NM_023312.2.
DR RefSeq; XP_017168432.1; XM_017312943.1.
DR PDB; 6G2J; EM; 3.30 A; Z=1-144.
DR PDB; 6G72; EM; 3.90 A; Z=1-144.
DR PDB; 6ZR2; EM; 3.10 A; Z=1-144.
DR PDB; 6ZTQ; EM; 3.00 A; Z=1-144.
DR PDB; 7AK5; EM; 3.17 A; Z=1-144.
DR PDB; 7AK6; EM; 3.82 A; Z=1-144.
DR PDB; 7B93; EM; 3.04 A; Z=1-144.
DR PDB; 7PSA; EM; 3.40 A; Z=1-144.
DR PDBsum; 6G2J; -.
DR PDBsum; 6G72; -.
DR PDBsum; 6ZR2; -.
DR PDBsum; 6ZTQ; -.
DR PDBsum; 7AK5; -.
DR PDBsum; 7AK6; -.
DR PDBsum; 7B93; -.
DR PDBsum; 7PSA; -.
DR AlphaFoldDB; Q9ERS2; -.
DR SMR; Q9ERS2; -.
DR BioGRID; 212001; 8.
DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR CORUM; Q9ERS2; -.
DR IntAct; Q9ERS2; 9.
DR MINT; Q9ERS2; -.
DR STRING; 10090.ENSMUSP00000105796; -.
DR iPTMnet; Q9ERS2; -.
DR PhosphoSitePlus; Q9ERS2; -.
DR EPD; Q9ERS2; -.
DR jPOST; Q9ERS2; -.
DR MaxQB; Q9ERS2; -.
DR PaxDb; Q9ERS2; -.
DR PeptideAtlas; Q9ERS2; -.
DR PRIDE; Q9ERS2; -.
DR ProteomicsDB; 293642; -.
DR Antibodypedia; 28492; 294 antibodies from 36 providers.
DR DNASU; 67184; -.
DR Ensembl; ENSMUST00000110167; ENSMUSP00000105796; ENSMUSG00000036199.
DR GeneID; 67184; -.
DR KEGG; mmu:67184; -.
DR UCSC; uc009lyd.1; mouse.
DR CTD; 51079; -.
DR MGI; MGI:1914434; Ndufa13.
DR VEuPathDB; HostDB:ENSMUSG00000036199; -.
DR eggNOG; KOG3300; Eukaryota.
DR GeneTree; ENSGT00390000000719; -.
DR HOGENOM; CLU_119720_0_0_1; -.
DR InParanoid; Q9ERS2; -.
DR OMA; GFRPAAY; -.
DR OrthoDB; 1030667at2759; -.
DR PhylomeDB; Q9ERS2; -.
DR TreeFam; TF315182; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 67184; 28 hits in 74 CRISPR screens.
DR ChiTaRS; Ndufa13; mouse.
DR PRO; PR:Q9ERS2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9ERS2; protein.
DR Bgee; ENSMUSG00000036199; Expressed in interventricular septum and 137 other tissues.
DR Genevisible; Q9ERS2; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005746; C:mitochondrial respirasome; ISS:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; TAS:MGI.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0035458; P:cellular response to interferon-beta; IEA:Ensembl.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR InterPro; IPR009346; GRIM-19.
DR PANTHER; PTHR12966; PTHR12966; 1.
DR Pfam; PF06212; GRIM-19; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Direct protein sequencing;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleus; Reference proteome; Respiratory chain; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q95KV7"
FT CHAIN 2..144
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 13"
FT /id="PRO_0000118805"
FT TRANSMEM 30..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q95KV7"
FT CONFLICT 4..6
FT /note="SKV -> TTI (in Ref. 2; BAB22505)"
FT /evidence="ECO:0000305"
FT CONFLICT 14..15
FT /note="GG -> EE (in Ref. 2; BAB22505)"
FT /evidence="ECO:0000305"
FT HELIX 33..97
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:7B93"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 121..125
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:6ZTQ"
SQ SEQUENCE 144 AA; 16860 MW; 8F69E9CF49384E37 CRC64;
MAASKVKQDM PPPGGYGPID YKRNLPRRGL SGYSMFAVGI GALIFGYWRM MRWNQERRRL
LIEDLEARIA LMPLFQAEKD RRTLQILREN LEEEAIIMKD VPNWKVGESV FHTTRWVPPL
IGEMYGLRTK EEMSNANFGF TWYT
