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NU5M_CANLF
ID   NU5M_CANLF              Reviewed;         606 AA.
AC   Q9ZZ57; Q66QB1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 3.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 5;
DE            EC=7.1.1.2 {ECO:0000250|UniProtKB:P03915};
DE   AltName: Full=NADH dehydrogenase subunit 5;
GN   Name=MT-ND5; Synonyms=MTND5, NADH5, ND5;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Boxer {ECO:0000312|Proteomes:UP000002254};
RX   PubMed=9878232; DOI=10.1006/mpev.1998.0513;
RA   Kim K.S., Lee S.E., Jeong H.W., Ha J.H.;
RT   "The complete nucleotide sequence of the domestic dog (Canis familiaris)
RT   mitochondrial genome.";
RL   Mol. Phylogenet. Evol. 10:210-220(1998).
RN   [2]
RP   SEQUENCE REVISION TO 117; 134; 201; 401 AND 405.
RA   Kim K.S., Lee S.E., Jeong H.W., Jeong S.Y., Sohn H.S., Ha J.H.;
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Beagle;
RA   Zhu S., Xu Q., Chang H.;
RT   "The complete mitochondrial DNA sequence of the Beagle dog (Canis
RT   familiaris).";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC       NADH through the respiratory chain, using ubiquinone as an electron
CC       acceptor. Essential for the catalytic activity and assembly of complex
CC       I. {ECO:0000250|UniProtKB:P03915}.
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         Evidence={ECO:0000250|UniProtKB:P03915};
CC   -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC       I) which is composed of 45 different subunits.
CC       {ECO:0000250|UniProtKB:P03920}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P03920}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR   EMBL; U96639; AAD04773.2; -; Genomic_DNA.
DR   EMBL; AY729880; AAU12157.1; -; Genomic_DNA.
DR   PIR; T11503; T11503.
DR   RefSeq; NP_008481.4; NC_002008.4.
DR   AlphaFoldDB; Q9ZZ57; -.
DR   SMR; Q9ZZ57; -.
DR   STRING; 9612.ENSCAFP00000030319; -.
DR   PaxDb; Q9ZZ57; -.
DR   GeneID; 804484; -.
DR   KEGG; cfa:804484; -.
DR   CTD; 4540; -.
DR   eggNOG; KOG4668; Eukaryota.
DR   InParanoid; Q9ZZ57; -.
DR   OrthoDB; 526738at2759; -.
DR   Proteomes; UP000002254; Mitochondrion.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISS:UniProtKB.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR   InterPro; IPR010934; NADH_DH_su5_C.
DR   InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   InterPro; IPR003945; NU5C-like.
DR   InterPro; IPR001516; Proton_antipo_N.
DR   PANTHER; PTHR42829; PTHR42829; 1.
DR   Pfam; PF06455; NADH5_C; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   Pfam; PF00662; Proton_antipo_N; 1.
DR   TIGRFAMs; TIGR01974; NDH_I_L; 1.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   NAD; Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW   Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..606
FT                   /note="NADH-ubiquinone oxidoreductase chain 5"
FT                   /id="PRO_0000118073"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        457..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        488..508
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        582..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        63
FT                   /note="F -> I (in Ref. 1; AAD04773)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        83
FT                   /note="N -> D (in Ref. 1; AAD04773)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        300
FT                   /note="E -> K (in Ref. 1; AAD04773)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303
FT                   /note="S -> A (in Ref. 1; AAD04773)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        335
FT                   /note="C -> F (in Ref. 1; AAD04773)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        495
FT                   /note="I -> T (in Ref. 1; AAD04773)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        508
FT                   /note="T -> S (in Ref. 1; AAD04773)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        606
FT                   /note="E -> G (in Ref. 1; AAD04773)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   606 AA;  68465 MW;  51D20BE07765702A CRC64;
     MNMFSSCMIT ALVILTLPII MSSTKLYKNK LYPYYVKTAT SYAFMISMIP TMMFIYSGQE
     TIFSNWHWMT IQTMKLSMSF KLNYFSMIFV PVALFVTWSI MEFSMWYMHS DPYINRFFKY
     LLLFLITMMV LVTANNMFQL FIGWEGVGIM SFLLIGWWYG RTDANTAALQ AVLYNRIGDV
     GFIMTMAWFL LNLNTWDLQQ IFITTNDNFN LPLLGLLLAA TGKSAQFGLH PWLPSAMEGP
     TPVSALLHSS TMVVAGVFLL IRFHPLMEHN QTIQTLTLCL GAITTLFTAI CALTQNDIKE
     IVSFSTSSQL GLMMVTIGIN QPYLAFLHIC THAFCKAMLF MCSGSVIHSL NDEQDIRKMG
     GLFKVLPFTT TSLIIGSLAL TGMPFLTGFY SKDLIIESAN TSNTNAWALL ITLVATSLTA
     AYSTRIMFFA LLGQPRFSPM ILINENNPLL INSIKRLLIG SVFAGYIISH SITPTTIPQM
     TMPHYLKMTA LAVTILGFIL ALELNLTTQG LKFNYPSNYF KFSSLLGYYP TIMHRLTPKT
     SLTISQKSAS MLLDSIWLEN ILPKSISYFQ MKSSTLISNQ KGLIKLYFLS FMLTMILSLL
     ILNYHE
 
 
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