NDUV2_PANTR
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 03-AUG-2022, entry version 111.
DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;
DE EC=7.1.1.2;
DE AltName: Full=NADH-ubiquinone oxidoreductase 24 kDa subunit;
DE Flags: Precursor;
GN Name=NDUFV2;
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. {ECO:0000250|UniProtKB:P04394}.
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
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}.
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DR EMBL; DQ885645; ABH12154.1; -; mRNA.
DR RefSeq; NP_001065254.1; NM_001071786.1.
DR AlphaFoldDB; Q0MQI9; -.
DR SMR; Q0MQI9; -.
DR STRING; 9598.ENSPTRP00000016775; -.
DR PaxDb; Q0MQI9; -.
DR Ensembl; ENSPTRT00000099813; ENSPTRP00000068755; ENSPTRG00000009856.
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; 1396088at2759; -.
DR TreeFam; TF300004; -.
DR Proteomes; UP000002277; Chromosome 18.
DR Bgee; ENSPTRG00000009856; Expressed in heart and 20 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
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; IEA:UniProtKB-EC.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR CDD; cd03064; TRX_Fd_NuoE; 1.
DR Gene3D; 1.10.10.1590; -; 1.
DR InterPro; IPR002023; NuoE-like.
DR InterPro; IPR042128; NuoE_dom.
DR InterPro; IPR041921; NuoE_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
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 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:0000255"
FT BINDING 140
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 176
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 180
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
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
