NDUS7_BOVIN
ID NDUS7_BOVIN Reviewed; 216 AA.
AC P42026; Q2TBS6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:O75251};
DE AltName: Full=Complex I-20kD;
DE Short=CI-20kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 20 kDa subunit;
DE AltName: Full=PSST subunit;
DE Flags: Precursor;
GN Name=NDUFS7;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND PROTEIN SEQUENCE
RP OF N-TERMINUS.
RC TISSUE=Heart;
RX PubMed=1577158; DOI=10.1016/0014-5793(92)80248-f;
RA Arizmendi J.M., Runswick M.J., Skehel J.M., Walker J.E.;
RT "NADH: ubiquinone oxidoreductase from bovine heart mitochondria. A fourth
RT nuclear encoded subunit with a homologue encoded in chloroplast genomes.";
RL FEBS Lett. 301:237-242(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 107-120, AND HYDROXYLATION AT ARG-114.
RX PubMed=23836892; DOI=10.1074/jbc.m113.488106;
RA Carroll J., Ding S., Fearnley I.M., Walker J.E.;
RT "Post-translational modifications near the quinone binding site of
RT mammalian complex I.";
RL J. Biol. Chem. 288:24799-24808(2013).
RN [4]
RP PARTIAL PROTEIN SEQUENCE, SUBUNIT, IDENTIFICATION IN COMPLEX I, SUBCELLULAR
RP LOCATION, AND FUNCTION.
RX PubMed=10852722; DOI=10.1021/bi000335t;
RA Sazanov L.A., Peak-Chew S.Y., Fearnley I.M., Walker J.E.;
RT "Resolution of the membrane domain of bovine complex I into subcomplexes:
RT implications for the structural organization of the enzyme.";
RL Biochemistry 39:7229-7235(2000).
RN [5]
RP SUBUNIT, IDENTIFICATION IN COMPLEX I, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18721790; DOI=10.1016/j.ab.2008.07.029;
RA Lemma-Gray P., Valusova E., Carroll C.A., Weintraub S.T., Musatov A.,
RA Robinson N.C.;
RT "Subunit analysis of bovine heart complex I by reversed-phase high-
RT performance liquid chromatography, electrospray ionization-tandem mass
RT spectrometry, and matrix-assisted laser desorption/ionization-time-of-
RT flight mass spectrometry.";
RL Anal. Biochem. 382:116-121(2008).
RN [6]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=25209663; DOI=10.1038/nature13686;
RA Vinothkumar K.R., Zhu J., Hirst J.;
RT "Architecture of mammalian respiratory complex I.";
RL Nature 515:80-84(2014).
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 (PubMed:10852722, PubMed:18721790). Essential for the
CC catalytic activity of complex I (By similarity).
CC {ECO:0000250|UniProtKB:O75251, ECO:0000269|PubMed:10852722,
CC ECO:0000269|PubMed:18721790}.
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:O75251};
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 (PubMed:10852722,
CC PubMed:18721790, PubMed:25209663). This is a component of the iron-
CC sulfur (IP) fragment of the enzyme (PubMed:25209663).
CC {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790,
CC ECO:0000269|PubMed:25209663}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790,
CC ECO:0000269|PubMed:25209663}; Peripheral membrane protein
CC {ECO:0000305|PubMed:25209663}; Matrix side
CC {ECO:0000305|PubMed:25209663}.
CC -!- PTM: Hydroxylated ar Arg-114 by NDUFAF5 early in the pathway of
CC assembly of complex I, before the formation of the juncture between
CC peripheral and membrane arms. {ECO:0000250|UniProtKB:O75251}.
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; X65020; CAA46154.1; -; mRNA.
DR EMBL; BC109716; AAI09717.1; -; mRNA.
DR PIR; S22371; S22371.
DR RefSeq; NP_001033111.1; NM_001038022.1.
DR RefSeq; XP_005209312.1; XM_005209255.3.
DR RefSeq; XP_005209313.1; XM_005209256.1.
DR PDB; 5LC5; EM; 4.35 A; B=64-210.
DR PDB; 5LDW; EM; 4.27 A; B=38-216.
DR PDB; 5LDX; EM; 5.60 A; B=38-216.
DR PDB; 5LNK; EM; 3.90 A; 6=38-216.
DR PDB; 5O31; EM; 4.13 A; B=38-216.
DR PDB; 7QSD; EM; 3.10 A; B=1-216.
DR PDBsum; 5LC5; -.
DR PDBsum; 5LDW; -.
DR PDBsum; 5LDX; -.
DR PDBsum; 5LNK; -.
DR PDBsum; 5O31; -.
DR PDBsum; 7QSD; -.
DR AlphaFoldDB; P42026; -.
DR SMR; P42026; -.
DR CORUM; P42026; -.
DR DIP; DIP-38820N; -.
DR IntAct; P42026; 2.
DR STRING; 9913.ENSBTAP00000025870; -.
DR TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; P42026; -.
DR PeptideAtlas; P42026; -.
DR PRIDE; P42026; -.
DR Ensembl; ENSBTAT00000025870; ENSBTAP00000025870; ENSBTAG00000019419.
DR Ensembl; ENSBTAT00000053067; ENSBTAP00000051744; ENSBTAG00000019419.
DR GeneID; 338079; -.
DR KEGG; bta:338079; -.
DR CTD; 374291; -.
DR VEuPathDB; HostDB:ENSBTAG00000019419; -.
DR VGNC; VGNC:31972; NDUFS7.
DR eggNOG; KOG1687; Eukaryota.
DR GeneTree; ENSGT00390000006565; -.
DR HOGENOM; CLU_055737_1_2_1; -.
DR InParanoid; P42026; -.
DR OMA; AGWVRKS; -.
DR OrthoDB; 1278656at2759; -.
DR TreeFam; TF312859; -.
DR Reactome; R-BTA-611105; Respiratory electron transport.
DR Reactome; R-BTA-6799198; Complex I biogenesis.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000019419; Expressed in laryngeal cartilage and 108 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 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:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISS:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR HAMAP; MF_01356; NDH1_NuoB; 1.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR Pfam; PF01058; Oxidored_q6; 1.
DR TIGRFAMs; TIGR01957; nuoB_fam; 1.
DR PROSITE; PS01150; COMPLEX1_20K; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport;
KW Hydroxylation; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Oxidoreductase; Reference proteome;
KW Respiratory chain; Transit peptide; Translocase; Transport; Ubiquinone.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1577158"
FT CHAIN 38..216
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 7, mitochondrial"
FT /id="PRO_0000020026"
FT BINDING 91
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 186
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT MOD_RES 114
FT /note="Hydroxyarginine"
FT /evidence="ECO:0000269|PubMed:23836892"
SQ SEQUENCE 216 AA; 23771 MW; 514B8A63C59BE641 CRC64;
MAALAALRLL HPILAVRSGV GAALQVRGVH SSMAADSPSS TQPAVSQARA VVPKPAALPS
SRGEYVVAKL DDLINWARRS SLWPMTFGLA CCAVEMMHMA APRYDMDRFG VVFRASPRQS
DVMIVAGTLT NKMAPALRKV YDQMPEPRYV VSMGSCANGG GYYHYSYSVV RGCDRIVPVD
IYVPGCPPTA EALLYGILQL QKKIKREKRL RIWYRR
