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NDUA7_MOUSE
ID   NDUA7_MOUSE             Reviewed;         113 AA.
AC   Q9Z1P6;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7;
DE   AltName: Full=Complex I-B14.5a;
DE            Short=CI-B14.5a;
DE   AltName: Full=NADH-ubiquinone oxidoreductase subunit B14.5a;
GN   Name=Ndufa7;
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 GENOMIC DNA].
RC   STRAIN=129;
RA   Rowen L., Qin S., Madan A., Loretz C., Hall J., James R., Dors M.,
RA   Shaffer T., Abbasi N., Ratcliffe A., Dickhoff R., Lasky S., Hood L.;
RT   "Sequence of the mouse major histocompatibility complex class II region.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=15112104; DOI=10.1007/s00335-003-2329-1;
RA   Abe K., Yuzuriha M., Sugimoto M., Ko M.S., Brathwaite M.E., Waeltz P.,
RA   Nagaraja R.;
RT   "Gene content of the 750-kb critical region for mouse embryonic ectoderm
RT   lethal tcl-w5.";
RL   Mamm. Genome 15:265-276(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Embryonic stem cell, and Kidney;
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   [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   PROTEIN SEQUENCE OF 13-23; 49-57 AND 62-74, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   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).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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.
CC       {ECO:0000250|UniProtKB:O95182}.
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits.
CC       {ECO:0000250|UniProtKB:O95182}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:O95182}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:O95182}; Matrix side
CC       {ECO:0000250|UniProtKB:O95182}.
CC   -!- SIMILARITY: Belongs to the complex I NDUFA7 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AF110520; AAC97968.1; -; Genomic_DNA.
DR   EMBL; AF528162; AAO17379.1; -; Genomic_DNA.
DR   EMBL; AK002476; BAB22129.1; -; mRNA.
DR   EMBL; AK003468; BAB22805.1; -; mRNA.
DR   EMBL; AK010299; BAB26832.1; -; mRNA.
DR   EMBL; BC052817; AAH52817.1; -; mRNA.
DR   EMBL; BC055698; AAH55698.1; -; mRNA.
DR   CCDS; CCDS28631.1; -.
DR   RefSeq; NP_075691.1; NM_023202.4.
DR   PDB; 6G2J; EM; 3.30 A; r=1-113.
DR   PDB; 6G72; EM; 3.90 A; r=1-113.
DR   PDB; 6ZR2; EM; 3.10 A; r=1-113.
DR   PDB; 6ZTQ; EM; 3.00 A; r=1-113.
DR   PDB; 7AK5; EM; 3.17 A; r=2-113.
DR   PDB; 7AK6; EM; 3.82 A; r=2-113.
DR   PDB; 7B93; EM; 3.04 A; r=1-113.
DR   PDB; 7PSA; EM; 3.40 A; r=1-113.
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; Q9Z1P6; -.
DR   SMR; Q9Z1P6; -.
DR   BioGRID; 211459; 54.
DR   ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR   CORUM; Q9Z1P6; -.
DR   IntAct; Q9Z1P6; 2.
DR   STRING; 10090.ENSMUSP00000039692; -.
DR   iPTMnet; Q9Z1P6; -.
DR   PhosphoSitePlus; Q9Z1P6; -.
DR   SwissPalm; Q9Z1P6; -.
DR   EPD; Q9Z1P6; -.
DR   jPOST; Q9Z1P6; -.
DR   MaxQB; Q9Z1P6; -.
DR   PaxDb; Q9Z1P6; -.
DR   PeptideAtlas; Q9Z1P6; -.
DR   PRIDE; Q9Z1P6; -.
DR   ProteomicsDB; 293640; -.
DR   DNASU; 66416; -.
DR   Ensembl; ENSMUST00000048249; ENSMUSP00000039692; ENSMUSG00000041881.
DR   GeneID; 66416; -.
DR   KEGG; mmu:66416; -.
DR   UCSC; uc008bzu.2; mouse.
DR   CTD; 4701; -.
DR   MGI; MGI:1913666; Ndufa7.
DR   VEuPathDB; HostDB:ENSMUSG00000041881; -.
DR   eggNOG; KOG4630; Eukaryota.
DR   GeneTree; ENSGT00390000006553; -.
DR   HOGENOM; CLU_149566_0_0_1; -.
DR   InParanoid; Q9Z1P6; -.
DR   OMA; NWASGQN; -.
DR   OrthoDB; 1465659at2759; -.
DR   PhylomeDB; Q9Z1P6; -.
DR   TreeFam; TF319126; -.
DR   Reactome; R-MMU-611105; Respiratory electron transport.
DR   Reactome; R-MMU-6799198; Complex I biogenesis.
DR   BioGRID-ORCS; 66416; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Ndufa7; mouse.
DR   PRO; PR:Q9Z1P6; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q9Z1P6; protein.
DR   Bgee; ENSMUSG00000041881; Expressed in choroid plexus of fourth ventricle and 260 other tissues.
DR   ExpressionAtlas; Q9Z1P6; baseline and differential.
DR   Genevisible; Q9Z1P6; MM.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR   GO; GO:0005761; C:mitochondrial ribosome; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR   GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR   InterPro; IPR009947; NDUA7.
DR   PANTHER; PTHR12485; PTHR12485; 1.
DR   Pfam; PF07347; CI-B14_5a; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q05752"
FT   CHAIN           2..113
FT                   /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT                   subunit 7"
FT                   /id="PRO_0000118835"
FT   REGION          80..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05752"
FT   MOD_RES         40
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         96
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O95182"
FT   TURN            5..7
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           8..16
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   STRAND          21..23
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   STRAND          28..31
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   TURN            54..56
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:6ZR2"
FT   STRAND          67..70
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   TURN            72..75
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
SQ   SEQUENCE   113 AA;  12576 MW;  875912131AE4C1D9 CRC64;
     MASATRVIQK LRNWASGQDL QAKLQLRYQE IAKRTQPPPK LPVGPSHKLS NNYYCTRDGR
     REVVPPSIIM SSQKALVSGK AAESSAMAAT EKKAVTPAPP MKRWELSKDQ PYL
 
 
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