NDUS3_BOVIN
ID NDUS3_BOVIN Reviewed; 266 AA.
AC P23709;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:O75489};
DE AltName: Full=Complex I-30kD;
DE Short=CI-30kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 30 kDa subunit;
DE Flags: Precursor;
GN Name=NDUFS3;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1899621; DOI=10.1021/bi00221a024;
RA Pilkington S.J., Skehel J.M., Walker J.E.;
RT "The 30-kilodalton subunit of bovine mitochondrial complex I is homologous
RT to a protein coded in chloroplast DNA.";
RL Biochemistry 30:1901-1908(1991).
RN [2]
RP PROTEIN SEQUENCE OF 59-99 AND 197-266.
RC TISSUE=Heart;
RX PubMed=1907966; DOI=10.1093/oxfordjournals.jbchem.a123416;
RA Masui R., Wakabayashi S., Matsubara H., Hatefi Y.;
RT "The amino acid sequences of two 13 kDa polypeptides and partial amino acid
RT sequence of 30 kDa polypeptide of complex I from bovine heart mitochondria:
RT possible location of iron-sulfur clusters.";
RL J. Biochem. 109:534-543(1991).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, PROTEIN SEQUENCE OF N-TERMINUS, IDENTIFICATION IN
RP COMPLEX I, SUBCELLULAR 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 [4]
RP IDENTIFICATION IN COMPLEX I, SUBUNIT, 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 [5]
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:18721790, PubMed:10852722). Essential for the
CC catalytic activity and assembly of complex I (By similarity).
CC {ECO:0000250|UniProtKB:O75489, 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:O75489};
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). Interacts with NDUFAF3 (By
CC similarity). Interacts with RAB5IF (By similarity). Found in
CC subcomplexes containing subunits NDUFS2, MT-ND1 and NDUFA13 (By
CC similarity). {ECO:0000250|UniProtKB:O75489,
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 -!- SIMILARITY: Belongs to the complex I 30 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; M58469; AAA30663.1; ALT_SEQ; mRNA.
DR PIR; A37957; A37957.
DR RefSeq; NP_777244.1; NM_174819.3.
DR PDB; 5LC5; EM; 4.35 A; C=46-251.
DR PDB; 5LDW; EM; 4.27 A; C=39-266.
DR PDB; 5LDX; EM; 5.60 A; C=39-266.
DR PDB; 5O31; EM; 4.13 A; C=39-266.
DR PDB; 7QSD; EM; 3.10 A; C=1-266.
DR PDBsum; 5LC5; -.
DR PDBsum; 5LDW; -.
DR PDBsum; 5LDX; -.
DR PDBsum; 5O31; -.
DR PDBsum; 7QSD; -.
DR AlphaFoldDB; P23709; -.
DR SMR; P23709; -.
DR CORUM; P23709; -.
DR DIP; DIP-38807N; -.
DR IntAct; P23709; 3.
DR STRING; 9913.ENSBTAP00000024600; -.
DR TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; P23709; -.
DR PeptideAtlas; P23709; -.
DR PRIDE; P23709; -.
DR GeneID; 287327; -.
DR KEGG; bta:287327; -.
DR CTD; 4722; -.
DR eggNOG; KOG1713; Eukaryota.
DR InParanoid; P23709; -.
DR OrthoDB; 1276923at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0003954; F:NADH dehydrogenase activity; ISS:UniProtKB.
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 GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR Gene3D; 3.30.460.80; -; 1.
DR HAMAP; MF_01357; NDH1_NuoC; 1.
DR InterPro; IPR010218; NADH_DH_suC.
DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR InterPro; IPR020396; NADH_UbQ_OxRdtase_CS.
DR Pfam; PF00329; Complex1_30kDa; 1.
DR SUPFAM; SSF143243; SSF143243; 1.
DR TIGRFAMs; TIGR01961; NuoC_fam; 1.
DR PROSITE; PS00542; COMPLEX1_30K; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase;
KW Reference proteome; Respiratory chain; Transit peptide; Translocase;
KW Transport; Ubiquinone.
FT TRANSIT 1..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:10852722"
FT CHAIN 39..266
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 3, mitochondrial"
FT /id="PRO_0000019997"
FT CONFLICT 254
FT /note="L -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 266 AA; 30284 MW; 43494B3359D2FEB1 CRC64;
MAAAVAAAAR GCWQRLVGSA APARVAGRPS VLLLPVRRES SAADTRPTVR PRNDVAHKQL
SAFGEYVAEI LPKYVQQVQV SCFNELEICI HPDGVIPVLT FLRDHSNAQF KSLADLTAVD
IPTRQNRFEI VYNLLSLRFN SRIRVKTYTD ELTPIESSVP VYKAANWYER EIWDMFGVFF
ANHPDLRRIL TDYGFEGHPF RKDFPLSGYV ELRYDDEVKR VVAEPVELAQ EFRKFDLNSP
WEAFPAYRQP PESLKLEAGD TKPEAK
