NU5M_PHOVI
ID NU5M_PHOVI Reviewed; 609 AA.
AC Q00542;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 5;
GN Name=MT-ND5; Synonyms=MTND5, NADH5, ND5;
OS Phoca vitulina (Harbor seal).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Phocidae; Phoca.
OX NCBI_TaxID=9720;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1593642; DOI=10.1007/bf00160463;
RA Arnason U., Johnsson E.;
RT "The complete mitochondrial DNA sequence of the harbor seal, Phoca
RT vitulina.";
RL J. Mol. Evol. 34:493-505(1992).
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 {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR EMBL; X63726; CAA45267.1; -; Genomic_DNA.
DR PIR; S26161; S26161.
DR RefSeq; NP_006938.1; NC_001325.1.
DR AlphaFoldDB; Q00542; -.
DR SMR; Q00542; -.
DR GeneID; 807656; -.
DR CTD; 4540; -.
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:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
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..609
FT /note="NADH-ubiquinone oxidoreductase chain 5"
FT /id="PRO_0000118131"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 609 AA; 68666 MW; 3BF5ED46AEF657EA CRC64;
MKVINLFASS IITTLSMLTL PIVLTSTSIY KNKLYPQYVK TTISYAFMIS MIPTTMFIYS
GQEMIISNWH WMTIQTMKLT LSFKLDHFSM IFVPVALFVT WSIMEFSMWY MHSDPFINRF
FKYLLMFLIT MMILVTANNL FQLFIGWEGV GIMSFLLIGW WHGRTDANTA ALQAVLYNRI
GDVGFIMAMA WFLINLNTWE LQQIFISHHN NLNMPLMGLL LAATGKSAQF GLHPWLPSAM
EGPTPVSALL HSSTMVVAGV FLLIRFHPLM EHNTMMQTTT LCLGAITTLF TAICALTQND
IKKIIAFSTS SQLGLMIVTI GINQPHLAFL HICTHAFFKA MLFMCSGSII HNLNDEQDIR
KMGGLYKVLP FTTTSLIVGS LALTGMPFLT GFYSKDLIIE TANTSYTNAW ALLLTLVATS
MTAAYSTRIM FFTLLGQPRF NPMITINENS PLLINSIKRL LLGSIFAGYL ISYNITPTST
PQMTMPYYLK LTALTVTLLG FILALELNLT SQSLKLKYPS NLFKFSSLLG YFPTIIHRYM
PMVNLSASQK LASTLLDAIW LESALPKSIS YFHMKSSVTI SNQKGLIKLY FLSFIITLIL
ALMMINSHE