ID   NDUS7_MOUSE             Reviewed;         224 AA.
AC   Q9DC70;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   04-NOV-2008, entry version 51.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;
DE            EC=1.6.5.3;
DE            EC=1.6.99.3;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 20 kDa subunit;
DE   AltName: Full=Complex I-20kD;
DE            Short=CI-20kD;
DE   Flags: Precursor;
GN   Name=Ndufs7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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=Colon;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 78-86; 127-140 AND 157-179, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory
CC       chain NADH dehydrogenase (Complex I) that is believed to belong to
CC       the minimal assembly required for catalysis. Complex I functions
CC       in the transfer of electrons from NADH to the respiratory chain.
CC       The immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + ubiquinone = NAD(+) + ubiquinol.
CC   -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster (Potential).
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits This is a
CC       component of the iron-sulfur (IP) fragment of the enzyme (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
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DR   EMBL; AK003132; BAB22592.1; -; mRNA.
DR   EMBL; BC013503; AAH13503.1; -; mRNA.
DR   RefSeq; NP_083548.1; -.
DR   UniGene; Mm.28712; -.
DR   Ensembl; ENSMUSG00000020153; Mus musculus.
DR   GeneID; 75406; -.
DR   KEGG; mmu:75406; -.
DR   NMPDR; fig|10090.3.peg.14026; -.
DR   MGI; MGI:1922656; Ndufs7.
DR   HOVERGEN; Q9DC70; -.
DR   NextBio; 342928; -.
DR   ArrayExpress; Q9DC70; -.
DR   CleanEx; MM_NDUFS7; -.
DR   GermOnline; ENSMUSG00000020153; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   InterPro; IPR006138; NADH_DHase_20kDa_su.
DR   InterPro; IPR014406; NiFe_hyd_3_ssu/Q_oxred_NuoB.
DR   InterPro; IPR006137; OxRdtase_q6.
DR   PANTHER; PTHR11995:SF2; NADH_DH_20kDa; 1.
DR   PANTHER; PTHR11995; NiFe_hyd_3_ssu/Q_oxred_NuoB; 1.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   TIGRFAMs; TIGR01957; nuoB_fam; 1.
DR   PROSITE; PS01150; COMPLEX1_20K; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Mitochondrion; NAD; Oxidoreductase;
KW   Respiratory chain; Transit peptide; Transport; Ubiquinone.
FT   TRANSIT       1     35       Mitochondrion (By similarity).
FT   CHAIN        36    224       NADH dehydrogenase [ubiquinone] iron-
FT                                sulfur protein 7, mitochondrial.
FT                                /FTId=PRO_0000020028.
FT   METAL        99     99       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       100    100       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       164    164       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       194    194       Iron-sulfur (4Fe-4S) (Potential).
SQ   SEQUENCE   224 AA;  24683 MW;  234F3FF0ABC36A92 CRC64;
     MAALAAPGLL SVRILGLRTA QVQLRRVHQS VATEGPSPSP SPSLSSTQSA VSKAGAGAVV
     PKLSHLPRSR AEYVVTKLDD LINWARRSSL WPMTFGLACC AVEMMHMAAP RYDMDRFGVV
     FRASPRQADV MIVAGTLTNK MAPALRKVYD QMPEPRYVVS MGSCANGGGY YHYSYSVVRG
     CDRIVPVDIY VPGCPPTAEA LLYGILQLQR KIKREQKLKI WYRR
//