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NDUC2_MOUSE
ID   NDUC2_MOUSE             Reviewed;         120 AA.
AC   Q9CQ54; Q3TLB2;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 subunit C2 {ECO:0000305};
DE   AltName: Full=Complex I-B14.5b;
DE            Short=CI-B14.5b;
DE   AltName: Full=NADH-ubiquinone oxidoreductase subunit B14.5b;
GN   Name=Ndufc2 {ECO:0000312|MGI:MGI:1344370};
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; TISSUE=Bone marrow, Kidney, Pancreas, and Stomach;
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 MRNA].
RC   TISSUE=Mammary gland;
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   [3]
RP   PROTEIN SEQUENCE OF 31-49; 79-104 AND 107-120, 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   [4]
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 but required for the complex assembly. Complex I
CC       functions in the transfer of electrons from NADH to the respiratory
CC       chain. The immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone. {ECO:0000250|UniProtKB:O95298}.
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits. Interacts with
CC       TMEM242 (By similarity). {ECO:0000250|UniProtKB:O95298}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:O95298}; Single-pass membrane protein
CC       {ECO:0000255}; Matrix side {ECO:0000250|UniProtKB:O95298}.
CC   -!- SIMILARITY: Belongs to the complex I NDUFC2 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AK002373; BAB22050.1; -; mRNA.
DR   EMBL; AK008889; BAB25955.1; -; mRNA.
DR   EMBL; AK019002; BAB31504.1; -; mRNA.
DR   EMBL; AK153547; BAE32084.1; -; mRNA.
DR   EMBL; AK166594; BAE38880.1; -; mRNA.
DR   EMBL; AK168342; BAE40279.1; -; mRNA.
DR   EMBL; BC002097; AAH02097.1; -; mRNA.
DR   CCDS; CCDS21457.1; -.
DR   RefSeq; NP_077182.1; NM_024220.2.
DR   PDB; 6G2J; EM; 3.30 A; d=1-120.
DR   PDB; 6G72; EM; 3.90 A; d=1-120.
DR   PDB; 6ZR2; EM; 3.10 A; d=1-120.
DR   PDB; 6ZTQ; EM; 3.00 A; d=1-120.
DR   PDB; 7AK5; EM; 3.17 A; d=1-120.
DR   PDB; 7AK6; EM; 3.82 A; d=1-120.
DR   PDB; 7B93; EM; 3.04 A; d=1-120.
DR   PDB; 7PSA; EM; 3.40 A; d=1-120.
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; Q9CQ54; -.
DR   SMR; Q9CQ54; -.
DR   BioGRID; 212722; 51.
DR   ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR   CORUM; Q9CQ54; -.
DR   IntAct; Q9CQ54; 3.
DR   STRING; 10090.ENSMUSP00000032882; -.
DR   iPTMnet; Q9CQ54; -.
DR   PhosphoSitePlus; Q9CQ54; -.
DR   SwissPalm; Q9CQ54; -.
DR   EPD; Q9CQ54; -.
DR   jPOST; Q9CQ54; -.
DR   MaxQB; Q9CQ54; -.
DR   PaxDb; Q9CQ54; -.
DR   PeptideAtlas; Q9CQ54; -.
DR   PRIDE; Q9CQ54; -.
DR   ProteomicsDB; 287469; -.
DR   DNASU; 68197; -.
DR   Ensembl; ENSMUST00000032882; ENSMUSP00000032882; ENSMUSG00000030647.
DR   GeneID; 68197; -.
DR   KEGG; mmu:68197; -.
DR   UCSC; uc009ijd.2; mouse.
DR   CTD; 4718; -.
DR   MGI; MGI:1344370; Ndufc2.
DR   VEuPathDB; HostDB:ENSMUSG00000030647; -.
DR   eggNOG; KOG4516; Eukaryota.
DR   GeneTree; ENSGT00390000010352; -.
DR   HOGENOM; CLU_156652_0_0_1; -.
DR   InParanoid; Q9CQ54; -.
DR   OMA; WFIGYHL; -.
DR   OrthoDB; 1606491at2759; -.
DR   PhylomeDB; Q9CQ54; -.
DR   TreeFam; TF314723; -.
DR   Reactome; R-MMU-611105; Respiratory electron transport.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-6799198; Complex I biogenesis.
DR   BioGRID-ORCS; 68197; 21 hits in 73 CRISPR screens.
DR   ChiTaRS; Ndufc2; mouse.
DR   PRO; PR:Q9CQ54; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9CQ54; protein.
DR   Bgee; ENSMUSG00000030647; Expressed in facial nucleus and 242 other tissues.
DR   ExpressionAtlas; Q9CQ54; baseline and differential.
DR   Genevisible; Q9CQ54; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR   GO; GO:0060547; P:negative regulation of necrotic cell death; ISO:MGI.
DR   GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR   GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISO:MGI.
DR   GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:MGI.
DR   GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISO:MGI.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR   GO; GO:0050727; P:regulation of inflammatory response; ISO:MGI.
DR   InterPro; IPR009423; NDUC2.
DR   PANTHER; PTHR13099; PTHR13099; 1.
DR   Pfam; PF06374; NDUF_C2; 1.
DR   PIRSF; PIRSF017834; NADH-UbQ_OxRdtase_b14.5b; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Electron transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Respiratory chain; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..120
FT                   /note="NADH dehydrogenase [ubiquinone] 1 subunit C2"
FT                   /id="PRO_0000118839"
FT   TRANSMEM        57..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   HELIX           2..4
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           16..20
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           29..48
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   STRAND          53..56
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           58..96
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   TURN            98..100
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   TURN            109..111
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
SQ   SEQUENCE   120 AA;  14164 MW;  C47218CE19B49D1C CRC64;
     MMNGRPGHEP LKFLPDEARS LPPPKLNDPR LVYMGLLGYC TGLMDNMLRM RPVMRAGLHR
     QLLFVTSFVF AGYFYLKRQN YLYAVKDHDM FGYIKLHPED FPEKEKKTYA EILEPFHPVR
 
 
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