ID   NDUV2_PANTR             Reviewed;         249 AA.
AC   Q0MQI9;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   24-JAN-2024, entry version 116.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial {ECO:0000250|UniProtKB:P19404};
DE            EC=7.1.1.2 {ECO:0000250|UniProtKB:P19404};
DE   AltName: Full=NADH-ubiquinone oxidoreductase 24 kDa subunit;
DE   Flags: Precursor;
GN   Name=NDUFV2 {ECO:0000250|UniProtKB:P19404};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16828987; DOI=10.1016/j.gene.2006.03.015;
RA   Mishmar D., Ruiz-Pesini E., Mondragon-Palomino M., Procaccio V., Gaut B.,
RA   Wallace D.C.;
RT   "Adaptive selection of mitochondrial complex I subunits during primate
RT   radiation.";
RL   Gene 378:11-18(2006).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC       NADH through the respiratory chain, using ubiquinone as an electron
CC       acceptor. Parts of the peripheral arm of the enzyme, where the
CC       electrons from NADH are accepted by flavin mononucleotide (FMN) and
CC       then passed along a chain of iron-sulfur clusters by electron
CC       tunnelling to the final acceptor ubiquinone. Contains one iron-sulfur
CC       cluster. {ECO:0000250|UniProtKB:P19404}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC         COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC         Evidence={ECO:0000250|UniProtKB:P19404};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29092;
CC         Evidence={ECO:0000250|UniProtKB:P19404};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000250|UniProtKB:P19404};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:P19404};
CC   -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC       I) which is composed of 45 different subunits. This is a component of
CC       the flavoprotein-sulfur (FP) fragment of the enzyme (By similarity).
CC       {ECO:0000250|UniProtKB:P04394}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P04394}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P04394}; Matrix side
CC       {ECO:0000250|UniProtKB:P04394}.
CC   -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ885645; ABH12154.1; -; mRNA.
DR   RefSeq; NP_001065254.1; NM_001071786.1.
DR   AlphaFoldDB; Q0MQI9; -.
DR   SMR; Q0MQI9; -.
DR   STRING; 9598.ENSPTRP00000073779; -.
DR   PaxDb; 9598-ENSPTRP00000016775; -.
DR   Ensembl; ENSPTRT00000099813.1; ENSPTRP00000068755.1; ENSPTRG00000009856.6.
DR   GeneID; 455295; -.
DR   KEGG; ptr:455295; -.
DR   CTD; 4729; -.
DR   eggNOG; KOG3196; Eukaryota.
DR   GeneTree; ENSGT00390000017580; -.
DR   HOGENOM; CLU_054362_1_0_1; -.
DR   InParanoid; Q0MQI9; -.
DR   OrthoDB; 177389at2759; -.
DR   TreeFam; TF300004; -.
DR   Proteomes; UP000002277; Chromosome 18.
DR   Bgee; ENSPTRG00000009856; Expressed in heart and 20 other cell types or tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISS:UniProtKB.
DR   CDD; cd03064; TRX_Fd_NuoE; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.10.10.1590; NADH-quinone oxidoreductase subunit E; 1.
DR   InterPro; IPR002023; NuoE-like.
DR   InterPro; IPR042128; NuoE_dom.
DR   InterPro; IPR041921; NuoE_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR01958; nuoE_fam; 1.
DR   PANTHER; PTHR10371:SF3; NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10371; NADH DEHYDROGENASE UBIQUINONE FLAVOPROTEIN 2, MITOCHONDRIAL; 1.
DR   Pfam; PF01257; 2Fe-2S_thioredx; 1.
DR   PIRSF; PIRSF000216; NADH_DH_24kDa; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS01099; COMPLEX1_24K; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Acetylation; Electron transport; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; Respiratory chain;
KW   Transit peptide; Translocase; Transport; Ubiquinone.
FT   TRANSIT         1..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..249
FT                   /note="NADH dehydrogenase [ubiquinone] flavoprotein 2,
FT                   mitochondrial"
FT                   /id="PRO_0000251880"
FT   REGION          213..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         135
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P04394"
FT   BINDING         140
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P04394"
FT   BINDING         176
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P19404"
FT   BINDING         180
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P19404"
FT   MOD_RES         61
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D6J6"
FT   MOD_RES         193
FT                   /note="Phosphotyrosine; by SRC"
FT                   /evidence="ECO:0000250|UniProtKB:P19404"
SQ   SEQUENCE   249 AA;  27360 MW;  A94C5139329B084F CRC64;
     MFFSAALRAR AAGLTAHWGR HVRNLHKTAK QNGAGGALFV HRDTPENNPD TPFDFTPENY
     KRIEAIVKNY PEGHKAAAVL PVLDLAQRQN GWLPISAMNK VAEVLQVPPM RVYEVATFYT
     MYNRKPVGKY HIQVCTTTPC MLRNSDSILE AIQKKLGIKV GETTPDKLFT LIEVECLGAC
     VNAPMVQIND NYYEDLTAKD IEEIIDELKA GKIPKPGPRS GRFSCEPAGG LTSLTEPPKG
     PGFGVQAGL
//