NDUA7_BOVIN
ID NDUA7_BOVIN Reviewed; 113 AA.
AC Q05752; A6H7C3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7;
DE AltName: Full=Complex I-B14.5a;
DE Short=CI-B14.5a;
DE AltName: Full=NADH-ubiquinone oxidoreductase subunit B14.5a;
GN Name=NDUFA7; Synonyms=CI-B14-5A;
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], ACETYLATION AT ALA-2, AND PARTIAL PROTEIN
RP SEQUENCE.
RC TISSUE=Heart;
RX PubMed=1426273; DOI=10.1016/0014-5793(92)81189-s;
RA Arizmendi J.M., Skehel J.M., Runswick M.J., Fearnley I.M., Walker J.E.;
RT "Complementary DNA sequences of two 14.5 kDa subunits of NADH:ubiquinone
RT oxidoreductase from bovine heart mitochondria. Completion of the primary
RT structure of the complex?";
RL FEBS Lett. 313:80-84(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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:O95182}.
CC -!- SUBUNIT: Complex I is composed of 45 different subunits.
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}; Matrix side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the complex I NDUFA7 subunit family.
CC {ECO:0000305}.
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DR EMBL; X68585; CAA48575.1; -; mRNA.
DR EMBL; BC146193; AAI46194.1; -; mRNA.
DR PIR; S27226; S27226.
DR RefSeq; NP_788831.1; NM_176658.2.
DR PDB; 5O31; EM; 4.13 A; r=2-113.
DR PDB; 7QSD; EM; 3.10 A; r=1-113.
DR PDBsum; 5O31; -.
DR PDBsum; 7QSD; -.
DR AlphaFoldDB; Q05752; -.
DR SMR; Q05752; -.
DR CORUM; Q05752; -.
DR DIP; DIP-38795N; -.
DR IntAct; Q05752; 2.
DR STRING; 9913.ENSBTAP00000056610; -.
DR TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR iPTMnet; Q05752; -.
DR PaxDb; Q05752; -.
DR PeptideAtlas; Q05752; -.
DR PRIDE; Q05752; -.
DR Ensembl; ENSBTAT00000077911; ENSBTAP00000069350; ENSBTAG00000052280.
DR GeneID; 338063; -.
DR KEGG; bta:338063; -.
DR CTD; 4701; -.
DR VEuPathDB; HostDB:ENSBTAG00000052280; -.
DR eggNOG; KOG4630; Eukaryota.
DR GeneTree; ENSGT00390000006553; -.
DR HOGENOM; CLU_149566_0_0_1; -.
DR InParanoid; Q05752; -.
DR OMA; NWASGQN; -.
DR OrthoDB; 1465659at2759; -.
DR TreeFam; TF319126; -.
DR Reactome; R-BTA-611105; Respiratory electron transport.
DR Reactome; R-BTA-6799198; Complex I biogenesis.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000052280; Expressed in tongue muscle and 108 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:AgBase.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0005761; C:mitochondrial ribosome; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; TAS:AgBase.
DR GO; GO:0016491; F:oxidoreductase activity; NAS:AgBase.
DR GO; GO:0003735; F:structural constituent of ribosome; HDA:UniProtKB.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; TAS:AgBase.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IDA:AgBase.
DR GO; GO:0032543; P:mitochondrial translation; HDA:UniProtKB.
DR InterPro; IPR009947; NDUA7.
DR PANTHER; PTHR12485; PTHR12485; 1.
DR Pfam; PF07347; CI-B14_5a; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1426273"
FT CHAIN 2..113
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 7"
FT /id="PRO_0000118833"
FT REGION 32..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:1426273"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1P6"
SQ SEQUENCE 113 AA; 12677 MW; 49A79CD9F3B46118 CRC64;
MASATRFIQW LRNWASGRDL QAKLQLRYQE ISKRTQPPPK LPVGPSHKLS NNYYCTRDGR
REAMPPSIVM SSQKVLVAGK PAESSAVAAS EKKAVSPAPP IKRWELSQDE PYL