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NU2M_DROYA
ID   NU2M_DROYA              Reviewed;         341 AA.
AC   P03895;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 2;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 2;
GN   Name=mt:ND2; Synonyms=ND2;
OS   Drosophila yakuba (Fruit fly).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6314262; DOI=10.1093/nar/11.19.6859;
RA   Clary D.O., Wolstenholme D.R.;
RT   "Genes for cytochrome c oxidase subunit I, URF2, and three tRNAs in
RT   Drosophila mitochondrial DNA.";
RL   Nucleic Acids Res. 11:6859-6872(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2317.6 Ivory Coast;
RX   PubMed=3001325; DOI=10.1007/bf02099755;
RA   Clary D.O., Wolstenholme D.R.;
RT   "The mitochondrial DNA molecular of Drosophila yakuba: nucleotide sequence,
RT   gene organization, and genetic code.";
RL   J. Mol. Evol. 22:252-271(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
RX   PubMed=6294611; DOI=10.1093/nar/10.21.6619;
RA   Clary D.O., Goddard J.M., Martin S.C., Fauron C.M.-R., Wolstenholme D.R.;
RT   "Drosophila mitochondrial DNA: a novel gene order.";
RL   Nucleic Acids Res. 10:6619-6637(1982).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
RX   PubMed=3116271; DOI=10.1007/bf02101753;
RA   Clary D.O., Wolstenholme D.R.;
RT   "Drosophila mitochondrial DNA: conserved sequences in the A + T-rich region
RT   and supporting evidence for a secondary structure model of the small
RT   ribosomal RNA.";
RL   J. Mol. Evol. 25:116-125(1987).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) that is believed to belong to the
CC       minimal assembly required for catalysis. Complex I functions in the
CC       transfer of electrons from NADH to the respiratory chain. The immediate
CC       electron acceptor for the enzyme is believed to be ubiquinone (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC         COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000305}.
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DR   EMBL; X05915; CAA29342.1; -; Genomic_DNA.
DR   EMBL; X03240; CAA26985.1; -; Genomic_DNA.
DR   PIR; B93488; QXFF2Y.
DR   RefSeq; NP_006902.1; NC_001322.1.
DR   AlphaFoldDB; P03895; -.
DR   SMR; P03895; -.
DR   PRIDE; P03895; -.
DR   GeneID; 807621; -.
DR   KEGG; dya:ND2; -.
DR   CTD; 4536; -.
DR   FlyBase; FBgn0013184; Dyak\mt:ND2.
DR   Proteomes; UP000002282; Mitochondrion.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro.
DR   InterPro; IPR010933; NADH_DH_su2_C.
DR   InterPro; IPR003917; NADH_UbQ_OxRdtase_chain2.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   Pfam; PF06444; NADH_dehy_S2_C; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   PRINTS; PR01436; NADHDHGNASE2.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   NAD; Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   CHAIN           1..341
FT                   /note="NADH-ubiquinone oxidoreductase chain 2"
FT                   /id="PRO_0000117584"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   341 AA;  39496 MW;  E6117DE50BE9D4AF CRC64;
     MFYNSSKILF TTIMIIGTLI TVTSNSWLGA WMGLEINLLS FIPLLSDNNN LMSTEASLKY
     FLTQALASTV LLFSSILLML ANNLNNEINE SFTSMIIMSA LLLKSGAAPF HFWFPNMMEG
     LTWMNALMLM TWQKIAPLML ISYLNIKNLL LISVILSVII GAIGGLNQTS LRKLMAFSSI
     NHLGWMLSSL MISESIWLIY FIFYSFLSFV LTFMFNIFKL FHLNQLFSWF VNSKILKFSL
     FMNFLSLGGL PPFLGFLPKW LVIQQLTMCN QYFLLTLMMM STLITLFFYL RICYSAFMLN
     YFENNWIMEM NMNSNNTNLY LIMTFFSIFG LFLISLFFFM L
 
 
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