NU2M_ANOGA
ID NU2M_ANOGA Reviewed; 341 AA.
AC P34848;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 2;
GN Name=mt:ND2; Synonyms=ND2;
OS Anopheles gambiae (African malaria mosquito).
OG Mitochondrion.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G3;
RX PubMed=9087549; DOI=10.1111/j.1365-2583.1993.tb00131.x;
RA Beard C.B., Hamm D.M., Collins F.H.;
RT "The mitochondrial genome of the mosquito Anopheles gambiae: DNA sequence,
RT genome organization, and comparisons with mitochondrial sequences of other
RT insects.";
RL Insect Mol. Biol. 2:103-124(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; L20934; AAD12190.1; -; Genomic_DNA.
DR PIR; T09800; T09800.
DR RefSeq; NP_008069.1; NC_002084.1.
DR AlphaFoldDB; P34848; -.
DR SMR; P34848; -.
DR STRING; 7165.AGAP028360-PA; -.
DR GeneID; 1267413; -.
DR KEGG; aga:ND2; -.
DR CTD; 4536; -.
DR VEuPathDB; VectorBase:AGAP028360; -.
DR eggNOG; KOG4668; Eukaryota.
DR HOGENOM; CLU_007100_1_3_1; -.
DR InParanoid; P34848; -.
DR OMA; HFWVPEV; -.
DR OrthoDB; 1153818at2759; -.
DR Proteomes; UP000007062; Mitochondrion.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
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..341
FT /note="NADH-ubiquinone oxidoreductase chain 2"
FT /id="PRO_0000117548"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 341 AA; 39469 MW; D95DC644E59485DF CRC64;
MKKISNNIFL IMLIFGTLVT ISSNSWLGAW MGLEINLLSF IPLMNDNKKN LLTSESSLKY
FLTQAFASSI LLFAIIMLMF LYNNNLSLYN SFNEILILST LLLKSGAAPF HFWFPEVMEG
LSWVNGLILM TWQKIAPLML ISYNFIYNFF MISIILSMLI GSLGGLNQTS IRKLMAFSSI
NHLGWMLLAM MNNEMLWMTY FLMYSLLSFS IVLMFNNFKL FYFNQIFNLS MMNPIIKLLI
FLNLLSLGGL PPFLGFLPKW LVIQNLTAMN QLFILTISVC LTLITLYFYL RLSYSIFMLN
YQKNSWMLKN NFNNKMSSIS LIFNFISIGG LVMISMIYII M