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NU4M_TRIRU
ID   NU4M_TRIRU              Reviewed;         494 AA.
AC   Q36834; Q9T9N0;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 4;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 4;
GN   Name=ND4; Synonyms=NADH4;
OS   Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=5551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IP 1817.89;
RX   PubMed=10022946; DOI=10.1007/s002940050429;
RA   de Bievre C., Dujon B.;
RT   "Organisation of the mitochondrial genome of Trichophyton rubrum III. DNA
RT   sequence analysis of the NADH dehydrogenase subunits 1, 2, 3, 4, 5 and the
RT   cytochrome b gene.";
RL   Curr. Genet. 35:30-35(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 478-494.
RC   STRAIN=IP 1817.89;
RX   PubMed=8593686; DOI=10.1007/bf00518168;
RA   de Bievre C., Dujon B.;
RT   "Organisation of the mitochondrial genome of Trichophyton rubrum. DNA
RT   sequence analysis of the ND4 gene, the ATPase subunit-6 gene, the ribosomal
RT   RNA small-subunit gene, the ND6 gene, the COXIII gene, the ATPase subunit-8
RT   gene and six tRNA genes that correspond respectively to the tyrosine,
RT   lysine, glutamine, asparagine, isoleucine and tryptophan isoacceptors.";
RL   Curr. Genet. 28:553-559(1995).
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 membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
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DR   EMBL; Y18476; CAA77190.1; -; Genomic_DNA.
DR   EMBL; X88896; CAA61354.1; -; Genomic_DNA.
DR   PIR; T14246; T14246.
DR   AlphaFoldDB; Q36834; -.
DR   SMR; Q36834; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial 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:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR   InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   PANTHER; PTHR43507; PTHR43507; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   PRINTS; PR01437; NUOXDRDTASE4.
DR   TIGRFAMs; TIGR01972; NDH_I_M; 1.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; NAD; Respiratory chain;
KW   Translocase; Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..494
FT                   /note="NADH-ubiquinone oxidoreductase chain 4"
FT                   /id="PRO_0000118001"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        460..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   494 AA;  55768 MW;  1622F4BD8E4EA48F CRC64;
     MFFQNIMIYL FSLLLIPLIV YFLLIYIRLR YSNNSNNQIK TIGLTTLIIN LILSMIIFIL
     FDFSSKQFQL QLEEIYKISY FDLYLGIDGI SIYFLLLTTM IMPISLVANW NSIDSKNVLS
     FVIIILLLET LLLAVFLVLD ILLFYIFFES ILPPLFLLIG LFGSSDKVRA SFYLFLYTLL
     GSLFMLLSII TMSSIMGATA FDALSKANFS YITQLFLFYG IFISFAVKTP TIFLNTWLLK
     AHVESPLAGS VILAGIVWKL RWYGIFRLII PLLPKASMDY TYIVYVIGVI TIFYTSFSTL
     RTIAIKELIA YSSVSHAAVY LLSAFSNTIQ GIEGAIALGL AHGFVSSGLF ICVGGILYDR
     SSTRLITYYR GMAQLMPIFC ILFLYITLGN CGSPLTLNFI GEFMSLYGIF ERISVLGVLA
     STSIVFSAAY TIFMFNRIAF GGQFSSYFFN YVKDLSKREF ILLISLVVPA VFFGIYPAVI
     LDGLHYSVSG LIYN
 
 
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