NU4M_CANLU
ID NU4M_CANLU Reviewed; 459 AA.
AC Q3L6Y5; Q1HKA7; Q1HKE6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4;
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:P03905};
DE AltName: Full=NADH dehydrogenase subunit 4;
GN Name=MT-ND4; Synonyms=MTND4, NADH4, ND4;
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-29; LEU-40 AND SER-425.
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:P03905}.
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:P03905};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits.
CC {ECO:0000250|UniProtKB:P03910}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P03910}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
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DR EMBL; AY598503; AAU00449.1; -; Genomic_DNA.
DR EMBL; DQ480503; ABE48164.1; -; Genomic_DNA.
DR EMBL; DQ480504; ABE48177.1; -; Genomic_DNA.
DR EMBL; DQ480505; ABE48190.1; -; Genomic_DNA.
DR EMBL; DQ480506; ABE48203.1; -; Genomic_DNA.
DR EMBL; DQ480508; ABE48229.1; -; Genomic_DNA.
DR EMBL; DQ480507; ABE48216.1; -; Genomic_DNA.
DR RefSeq; YP_626737.1; NC_008092.1.
DR AlphaFoldDB; Q3L6Y5; -.
DR SMR; Q3L6Y5; -.
DR GeneID; 4097760; -.
DR CTD; 4538; -.
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; IPR000260; NADH4_N.
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; PF01059; Oxidored_q5_N; 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; Mitochondrion inner membrane;
KW NAD; Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..459
FT /note="NADH-ubiquinone oxidoreductase chain 4"
FT /id="PRO_0000269896"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 29
FT /note="T -> A"
FT /evidence="ECO:0000269|PubMed:16809672"
FT VARIANT 40
FT /note="F -> L"
FT /evidence="ECO:0000269|PubMed:16809672"
FT VARIANT 425
FT /note="N -> S"
FT /evidence="ECO:0000269|PubMed:16809672"
SQ SEQUENCE 459 AA; 52083 MW; 7729549DB117E3DC CRC64;
MLKIIIPTIM LIPLTWMSKP NMIWINTTTY GLLISLISLF YLNQPNDNTL NSSLMFFSDS
LSAPLLALTT WLLPLMLMAS QHHLSKEPLT RKKLYISMLI LLQLFLIMTF TASELIFFYI
LFEATLIPTL IIITRWGNQT ERLNAGLYFL FYTLMGSLPL LVALLYIHNF MGSLNFLMIQ
YWIQPLPNSW SNIFLWLACM MAFMVKMPLY GLHLWLPKAH VEAPIAGSMV LAAVLLKLGG
YGMMRITTLL NPLTNFMAYP FMMLSLWGMI MTSSICLRQT DLKSLIAYSS VSHMALVIVA
VLIQTPWSYM GATALMIAHG LTSSMLFCLA NSNYERIHSR TMILARGLQT LLPLMAAWWL
LASLTNLALP PTINLIGELF VVMSSFSWSN ITIILMGINI TITALYSLYM LITTQRGKYS
HHIKNIKPSF TRENALMTLH LLPLLLLSLN PKIILGPIY
