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NU3M_PHOVI
ID   NU3M_PHOVI              Reviewed;         115 AA.
AC   Q00541; Q08H12;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 3 {ECO:0000250|UniProtKB:P03897};
DE            EC=7.1.1.2 {ECO:0000250|UniProtKB:P03897};
DE   AltName: Full=NADH dehydrogenase subunit 3;
GN   Name=MT-ND3 {ECO:0000250|UniProtKB:P03897}; Synonyms=MTND3, NADH3, ND3;
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).
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. Essential for the catalytic activity of complex I.
CC       {ECO:0000250|UniProtKB:P03897}.
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:P03897};
CC   -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC       I) which is composed of 45 different subunits. Interacts with TMEM186.
CC       Interacts with TMEM242 (By similarity). {ECO:0000250|UniProtKB:P03897}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P03898}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 3 family. {ECO:0000305}.
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DR   EMBL; X63726; CAA45264.1; -; Genomic_DNA.
DR   EMBL; AM181032; CAJ57086.1; -; Genomic_DNA.
DR   PIR; S26158; S26158.
DR   RefSeq; NP_006935.1; NC_001325.1.
DR   AlphaFoldDB; Q00541; -.
DR   SMR; Q00541; -.
DR   GeneID; 807651; -.
DR   CTD; 4537; -.
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   Gene3D; 1.20.58.1610; -; 1.
DR   InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3.
DR   InterPro; IPR038430; NDAH_ubi_oxred_su3_sf.
DR   PANTHER; PTHR11058; PTHR11058; 1.
DR   Pfam; PF00507; Oxidored_q4; 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..115
FT                   /note="NADH-ubiquinone oxidoreductase chain 3"
FT                   /id="PRO_0000117802"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   115 AA;  12911 MW;  AD9625E82F7E1964 CRC64;
     MNMALTLFTN TALASLLVLI AFWLPQLNTY SEKASPYECG FDPMGSARLP FSMKFFLVAI
     TFLLFDLEIA LLLPLPWASH TDNLTTMLTM ALLLISLLAA SLAYEWTEKG LEWTE
 
 
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