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NDUAA_RAT
ID   NDUAA_RAT               Reviewed;         355 AA.
AC   Q561S0; Q80WE0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial;
DE   AltName: Full=Complex I-42kD;
DE            Short=CI-42kD;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 42 kDa subunit;
DE   Flags: Precursor;
GN   Name=Ndufa10;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zhang G., Liu F., Yang P.;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 140-161; 182-192 AND 303-326, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (NOV-2006) to UniProtKB.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=Holtzman; TISSUE=Sperm;
RX   PubMed=20966424; DOI=10.2164/jandrol.110.010967;
RA   Suryawanshi A.R., Khan S.A., Gajbhiye R.K., Gurav M.Y., Khole V.V.;
RT   "Differential proteomics leads to identification of domain specific
RT   epididymal sperm proteins.";
RL   J. Androl. 32:240-259(2011).
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:O95299}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits. This a
CC       component of the hydrophobic protein fraction.
CC       {ECO:0000250|UniProtKB:O95299}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:O95299}.
CC   -!- TISSUE SPECIFICITY: Expressed in the head and flagellum of epididymal
CC       sperm but not in testicular sperm (at protein level).
CC       {ECO:0000269|PubMed:20966424}.
CC   -!- PTM: Phosphorylation at Ser-250 by PINK1 is required for the binding
CC       and/or reduction of the complex I substrate ubiquinone.
CC       {ECO:0000250|UniProtKB:Q99LC3}.
CC   -!- SIMILARITY: Belongs to the complex I NDUFA10 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AY260163; AAP20092.1; -; mRNA.
DR   EMBL; BC093375; AAH93375.1; -; mRNA.
DR   RefSeq; NP_872612.1; NM_182671.2.
DR   RefSeq; NP_955789.2; NM_199495.2.
DR   AlphaFoldDB; Q561S0; -.
DR   SMR; Q561S0; -.
DR   BioGRID; 593710; 1.
DR   IntAct; Q561S0; 3.
DR   MINT; Q561S0; -.
DR   STRING; 10116.ENSRNOP00000022089; -.
DR   CarbonylDB; Q561S0; -.
DR   iPTMnet; Q561S0; -.
DR   PhosphoSitePlus; Q561S0; -.
DR   World-2DPAGE; 0004:Q561S0; -.
DR   jPOST; Q561S0; -.
DR   PaxDb; Q561S0; -.
DR   PRIDE; Q561S0; -.
DR   GeneID; 316632; -.
DR   GeneID; 678759; -.
DR   KEGG; rno:316632; -.
DR   KEGG; rno:678759; -.
DR   UCSC; RGD:727968; rat.
DR   CTD; 316632; -.
DR   CTD; 4705; -.
DR   RGD; 727968; Ndufa10.
DR   VEuPathDB; HostDB:ENSRNOG00000016470; -.
DR   eggNOG; KOG3877; Eukaryota.
DR   HOGENOM; CLU_050591_0_0_1; -.
DR   InParanoid; Q561S0; -.
DR   OMA; MFRQGYI; -.
DR   OrthoDB; 1147235at2759; -.
DR   PhylomeDB; Q561S0; -.
DR   TreeFam; TF314616; -.
DR   BRENDA; 7.1.1.2; 5301.
DR   Reactome; R-RNO-611105; Respiratory electron transport.
DR   Reactome; R-RNO-6799198; Complex I biogenesis.
DR   PRO; PR:Q561S0; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000016470; Expressed in heart and 19 other tissues.
DR   Genevisible; Q561S0; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISO:RGD.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISO:RGD.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   CDD; cd02030; NDUO42; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR031314; DNK_dom.
DR   InterPro; IPR015828; NDUFA10.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01712; dNK; 1.
DR   PIRSF; PIRSF000543; NADH_UQ_42KD; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; FAD;
KW   Flavoprotein; Mitochondrion; Phosphoprotein; Reference proteome;
KW   Respiratory chain; Transit peptide; Transport.
FT   TRANSIT         1..35
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:P34942"
FT   CHAIN           36..355
FT                   /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT                   subunit 10, mitochondrial"
FT                   /id="PRO_0000270761"
FT   MOD_RES         122
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC3"
FT   MOD_RES         122
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC3"
FT   MOD_RES         250
FT                   /note="Phosphoserine; by PINK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC3"
FT   MOD_RES         285
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LC3"
FT   CONFLICT        120
FT                   /note="N -> D (in Ref. 1; AAP20092)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176
FT                   /note="Q -> R (in Ref. 1; AAP20092)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        201
FT                   /note="P -> S (in Ref. 1; AAP20092)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="K -> Q (in Ref. 1; AAP20092)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        257
FT                   /note="V -> M (in Ref. 1; AAP20092)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   355 AA;  40493 MW;  DB59209F94B2CBD5 CRC64;
     MALRLLRLVP ASASARGLAA GAQRVGRIHT SVHCKLRYGL LASILGDKTT KKLHEYSRVI
     TVDGNICSGK NKLARDIAEQ LGMKHYPEAG IQYSSSTTGD GRPLDIEFSG SCSLEKFYDN
     PKSNDGNSYR LQSWLYASRL LQYSDALEHL LSTGQGVVLE RSIYSDFVFL EAMYNQGFIR
     KQCVDHYNEI KRLTLPEYLP PHAVIYIDVP VSEIQSRIQK KGDPHEMKVT SAYLQDIEDA
     YKKTFLPKMS EICEVLVYSS WEAEDSTKVV EDIEYLNYNK GPWLKQDDRT FHNLRMLVQD
     KREVLNYTTV PVYLPEITIG AHQGSRIYDS FRELPGRKYA PGYNADVGDK WIWLK
 
 
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