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NDUAC_MOUSE
ID   NDUAC_MOUSE             Reviewed;         145 AA.
AC   Q7TMF3; Q3TIA0;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12;
DE   AltName: Full=Complex I-B17.2;
DE            Short=CI-B17.2;
DE            Short=CIB17.2;
DE   AltName: Full=NADH-ubiquinone oxidoreductase subunit B17.2;
GN   Name=Ndufa12;
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].
RC   STRAIN=C57BL/6J, and DBA/2J;
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   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.
CC       {ECO:0000250|UniProtKB:Q9UI09}.
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits.
CC       {ECO:0000250|UniProtKB:Q9UI09}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q9UI09}; Peripheral membrane protein
CC       {ECO:0000255}; Matrix side {ECO:0000250|UniProtKB:Q9UI09}.
CC   -!- SIMILARITY: Belongs to the complex I NDUFA12 subunit family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB26955.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK010460; BAB26955.2; ALT_INIT; mRNA.
DR   EMBL; AK167943; BAE39946.1; -; mRNA.
DR   CCDS; CCDS24132.2; -.
DR   RefSeq; NP_079827.2; NM_025551.3.
DR   PDB; 6G2J; EM; 3.30 A; q=2-145.
DR   PDB; 6G72; EM; 3.90 A; q=2-145.
DR   PDB; 6ZR2; EM; 3.10 A; q=1-145.
DR   PDB; 6ZTQ; EM; 3.00 A; q=1-145.
DR   PDB; 7AK5; EM; 3.17 A; q=1-145.
DR   PDB; 7AK6; EM; 3.82 A; q=1-145.
DR   PDB; 7B93; EM; 3.04 A; q=1-145.
DR   PDB; 7PSA; EM; 3.40 A; q=1-145.
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; Q7TMF3; -.
DR   SMR; Q7TMF3; -.
DR   BioGRID; 211458; 38.
DR   ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR   CORUM; Q7TMF3; -.
DR   IntAct; Q7TMF3; 5.
DR   STRING; 10090.ENSMUSP00000136313; -.
DR   iPTMnet; Q7TMF3; -.
DR   PhosphoSitePlus; Q7TMF3; -.
DR   SwissPalm; Q7TMF3; -.
DR   EPD; Q7TMF3; -.
DR   jPOST; Q7TMF3; -.
DR   MaxQB; Q7TMF3; -.
DR   PaxDb; Q7TMF3; -.
DR   PeptideAtlas; Q7TMF3; -.
DR   PRIDE; Q7TMF3; -.
DR   ProteomicsDB; 293537; -.
DR   Antibodypedia; 30095; 179 antibodies from 27 providers.
DR   DNASU; 66414; -.
DR   Ensembl; ENSMUST00000020209; ENSMUSP00000020209; ENSMUSG00000020022.
DR   GeneID; 66414; -.
DR   KEGG; mmu:66414; -.
DR   CTD; 55967; -.
DR   MGI; MGI:1913664; Ndufa12.
DR   VEuPathDB; HostDB:ENSMUSG00000020022; -.
DR   eggNOG; KOG3382; Eukaryota.
DR   GeneTree; ENSGT00390000005848; -.
DR   HOGENOM; CLU_110455_1_0_1; -.
DR   InParanoid; Q7TMF3; -.
DR   OrthoDB; 1475919at2759; -.
DR   TreeFam; TF106106; -.
DR   Reactome; R-MMU-611105; Respiratory electron transport.
DR   Reactome; R-MMU-6799198; Complex I biogenesis.
DR   BioGRID-ORCS; 66414; 0 hits in 59 CRISPR screens.
DR   ChiTaRS; Ndufa12; mouse.
DR   PRO; PR:Q7TMF3; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q7TMF3; protein.
DR   Bgee; ENSMUSG00000020022; Expressed in right kidney and 88 other tissues.
DR   ExpressionAtlas; Q7TMF3; baseline and differential.
DR   Genevisible; Q7TMF3; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
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:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR   GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; ISO:MGI.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IEA:InterPro.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR   GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR   InterPro; IPR007763; NDUFA12.
DR   PANTHER; PTHR12910; PTHR12910; 1.
DR   Pfam; PF05071; NDUFA12; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Electron transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW   Transport.
FT   CHAIN           1..145
FT                   /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT                   subunit 12"
FT                   /id="PRO_0000118846"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:O97725"
FT   HELIX           3..14
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   STRAND          16..19
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           20..30
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   STRAND          37..41
FT                   /evidence="ECO:0007829|PDB:7B93"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   STRAND          47..50
FT                   /evidence="ECO:0007829|PDB:7B93"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   TURN            73..75
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           84..90
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   TURN            98..100
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   STRAND          118..122
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
SQ   SEQUENCE   145 AA;  17086 MW;  B53B37CD0DCDE8CA CRC64;
     MELVEVLKRG VQQVTGHGGL RGLLRVFFRA NDIRIGTLVG EDKYGNKYYE DNKQFFGRHR
     WVIYTTEMNG KNTFWDVDGS MVPPEWHRWL HCMTDDPPTT NPPTARKFIW TNHKFNVSAT
     PEQYVPYSTT RKKIHEWVPP STPYK
 
 
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