ID NDUV2_GORGO Reviewed; 249 AA. AC Q0MQI8; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2006, sequence version 1. DT 24-JAN-2024, entry version 92. 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 Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Gorilla. OX NCBI_TaxID=9595; 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; DQ885646; ABH12155.1; -; mRNA. DR RefSeq; NP_001266570.1; NM_001279641.1. DR AlphaFoldDB; Q0MQI8; -. DR SMR; Q0MQI8; -. DR STRING; 9593.ENSGGOP00000022602; -. DR GeneID; 101146734; -. DR KEGG; ggo:101146734; -. DR CTD; 4729; -. DR eggNOG; KOG3196; Eukaryota. DR InParanoid; Q0MQI8; -. DR OrthoDB; 177389at2759; -. DR Proteomes; UP000001519; Unplaced. 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_0000251879" 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; 27354 MW; 500355C8F6BE2C78 CRC64; MFFSAALRAR AAGLTAQWGR HVRNLHKTAM QNGAGGALFV HRDTPENNPD TPFDFTPENY KRIEAIVKNY PEGHKAAAVL PVLDLAQRQN GWLPISAMNK VAEVLQVPPM RVYEVATFYT MYNRKPVGKY HIQVCTTTPC MLRNSDSILE AIQKKLGIKV GETTPDKLFT LIEVECLGAC VNAPMVQIND NYYEDLTAKD IEEIIDELKA GKIPKPGPRS GRFSCEPAGG LTSLTEPPKG PGFGVQAGL //