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NU4LM_PUSHI
ID   NU4LM_PUSHI             Reviewed;          98 AA.
AC   Q08GV9; Q679A6;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 4L;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 4L;
GN   Name=MT-ND4L; Synonyms=MTND4L, NADH4L, ND4L;
OS   Pusa hispida (Ringed seal) (Phoca hispida).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Phocidae; Pusa.
OX   NCBI_TaxID=9718;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15336671; DOI=10.1016/j.ympev.2004.06.006;
RA   Davis C.S., Delisle I., Stirling I., Siniff D.B., Strobeck C.;
RT   "A phylogeny of the extant Phocidae inferred from complete mitochondrial
RT   DNA coding regions.";
RL   Mol. Phylogenet. Evol. 33:363-377(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16815048; DOI=10.1016/j.ympev.2006.05.022;
RA   Arnason U., Gullberg A., Janke A., Kullberg M., Lehman N., Petrov E.A.,
RA   Vainola R.;
RT   "Pinniped phylogeny and a new hypothesis for their origin and dispersal.";
RL   Mol. Phylogenet. Evol. 41:345-354(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. {ECO:0000250|UniProtKB:P03902}.
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   -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC       I) which is composed of 45 different subunits.
CC       {ECO:0000250|UniProtKB:P03902}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P03902}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 4L family. {ECO:0000305}.
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DR   EMBL; AM181036; CAJ57139.1; -; Genomic_DNA.
DR   EMBL; AY377238; AAQ93777.1; -; Genomic_DNA.
DR   RefSeq; YP_778924.1; NC_008433.1.
DR   AlphaFoldDB; Q08GV9; -.
DR   SMR; Q08GV9; -.
DR   GeneID; 4355912; -.
DR   CTD; 4539; -.
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; IEA:UniProtKB-EC.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K.
DR   InterPro; IPR039428; NUOK/Mnh_C1-like.
DR   PANTHER; PTHR11434; PTHR11434; 1.
DR   Pfam; PF00420; Oxidored_q2; 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..98
FT                   /note="NADH-ubiquinone oxidoreductase chain 4L"
FT                   /id="PRO_0000275094"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        45
FT                   /note="T -> A (in Ref. 1; AAQ93777)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        76
FT                   /note="L -> S (in Ref. 1; AAQ93777)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   98 AA;  10907 MW;  80C66AE2B033B52C CRC64;
     MSMVYANIFL AFIMSLMGLL MYRSHLMSSL LCLEGMMLSL FVMMTVTILN NHFTLANMAP
     IILLVFAACE AALGLLLLVM VSNTYGTDYV QNLNLLQC
 
 
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