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NU2M_DICDI
ID   NU2M_DICDI              Reviewed;         488 AA.
AC   O21048;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 2;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 2;
GN   Name=nad2; ORFNames=DDB_G0294020;
OS   Dictyostelium discoideum (Slime mold).
OG   Mitochondrion.
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AX3;
RX   PubMed=9000384; DOI=10.1007/s002940050179;
RA   Ogawa S., Matsuo K., Angata K., Yanagisawa K., Tanaka Y.;
RT   "Group-I introns in the cytochrome c oxidase genes of Dictyostelium
RT   discoideum: two related ORFs in one loop of a group-I intron, a cox1/2
RT   hybrid gene and an unusually large cox3 gene.";
RL   Curr. Genet. 31:80-88(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX3;
RX   PubMed=10821186; DOI=10.1007/pl00008685;
RA   Ogawa S., Yoshino R., Angata K., Iwamoto M., Pi M., Kuroe K., Matsuo K.,
RA   Morio T., Urushihara H., Yanagisawa K., Tanaka Y.;
RT   "The mitochondrial DNA of Dictyostelium discoideum: complete sequence, gene
RT   content and genome organization.";
RL   Mol. Gen. Genet. 263:514-519(2000).
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; D16579; BAA21119.1; -; Genomic_DNA.
DR   EMBL; AB000109; BAA78052.1; -; Genomic_DNA.
DR   PIR; T43748; T43748.
DR   RefSeq; NP_050070.1; NC_000895.1.
DR   AlphaFoldDB; O21048; -.
DR   SMR; O21048; -.
DR   GeneID; 2193892; -.
DR   KEGG; ddi:DidioMp03; -.
DR   dictyBase; DDB_G0294020; nad2.
DR   InParanoid; O21048; -.
DR   OMA; FYIRVIV; -.
DR   PhylomeDB; O21048; -.
DR   PRO; PR:O21048; -.
DR   Proteomes; UP000002195; Mitochondrion.
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   InterPro; IPR001750; ND/Mrp_mem.
DR   Pfam; PF00361; Proton_antipo_M; 1.
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..488
FT                   /note="NADH-ubiquinone oxidoreductase chain 2"
FT                   /id="PRO_0000311824"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        412..434
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        460..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   488 AA;  54842 MW;  245A76F6DA125B01 CRC64;
     MMFLFENSIN MIKYSIYLVP LIIMILLSIS IKEDSNRMML LFKSLKLTII LILVLLTIEE
     AIYVKLNGHL IKTELITFVE YILLVVSYLI ISMFEEGVKE GRKTKITEEA LILMYSSLIG
     MLISMEAHNL ITLFLSLEIT SICFYILALN KNSRKVSIEG GLKYYIIGGI ASTIILLGIV
     SIYKNTGSLM YTDILVIGME RIGNYQVQMG IALIVLGLII KLGVAPFHGW LIDTYEGTGM
     LMTFYLTITQ KIVTIIVLIN LYKNLITYLN IEVINKGLLV LILVTLIVGT VGSLRQQKVI
     RFIAYSAIVN SALLILFFVG NNTEELIIYS IYYLINYIIG LAVLINIIIG VVKTKNGGNI
     EILSELKNIW LNNKVIGISL IIVLIYLAGL PPFTNFISKI ILILPLIVEG KIYITMIIFF
     LTVGIMIYYM NVVKIIIIDK KQEVGVETYK MTKGGSITNI VGGIIWIIIS QIYLDEIISI
     IKIIVAIN
 
 
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