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NDUA5_BOVIN
ID   NDUA5_BOVIN             Reviewed;         116 AA.
AC   P23935; Q32P63;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5;
DE   AltName: Full=Complex I subunit B13;
DE   AltName: Full=Complex I-13kD-B;
DE            Short=CI-13kD-B;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 13 kDa-B subunit;
GN   Name=NDUFA5;
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 SUBCELLULAR
RP   LOCATION.
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=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 2-116, ACETYLATION AT ALA-2, AND SUBCELLULAR LOCATION.
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   [4]
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   [5]
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:Q16718}.
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:1518044,
CC       ECO:0000305|PubMed:18721790, ECO:0000305|PubMed:1907966}; Peripheral
CC       membrane protein; Matrix side.
CC   -!- SIMILARITY: Belongs to the complex I NDUFA5 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; X63218; CAA44903.1; -; mRNA.
DR   EMBL; BC108243; AAI08244.1; -; mRNA.
DR   PIR; S28244; S28244.
DR   RefSeq; NP_787023.1; NM_175829.2.
DR   PDB; 5LC5; EM; 4.35 A; V=1-116.
DR   PDB; 5LDW; EM; 4.27 A; V=2-116.
DR   PDB; 5LDX; EM; 5.60 A; V=2-116.
DR   PDB; 5O31; EM; 4.13 A; V=2-116.
DR   PDB; 7QSD; EM; 3.10 A; V=1-116.
DR   PDBsum; 5LC5; -.
DR   PDBsum; 5LDW; -.
DR   PDBsum; 5LDX; -.
DR   PDBsum; 5O31; -.
DR   PDBsum; 7QSD; -.
DR   AlphaFoldDB; P23935; -.
DR   SMR; P23935; -.
DR   CORUM; P23935; -.
DR   DIP; DIP-38832N; -.
DR   IntAct; P23935; 4.
DR   STRING; 9913.ENSBTAP00000012287; -.
DR   TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR   iPTMnet; P23935; -.
DR   PaxDb; P23935; -.
DR   PRIDE; P23935; -.
DR   Ensembl; ENSBTAT00000012287; ENSBTAP00000012287; ENSBTAG00000009334.
DR   GeneID; 327714; -.
DR   KEGG; bta:327714; -.
DR   CTD; 4698; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009334; -.
DR   VGNC; VGNC:31949; NDUFA5.
DR   eggNOG; KOG3365; Eukaryota.
DR   GeneTree; ENSGT00390000008099; -.
DR   HOGENOM; CLU_099943_2_0_1; -.
DR   InParanoid; P23935; -.
DR   OMA; VNEHPHR; -.
DR   OrthoDB; 1372253at2759; -.
DR   TreeFam; TF313785; -.
DR   Reactome; R-BTA-611105; Respiratory electron transport.
DR   Reactome; R-BTA-6799198; Complex I biogenesis.
DR   Reactome; R-BTA-9013408; RHOG GTPase cycle.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000009334; Expressed in tongue muscle and 104 other tissues.
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   GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR   InterPro; IPR006806; NDUFA5.
DR   PANTHER; PTHR12653; PTHR12653; 1.
DR   Pfam; PF04716; ETC_C1_NDUFA5; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1907966"
FT   CHAIN           2..116
FT                   /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT                   subunit 5"
FT                   /id="PRO_0000118631"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:1907966"
FT   MOD_RES         30
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16718"
FT   MOD_RES         46
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CPP6"
FT   MOD_RES         60
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16718"
FT   MOD_RES         89
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q63362"
FT   MOD_RES         98
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CPP6"
FT   MOD_RES         98
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CPP6"
FT   CONFLICT        108
FT                   /note="P -> W (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112
FT                   /note="Missing (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   116 AA;  13316 MW;  8AD6550D2ECD7B0D CRC64;
     MAGLLKKTTG LVGLAVCETP HERLKILYTK ILDVLGHIPK NAAYRKYTEQ ITNEKLSMVK
     AEPDVKKLEE RLQGGQIEEV ILQAENELSL ARKMIQWKPW EPLVEEPPAS QWKWPI
 
 
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