NDUS5_BOVIN
ID NDUS5_BOVIN Reviewed; 106 AA.
AC Q02379; Q3ZC47;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 5;
DE AltName: Full=Complex I-15 kDa;
DE Short=CI-15 kDa;
DE AltName: Full=NADH-ubiquinone oxidoreductase 15 kDa subunit;
GN Name=NDUFS5;
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 PROTEIN SEQUENCE OF 2-23.
RC TISSUE=Heart;
RX PubMed=1518044; DOI=10.1016/0022-2836(92)91052-q;
RA Walker J.E., Arizmendi J.M., Dupuis A., Fearnley I.M., Finel M., Medd S.M.,
RA Pilkington S.J., Runswick M.J., Skehel J.M.;
RT "Sequences of 20 subunits of NADH:ubiquinone oxidoreductase from bovine
RT heart mitochondria. Application of a novel strategy for sequencing proteins
RT using the polymerase chain reaction.";
RL J. Mol. Biol. 226:1051-1072(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PARTIAL PROTEIN SEQUENCE, SUBUNIT, IDENTIFICATION IN COMPLEX I, AND
RP SUBCELLULAR LOCATION.
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 SUBUNIT, IDENTIFICATION IN COMPLEX I, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC chain NADH dehydrogenase (Complex I), that is believed not to be
CC involved in catalysis. Complex I functions in the transfer of electrons
CC from NADH to the respiratory chain. The immediate electron acceptor for
CC the enzyme is believed to be ubiquinone.
CC {ECO:0000250|UniProtKB:O43920}.
CC -!- SUBUNIT: Mammalian complex I is composed of 45 different subunits. This
CC is a component of the iron-sulfur (IP) fragment of the enzyme.
CC {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:10852722, ECO:0000305|PubMed:18721790}; Peripheral
CC membrane protein {ECO:0000305}. Mitochondrion intermembrane space
CC {ECO:0000305}.
CC -!- DOMAIN: Contains two C-X9-C motifs that are predicted to form a helix-
CC coil-helix structure, permitting the formation of intramolecular
CC disulfide bonds. {ECO:0000250|UniProtKB:O43920}.
CC -!- SIMILARITY: Belongs to the complex I NDUFS5 subunit family.
CC {ECO:0000305}.
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DR EMBL; X63220; CAA44905.1; -; mRNA.
DR EMBL; BC102919; AAI02920.1; -; mRNA.
DR PIR; S28239; S28239.
DR RefSeq; NP_788825.1; NM_176652.2.
DR PDB; 5LC5; EM; 4.35 A; e=1-106.
DR PDB; 5LDW; EM; 4.27 A; e=2-106.
DR PDB; 5LDX; EM; 5.60 A; e=1-106.
DR PDB; 5O31; EM; 4.13 A; e=2-106.
DR PDB; 7QSD; EM; 3.10 A; e=1-106.
DR PDBsum; 5LC5; -.
DR PDBsum; 5LDW; -.
DR PDBsum; 5LDX; -.
DR PDBsum; 5O31; -.
DR PDBsum; 7QSD; -.
DR AlphaFoldDB; Q02379; -.
DR SMR; Q02379; -.
DR CORUM; Q02379; -.
DR DIP; DIP-38809N; -.
DR IntAct; Q02379; 2.
DR STRING; 9913.ENSBTAP00000013507; -.
DR TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; Q02379; -.
DR PRIDE; Q02379; -.
DR Ensembl; ENSBTAT00000013507; ENSBTAP00000013507; ENSBTAG00000010232.
DR Ensembl; ENSBTAT00000077219; ENSBTAP00000057919; ENSBTAG00000010232.
DR GeneID; 338057; -.
DR KEGG; bta:338057; -.
DR CTD; 4725; -.
DR VEuPathDB; HostDB:ENSBTAG00000010232; -.
DR VGNC; VGNC:31970; NDUFS5.
DR eggNOG; KOG4110; Eukaryota.
DR GeneTree; ENSGT00390000002919; -.
DR HOGENOM; CLU_176387_0_0_1; -.
DR InParanoid; Q02379; -.
DR OMA; CAHGIGQ; -.
DR OrthoDB; 1549192at2759; -.
DR TreeFam; TF332111; -.
DR Reactome; R-BTA-611105; Respiratory electron transport.
DR Reactome; R-BTA-6799198; Complex I biogenesis.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000010232; Expressed in oocyte and 106 other tissues.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR InterPro; IPR019342; NADH_UbQ_OxRdtase_FeS-su5.
DR PANTHER; PTHR15224; PTHR15224; 1.
DR Pfam; PF10200; Ndufs5; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1518044"
FT CHAIN 2..106
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 5"
FT /id="PRO_0000118785"
FT DOMAIN 30..74
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 84..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 33..43
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 56..66
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 33..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 43..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 106 AA; 12668 MW; 75BE02EF2C1A9144 CRC64;
MPFFDVQKRL GVDLDRWMTI QSAEQPHKIP SRCHAFEKEW IECAHGIGSI RAEKECKIEF
EDFRECLLRQ KTMKRLHAIR RQREKLIKEG KYTPPPHHSG QEEPRS
