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NU5M_CANLU
ID   NU5M_CANLU              Reviewed;         606 AA.
AC   Q1HK80; Q1HKA6; Q1HKD2; Q1HKE5; Q3L6Y3;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 57.
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 (Gray wolf).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15964215; DOI=10.1016/j.ympev.2005.04.025;
RA   Delisle I., Strobeck C.;
RT   "A phylogeny of the Caniformia (order Carnivora) based on 12 complete
RT   protein-coding mitochondrial genes.";
RL   Mol. Phylogenet. Evol. 37:192-201(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-77; PHE-77; SER-208;
RP   LEU-209; ILE-371; VAL-375; HIS-442; MET-489 AND MET-495.
RX   PubMed=16809672; DOI=10.1101/gr.5117706;
RA   Bjornerfeldt S., Webster M.T., Vila C.;
RT   "Relaxation of selective constraint on dog mitochondrial DNA following
RT   domestication.";
RL   Genome Res. 16:990-994(2006).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU00451.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY598505; AAU00451.1; ALT_INIT; Genomic_DNA.
DR   EMBL; DQ480503; ABE48165.1; -; Genomic_DNA.
DR   EMBL; DQ480504; ABE48178.1; -; Genomic_DNA.
DR   EMBL; DQ480505; ABE48191.1; -; Genomic_DNA.
DR   EMBL; DQ480506; ABE48204.1; -; Genomic_DNA.
DR   EMBL; DQ480507; ABE48217.1; -; Genomic_DNA.
DR   EMBL; DQ480508; ABE48230.1; -; Genomic_DNA.
DR   RefSeq; YP_626738.1; NC_008092.1.
DR   AlphaFoldDB; Q1HK80; -.
DR   SMR; Q1HK80; -.
DR   GeneID; 4097761; -.
DR   CTD; 4540; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
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; Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   CHAIN           1..606
FT                   /note="NADH-ubiquinone oxidoreductase chain 5"
FT                   /id="PRO_0000269897"
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        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   VARIANT         77
FT                   /note="S -> A"
FT                   /evidence="ECO:0000269|PubMed:16809672"
FT   VARIANT         77
FT                   /note="S -> F"
FT                   /evidence="ECO:0000269|PubMed:16809672"
FT   VARIANT         208
FT                   /note="N -> S"
FT                   /evidence="ECO:0000269|PubMed:16809672"
FT   VARIANT         209
FT                   /note="F -> L"
FT                   /evidence="ECO:0000269|PubMed:16809672"
FT   VARIANT         371
FT                   /note="T -> I"
FT                   /evidence="ECO:0000269|PubMed:16809672"
FT   VARIANT         375
FT                   /note="I -> V"
FT                   /evidence="ECO:0000269|PubMed:16809672"
FT   VARIANT         442
FT                   /note="L -> H"
FT                   /evidence="ECO:0000269|PubMed:16809672"
FT   VARIANT         489
FT                   /note="T -> M"
FT                   /evidence="ECO:0000269|PubMed:16809672"
FT   VARIANT         495
FT                   /note="I -> M"
FT                   /evidence="ECO:0000269|PubMed:16809672"
SQ   SEQUENCE   606 AA;  68402 MW;  7628DD4B5E5C4350 CRC64;
     MNMFSSCMIT ALVILTLPII MSSTKLYKNK LYPYYVKTAT SYAFMISMIP TMMFIYSGQE
     TIISNWHWMT IQTMKLSMSF KLDYFSMIFV PVALFVTWSI MEFSMWYMHS DPYINRFFKY
     LLLFLITMMV LVTANNMFQL FIGWEGVGIM SFLLIGWWYG RTDANTAALQ AVLYNRIGDV
     GFIMTMAWFL LNLNTWDLQQ IFITTNDNFN LPLLGLLLAA TGKSAQFGLH PWLPSAMEGP
     TPVSALLHSS TMVVAGVFLL IRFHPLMEHN QTIQTLTLCL GAITTLFTAI CALTQNDIKK
     IVAFSTSSQL GLMMVTIGIN QPYLAFLHIC THAFFKAMLF MCSGSIIHSL 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
     ILNYHG
 
 
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