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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
 
 
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