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NU2M_LOXAF
ID   NU2M_LOXAF              Reviewed;         347 AA.
AC   Q9TA28; Q2I3G0;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000250|UniProtKB:P03891};
DE            EC=7.1.1.2 {ECO:0000250|UniProtKB:P03891};
DE   AltName: Full=NADH dehydrogenase subunit 2;
GN   Name=MT-ND2 {ECO:0000250|UniProtKB:P03891}; Synonyms=MTND2, NADH2, ND2;
OS   Loxodonta africana (African elephant).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RA   Hauf J., Waddell P.J., Chalwatzis N., Joger U., Zimmermann F.K.;
RT   "The complete mitochondrial genome sequence of the African elephant
RT   (Loxodonta africana), phylogenetic relationships of Proboscidea to other
RT   mammals and D-loop heteroplasmy.";
RL   Zoology 102:184-195(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RX   PubMed=16448217; DOI=10.1371/journal.pbio.0040073;
RA   Rogaev E.I., Moliaka Y.K., Malyarchuk B.A., Kondrashov F.A., Derenko M.V.,
RA   Chumakov I., Grigorenko A.P.;
RT   "Complete mitochondrial genome and phylogeny of Pleistocene mammoth
RT   Mammuthus primigenius.";
RL   PLoS Biol. 4:403-410(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:P03891}.
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:P03891};
CC   -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC       I) which is composed of 45 different subunits. Interacts with TMEM242
CC       (By similarity). {ECO:0000250|UniProtKB:P03891,
CC       ECO:0000250|UniProtKB:P03892}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P03892}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000305}.
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DR   EMBL; AJ224821; CAA12139.1; -; Genomic_DNA.
DR   EMBL; DQ316069; ABC17905.1; -; Genomic_DNA.
DR   PIR; T45551; T45551.
DR   RefSeq; NP_009280.1; NC_000934.1.
DR   AlphaFoldDB; Q9TA28; -.
DR   SMR; Q9TA28; -.
DR   STRING; 9785.ENSLAFP00000029492; -.
DR   Ensembl; ENSLAFT00000038044; ENSLAFP00000029492; ENSLAFG00000033278.
DR   GeneID; 808792; -.
DR   KEGG; lav:808792; -.
DR   CTD; 4536; -.
DR   eggNOG; KOG4668; Eukaryota.
DR   GeneTree; ENSGT00730000111348; -.
DR   HOGENOM; CLU_007100_1_3_1; -.
DR   InParanoid; Q9TA28; -.
DR   OMA; HFWVPEV; -.
DR   OrthoDB; 1153818at2759; -.
DR   TreeFam; TF343996; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:Ensembl.
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   GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR   InterPro; IPR010933; NADH_DH_su2_C.
DR   InterPro; IPR003917; NADH_UbQ_OxRdtase_chain2.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   Pfam; PF06444; NADH_dehy_S2_C; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   PRINTS; PR01436; NADHDHGNASE2.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   NAD; Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW   Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..347
FT                   /note="NADH-ubiquinone oxidoreductase chain 2"
FT                   /id="PRO_0000117602"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   347 AA;  39093 MW;  A2ADF1CC60F93BE4 CRC64;
     MNPLALSLIL TTLLAGTLIT MMSSHWLTAW MGLEMNMLTM IPILMKTTNP RSTEAATKYF
     MTQAMASMML MMALTINLMY SGQWSITKMT NPVASNMALM ALMTKLGSAP FHFWVPEVTQ
     GVELTPGMIL LTWQKLAPLS LLYQMATYTN TNLIYLSGLL SILIGGWGGL NQTQLRKILA
     YSSISHMGWM LIILPFNPTL TLLNLTIYIM LTLSIFMILT NTFTTSMSSL TLMWNKTPAM
     TIMLMTTLLS LGGLPPLSGF MPKWLMIHEL TKNNSIIMPL TMAIMALLNM YFYMRLIYYS
     SLTILPSTNN MKMTWRFTNT KHTMTLPTLI TLSNMLLPLT PMISMLE
 
 
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