NDUV1_GORGO
ID NDUV1_GORGO Reviewed; 464 AA.
AC Q0MQI5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;
DE EC=7.1.1.2;
DE AltName: Full=Complex I-51kD;
DE Short=CI-51kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 51 kDa subunit;
DE Flags: Precursor;
GN Name=NDUFV1;
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. {ECO:0000250|UniProtKB:P25708}.
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=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000305};
CC Note=Binds 1 FMN. {ECO:0000305};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits (By similarity). This is
CC a component of the flavoprotein-sulfur (FP) fragment of the enzyme (By
CC similarity). Interacts with RAB5IF (By similarity).
CC {ECO:0000250|UniProtKB:P49821}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P25708}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P25708}; Matrix side
CC {ECO:0000250|UniProtKB:P25708}.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; DQ885649; ABH12158.1; -; mRNA.
DR RefSeq; NP_001266473.1; NM_001279544.1.
DR AlphaFoldDB; Q0MQI5; -.
DR SMR; Q0MQI5; -.
DR STRING; 9593.ENSGGOP00000011650; -.
DR Ensembl; ENSGGOT00000011987; ENSGGOP00000011650; ENSGGOG00000011943.
DR GeneID; 101142811; -.
DR KEGG; ggo:101142811; -.
DR CTD; 4723; -.
DR eggNOG; KOG2658; Eukaryota.
DR GeneTree; ENSGT00390000010641; -.
DR HOGENOM; CLU_014881_0_1_1; -.
DR InParanoid; Q0MQI5; -.
DR OMA; CDDVIMD; -.
DR OrthoDB; 549172at2759; -.
DR Proteomes; UP000001519; Chromosome 11.
DR Bgee; ENSGGOG00000011943; Expressed in heart and 6 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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 Gene3D; 1.20.1440.230; -; 1.
DR Gene3D; 3.40.50.11540; -; 1.
DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR InterPro; IPR011537; NADH-UbQ_OxRdtase_suF.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR InterPro; IPR019554; Soluble_ligand-bd.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF10531; SLBB; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF140490; SSF140490; 1.
DR SUPFAM; SSF142019; SSF142019; 1.
DR TIGRFAMs; TIGR01959; nuoF_fam; 1.
DR PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Acetylation; Electron transport; Flavoprotein; FMN; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Methylation; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Oxidoreductase; Reference proteome;
KW Respiratory chain; Transit peptide; Translocase; Transport; Ubiquinone.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 21..464
FT /note="NADH dehydrogenase [ubiquinone] flavoprotein 1,
FT mitochondrial"
FT /id="PRO_0000251876"
FT BINDING 87..96
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250"
FT BINDING 199..247
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 382
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 385
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 425
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT MOD_RES 81
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91YT0"
FT MOD_RES 81
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91YT0"
FT MOD_RES 104
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91YT0"
FT MOD_RES 257
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q91YT0"
FT MOD_RES 375
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91YT0"
SQ SEQUENCE 464 AA; 50847 MW; 1641620FDD4794A0 CRC64;
MLATRRLLSW SLPARVSVRF SGDTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGALSRG
DWYKTKEILL KGPDWILGEI KTSGLRGRGG AGFPTGLKWS FMNKPSDGRP KYLVVNADEG
EPGTCKDREI LRHDPHKLVE GCLVGGRAMG ARAAYIYIRG EFYNEASNLQ VAIREAYEAG
LIGKNACGSG YDFDVFVVRG AGAYICGEET ALIESIEGKQ GKPRLKPPFP ADVGVFGCPT
TVANVETVAV SPTICRRGGT WFSGFGRERN SGTKLFNISG HVNHPCTVEE EMSVPLKELI
EKHAGGVTGG WENLLAVIPG GSSTPLIPKS VCETVLMDFD ALVQAQTGLG TAAVIVMDRS
TDIVKAIARL IEFYKHESCG QCTPCREGVD WMNKVMARFV RGDARPAEID SLWEISKQIE
GHTICALGDG AAWPVQGLIR HFRPELEERM QRFAQQHQAR QAAS
