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NDUA2_BOVIN
ID   NDUA2_BOVIN             Reviewed;          99 AA.
AC   Q02370; Q148D8; Q2VYC4;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;
DE   AltName: Full=Complex I-B8;
DE            Short=CI-B8;
DE   AltName: Full=NADH-ubiquinone oxidoreductase B8 subunit;
GN   Name=NDUFA2;
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 40-45; 47-61 AND 63-68.
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 [GENOMIC DNA].
RA   Conrad M.L., Mawer M.A., Davis S.K., Koop B.F.;
RT   "Genomic sequencing of the T cell receptor alpha locus.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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:O43678}.
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 NDUFA2 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; X63219; CAA44904.1; -; mRNA.
DR   EMBL; AY227782; ABC02172.1; -; Genomic_DNA.
DR   EMBL; BC118428; AAI18429.1; -; mRNA.
DR   PIR; S28249; S28249.
DR   RefSeq; NP_787009.1; NM_175815.2.
DR   PDB; 5LC5; EM; 4.35 A; S=17-96.
DR   PDB; 5LDW; EM; 4.27 A; S=1-99.
DR   PDB; 5LDX; EM; 5.60 A; S=1-99.
DR   PDB; 5O31; EM; 4.13 A; S=2-99.
DR   PDB; 7QSD; EM; 3.10 A; S=1-99.
DR   PDBsum; 5LC5; -.
DR   PDBsum; 5LDW; -.
DR   PDBsum; 5LDX; -.
DR   PDBsum; 5O31; -.
DR   PDBsum; 7QSD; -.
DR   AlphaFoldDB; Q02370; -.
DR   SMR; Q02370; -.
DR   CORUM; Q02370; -.
DR   DIP; DIP-38834N; -.
DR   IntAct; Q02370; 18.
DR   STRING; 9913.ENSBTAP00000020018; -.
DR   TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR   PaxDb; Q02370; -.
DR   PRIDE; Q02370; -.
DR   Ensembl; ENSBTAT00000020018; ENSBTAP00000020018; ENSBTAG00000015041.
DR   GeneID; 327698; -.
DR   KEGG; bta:327698; -.
DR   CTD; 4695; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015041; -.
DR   eggNOG; KOG3446; Eukaryota.
DR   GeneTree; ENSGT00390000006178; -.
DR   HOGENOM; CLU_110897_0_0_1; -.
DR   InParanoid; Q02370; -.
DR   OMA; INSHYVA; -.
DR   OrthoDB; 1633416at2759; -.
DR   TreeFam; TF300229; -.
DR   Reactome; R-BTA-611105; Respiratory electron transport.
DR   Reactome; R-BTA-6799198; Complex I biogenesis.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000015041; Expressed in oocyte and 108 other tissues.
DR   GO; GO:0031966; C:mitochondrial membrane; ISS:AgBase.
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; IPR016464; NADH_Ub_cplx-1_asu_su-2.
DR   InterPro; IPR007741; Ribosome/NADH_DH.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12878; PTHR12878; 1.
DR   Pfam; PF05047; L51_S25_CI-B8; 1.
DR   PIRSF; PIRSF005822; NDUA2; 1.
DR   SMART; SM00916; L51_S25_CI-B8; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; 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:0000250|UniProtKB:O43678"
FT   CHAIN           2..99
FT                   /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT                   subunit 2"
FT                   /id="PRO_0000118788"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O43678"
FT   MOD_RES         64
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQ75"
FT   MOD_RES         64
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQ75"
FT   MOD_RES         75
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQ75"
FT   DISULFID        24..58
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        44
FT                   /note="L -> V (in Ref. 2; ABC02172)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   99 AA;  11080 MW;  B844420E64652EC2 CRC64;
     MAAAAAIRGV RGKLGLREIR IHLCQRSPGS QGVRDFIEKR YVELKKANPD LPILIRECSD
     VQPKLWARYA FGQEKNVSLN NFSADQVTRA LENVLSSKA
 
 
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