Entry euk:NDUV2_HUMAN

ID   NDUV2_HUMAN             Reviewed;         249 AA.
AC   P19404; Q9BV41;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 2.
DT   10-MAY-2017, entry version 188.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;
DE            EC=1.6.5.3;
DE            EC=1.6.99.3;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 24 kDa subunit;
DE   Flags: Precursor;
GN   Name=NDUFV2;
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], AND VARIANT ALA-29.
RX   PubMed=2500970; DOI=10.1021/bi00434a021;
RA   Pilkington S.J., Walker J.E.;
RT   "Mitochondrial NADH-ubiquinone reductase: complementary DNA sequences
RT   of import precursors of the bovine and human 24-kDa subunit.";
RL   Biochemistry 28:3257-3264(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=12611891; DOI=10.1074/jbc.C300064200;
RA   Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F.,
RA   Ghosh S.S., Capaldi R.A.;
RT   "The subunit composition of the human NADH dehydrogenase obtained by
RT   rapid one-step immunopurification.";
RL   J. Biol. Chem. 278:13619-13622(2003).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [5]
RP   PHOSPHORYLATION AT TYR-193.
RX   PubMed=22823520; DOI=10.1042/BJ20120509;
RA   Ogura M., Yamaki J., Homma M.K., Homma Y.;
RT   "Mitochondrial c-Src regulates cell survival through phosphorylation
RT   of respiratory chain components.";
RL   Biochem. J. 447:281-289(2012).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [7]
RP   CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ASN-32, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
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). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) +
CC       ubiquinol + 4 H(+)(Out).
CC   -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000305};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits. This is a
CC       component of the flavoprotein-sulfur (FP) fragment of the enzyme.
CC       {ECO:0000269|PubMed:12611891}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; M22538; AAA75390.1; -; mRNA.
DR   EMBL; BC001632; AAH01632.1; -; mRNA.
DR   EMBL; BC017487; AAH17487.1; -; mRNA.
DR   CCDS; CCDS11842.1; -.
DR   PIR; A30113; A30113.
DR   RefSeq; NP_066552.2; NM_021074.4.
DR   UniGene; Hs.464572; -.
DR   ProteinModelPortal; P19404; -.
DR   SMR; P19404; -.
DR   BioGrid; 110807; 58.
DR   IntAct; P19404; 31.
DR   MINT; MINT-4991740; -.
DR   STRING; 9606.ENSP00000327268; -.
DR   ChEMBL; CHEMBL2363065; -.
DR   DrugBank; DB00157; NADH.
DR   iPTMnet; P19404; -.
DR   PhosphoSitePlus; P19404; -.
DR   BioMuta; NDUFV2; -.
DR   DMDM; 20455499; -.
DR   SWISS-2DPAGE; P19404; -.
DR   UCD-2DPAGE; P19404; -.
DR   EPD; P19404; -.
DR   MaxQB; P19404; -.
DR   PaxDb; P19404; -.
DR   PeptideAtlas; P19404; -.
DR   PRIDE; P19404; -.
DR   TopDownProteomics; P19404; -.
DR   DNASU; 4729; -.
DR   Ensembl; ENST00000318388; ENSP00000327268; ENSG00000178127.
DR   GeneID; 4729; -.
DR   KEGG; hsa:4729; -.
DR   UCSC; uc002knu.3; human.
DR   CTD; 4729; -.
DR   DisGeNET; 4729; -.
DR   GeneCards; NDUFV2; -.
DR   HGNC; HGNC:7717; NDUFV2.
DR   HPA; HPA003404; -.
DR   HPA; HPA077896; -.
DR   MalaCards; NDUFV2; -.
DR   MIM; 600532; gene.
DR   neXtProt; NX_P19404; -.
DR   OpenTargets; ENSG00000178127; -.
DR   Orphanet; 2609; Isolated NADH-CoQ reductase deficiency.
DR   PharmGKB; PA31527; -.
DR   eggNOG; KOG3196; Eukaryota.
DR   eggNOG; COG1905; LUCA.
DR   GeneTree; ENSGT00390000017580; -.
DR   HOGENOM; HOG000257748; -.
DR   HOVERGEN; HBG029601; -.
DR   InParanoid; P19404; -.
DR   KO; K03943; -.
DR   PhylomeDB; P19404; -.
DR   TreeFam; TF300004; -.
DR   Reactome; R-HSA-611105; Respiratory electron transport.
DR   Reactome; R-HSA-6799198; Complex I biogenesis.
DR   ChiTaRS; NDUFV2; human.
DR   GeneWiki; NDUFV2; -.
DR   GenomeRNAi; 4729; -.
DR   PRO; PR:P19404; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   Bgee; ENSG00000178127; -.
DR   CleanEx; HS_NDUFV2; -.
DR   ExpressionAtlas; P19404; baseline and differential.
DR   Genevisible; P19404; HS.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; NAS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IMP:UniProtKB.
DR   GO; GO:0048738; P:cardiac muscle tissue development; IMP:UniProtKB.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP:UniProtKB.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; TAS:Reactome.
DR   GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR   InterPro; IPR002023; NuoE-like.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   PANTHER; PTHR10371; PTHR10371; 1.
DR   PIRSF; PIRSF000216; NADH_DH_24kDa; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01958; nuoE_fam; 1.
DR   PROSITE; PS01099; COMPLEX1_24K; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Acetylation; Complete proteome; Electron transport; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; NAD; Oxidoreductase; Phosphoprotein;
KW   Polymorphism; Reference proteome; Respiratory chain; Transit peptide;
KW   Transport; Ubiquinone.
FT   TRANSIT       1     32       Mitochondrion.
FT                                {ECO:0000244|PubMed:25944712}.
FT   CHAIN        33    249       NADH dehydrogenase [ubiquinone]
FT                                flavoprotein 2, mitochondrial.
FT                                /FTId=PRO_0000020003.
FT   METAL       135    135       Iron-sulfur (2Fe-2S). {ECO:0000255}.
FT   METAL       140    140       Iron-sulfur (2Fe-2S). {ECO:0000255}.
FT   METAL       176    176       Iron-sulfur (2Fe-2S). {ECO:0000255}.
FT   METAL       180    180       Iron-sulfur (2Fe-2S). {ECO:0000255}.
FT   MOD_RES      61     61       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9D6J6}.
FT   MOD_RES     193    193       Phosphotyrosine; by SRC.
FT                                {ECO:0000269|PubMed:22823520}.
FT   VARIANT      29     29       V -> A (in dbSNP:rs906807).
FT                                {ECO:0000269|PubMed:2500970}.
FT                                /FTId=VAR_016167.
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CC   The following FT lines are automated annotations from the MyHits database.
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FT   MYHIT       166    184       ipat:COMPLEX1_24K [T]
SQ   SEQUENCE   249 AA;  27392 MW;  AAF46ABB0908B177 CRC64;
     MFFSAALRAR AAGLTAHWGR HVRNLHKTVM QNGAGGALFV HRDTPENNPD TPFDFTPENY
     KRIEAIVKNY PEGHKAAAVL PVLDLAQRQN GWLPISAMNK VAEVLQVPPM RVYEVATFYT
     MYNRKPVGKY HIQVCTTTPC MLRNSDSILE AIQKKLGIKV GETTPDKLFT LIEVECLGAC
     VNAPMVQIND NYYEDLTAKD IEEIIDELKA GKIPKPGPRS GRFSCEPAGG LTSLTEPPKG
     PGFGVQAGL
//