ID   NDUS7_HUMAN             Reviewed;         213 AA.
AC   O75251; Q2T9H7; Q9BV17;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 3.
DT   07-JUL-2009, entry version 92.
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   AltName: Full=PSST subunit;
DE   Flags: Precursor;
GN   Name=NDUFS7;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97092888; PubMed=8938450; DOI=10.1006/geno.1996.0572;
RA   Hyslop S.J., Duncan A.M.V., Pitkanen S., Robinson B.H.;
RT   "Assignment of the PSST subunit gene of human mitochondrial complex I
RT   to chromosome 19p13.";
RL   Genomics 37:375-380(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-23.
RC   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [5]
RP   VARIANT LS MET-122.
RX   MEDLINE=99287516; PubMed=10360771;
RX   DOI=10.1002/1531-8249(199906)45:6<787::AID-ANA13>3.0.CO;2-6;
RA   Triepels R.H., van den Heuvel L., Loeffen J.L.C.M., Buskens C.A.F.,
RA   Smeets R.J.P., Rubio Gozalbo M.E., Budde S.M., Mariman E.C.M.,
RA   Wijburg F.A., Barth P.G., Trijbels J.M.F., Smeitink J.A.M.;
RT   "Leigh syndrome associated with a mutation in the NDUFS7 (PSST)
RT   nuclear encoded subunit of complex I.";
RL   Ann. Neurol. 45:787-790(1999).
RN   [6]
RP   VARIANT COMPLEX I DEFICIENCY MET-122.
RX   MEDLINE=99264232; PubMed=10330338; DOI=10.1086/302432;
RA   Smeitink J., van den Heuvel L.;
RT   "Human mitochondrial complex I in health and disease.";
RL   Am. J. Hum. Genet. 64:1505-1510(1999).
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- DISEASE: Defects in NDUFS7 are a cause of Leigh syndrome (LS)
CC       [MIM:256000]. LS is a severe neurological disorder characterized
CC       by bilaterally symmetrical necrotic lesions in subcortical brain
CC       regions.
CC   -!- DISEASE: Defects in NDUFS7 are a cause of complex I mitochondrial
CC       respiratory chain deficiency [MIM:252010]. Complex I (NADH-
CC       ubiquinone oxidoreductase), the largest complex of the
CC       mitochondrial respiratory chain, contains more than 40 subunits.
CC       It is embedded in the inner mitochondrial membrane and is partly
CC       protruding in the matrix. Complex I deficiency is the most common
CC       cause of mitochondrial disorders. It represents largely one-third
CC       of all cases of respiratory chain deficiency and is responsible
CC       for a variety of clinical symptoms, ranging from neurological
CC       disorders to cardiomyopathy, liver failure, and myopathy.
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC27669.1; Type=Erroneous gene model prediction;
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.genetests.org/query?gene=NDUFS7";
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DR   EMBL; AC005329; AAC27669.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC001715; AAH01715.2; -; mRNA.
DR   EMBL; BC005954; AAH05954.1; -; mRNA.
DR   EMBL; BC111517; AAI11518.1; -; mRNA.
DR   IPI; IPI00307749; -.
DR   RefSeq; NP_077718.3; -.
DR   UniGene; Hs.211914; -.
DR   IntAct; O75251; 2.
DR   PRIDE; O75251; -.
DR   Ensembl; ENSG00000115286; Homo sapiens.
DR   GeneID; 374291; -.
DR   KEGG; hsa:374291; -.
DR   UCSC; uc002lse.2; human.
DR   GeneCards; GC19P001334; -.
DR   H-InvDB; HIX0014582; -.
DR   H-InvDB; HIX0092829; -.
DR   HGNC; HGNC:7714; NDUFS7.
DR   MIM; 252010; phenotype.
DR   MIM; 256000; phenotype.
DR   MIM; 601825; gene.
DR   Orphanet; 506; Leigh syndrome.
DR   Orphanet; 2609; NADH-CoQ reductase deficiency.
DR   PharmGKB; PA31524; -.
DR   HOVERGEN; O75251; -.
DR   OMA; O75251; AIASNSE.
DR   BRENDA; 1.6.5.3; 247.
DR   BRENDA; 1.6.99.3; 247.
DR   Reactome; REACT_1505; Integration of energy metabolism.
DR   Reactome; REACT_15380; Diabetes pathways.
DR   DrugBank; DB00157; NADH.
DR   NextBio; 100146; -.
DR   ArrayExpress; O75251; -.
DR   Bgee; O75251; -.
DR   CleanEx; HS_NDUFS7; -.
DR   GermOnline; ENSG00000115286; Homo sapiens.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IMP:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; NAS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to u...; NAS:UniProtKB.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I a...; IMP:UniProtKB.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR006138; NADH_UbQ_OxRdtase_su-20kDa.
DR   InterPro; IPR014406; NiFe_hyd_3_ssu/Q_oxred_NuoB.
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; Complete proteome; Disease mutation; Electron transport; Iron;
KW   Iron-sulfur; Leigh syndrome; Metal-binding; Mitochondrion; NAD;
KW   Oxidoreductase; Polymorphism; Respiratory chain; Transit peptide;
KW   Transport; Ubiquinone.
FT   TRANSIT       1     38       Mitochondrion (By similarity).
FT   CHAIN        39    213       NADH dehydrogenase [ubiquinone] iron-
FT                                sulfur protein 7, mitochondrial.
FT                                /FTId=PRO_0000020027.
FT   METAL        88     88       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL        89     89       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       153    153       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       183    183       Iron-sulfur (4Fe-4S) (Potential).
FT   VARIANT      23     23       P -> L (in dbSNP:rs1142530).
FT                                /FTId=VAR_014482.
FT   VARIANT     122    122       V -> M (in complex I deficiency and LS).
FT                                /FTId=VAR_008848.
SQ   SEQUENCE   213 AA;  23564 MW;  B3547EA24643C1B0 CRC64;
     MAVLSAPGLR GFRILGLRSS VGPAVQARGV HQSVATDGPS STQPALPKAR AVAPKPSSRG
     EYVVAKLDDL VNWARRSSLW PMTFGLACCA VEMMHMAAPR YDMDRFGVVF RASPRQSDVM
     IVAGTLTNKM APALRKVYDQ MPEPRYVVSM GSCANGGGYY HYSYSVVRGC DRIVPVDIYI
     PGCPPTAEAL LYGILQLQRK IKRERRLQIW YRR
//