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NU2M_MARPO
ID   NU2M_MARPO              Reviewed;         489 AA.
AC   P26846;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 2;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 2;
GN   Name=ND2; Synonyms=NAD2;
OS   Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=3197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1731062; DOI=10.1016/0022-2836(92)90708-r;
RA   Oda K., Yamato K., Ohta E., Nakamura Y., Takemura M., Nozato N., Akashi K.,
RA   Kanegae T., Ogura Y., Kohchi T., Ohyama K.;
RT   "Gene organization deduced from the complete sequence of liverwort
RT   Marchantia polymorpha mitochondrial DNA. A primitive form of plant
RT   mitochondrial genome.";
RL   J. Mol. Biol. 223:1-7(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8483448; DOI=10.1007/bf00279437;
RA   Nozato N., Oda K., Yamato K., Ohta E., Takemura M., Akashi K., Fukuzawa H.,
RA   Ohyama K.;
RT   "Cotranscriptional expression of mitochondrial genes for subunits of NADH
RT   dehydrogenase, nad5, nad4, nad2, in Marchantia polymorpha.";
RL   Mol. Gen. Genet. 237:343-350(1993).
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; Multi-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000305}.
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DR   EMBL; M68929; AAC09399.1; -; Genomic_DNA.
DR   PIR; S25943; S25943.
DR   RefSeq; NP_054402.1; NC_001660.1.
DR   AlphaFoldDB; P26846; -.
DR   SMR; P26846; -.
DR   GeneID; 2702662; -.
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:0009536; C:plastid; IEA:UniProt.
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   HAMAP; MF_00445; NDH1_NuoN_1; 1.
DR   InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   TIGRFAMs; TIGR01770; NDH_I_N; 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..489
FT                   /note="NADH-ubiquinone oxidoreductase chain 2"
FT                   /id="PRO_0000117605"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        459..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   489 AA;  54592 MW;  E5773CC5A929365A CRC64;
     MFEHDFLALF PEIFLINATI ILLIYGVVFS TSKKYDYPPL VRNVGWLGLL SVLITILLVA
     VGSPLAVANL VYNNLIIDNF TYFCQIFLLL STASTMVMCL DYFKQESLNA FESIVLILLS
     TCSMLFMISA YDLIAMYLAI ELQSLCFYVI AASKRDSEFS TEAGLKYFIL GAFSSGILLF
     GCSMIYGFTG VTNFEELAKI FTGYEITLFG AQSSGIFMGI LFIAVGFLFK ITAVPFHMWA
     PDVYEGSPTI VTAFFSIAPK ISILANMLRV FIYSFYDPTW QQLFFFCSIA SMILGALAAM
     AQNKVKRLLA YSSIGHVGYL LIGFSCGTIE GIQSLLIGIF IYVLMTVNVF AIVLALRQNR
     FKYIADLGAL AKTNPILAIT LSITMFSYAG IPPLAGFCSK FYLFFAALGC GAYLLALIGV
     VTSVISCFYY IRFVKIMYFD TPKTWVLYKP MDREKSLLLA ITVFFITFFF LYPSPLFLVT
     HQMALCLCL
 
 
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