NU5M_ANOAR
ID NU5M_ANOAR Reviewed; 384 AA.
AC P51899; O20867; O20868; O20869; O20872; O21815;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 5;
DE Flags: Fragment;
GN Name=ND5;
OS Anopheles arabiensis (Mosquito).
OG Mitochondrion.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7173;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-265.
RC STRAIN=Arzag, and GMAL;
RX PubMed=8041714; DOI=10.1073/pnas.91.15.6885;
RA Besansky N.J., Powell J.R., Caccone A., Hamm D.M., Scott J.A.,
RA Collins F.H.;
RT "Molecular phylogeny of the Anopheles gambiae complex suggests genetic
RT introgression between principal malaria vectors.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6885-6888(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-384, AND VARIANTS.
RX PubMed=9409838; DOI=10.1093/genetics/147.4.1817;
RA Besansky N.J., Lehmann T., Fahey G.T., Fontenille D., Braack L.E.O.,
RA Hawley W.A., Collins F.H.;
RT "Patterns of mitochondrial variation within and between African malaria
RT vectors, Anopheles gambiae and An. arabiensis, suggest extensive gene
RT flow.";
RL Genetics 147:1817-1828(1997).
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 {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR EMBL; U10124; AAB51631.1; -; Genomic_DNA.
DR EMBL; U10125; AAB51633.1; -; Genomic_DNA.
DR EMBL; AF020965; AAB81767.1; -; Genomic_DNA.
DR EMBL; AF020966; AAB81768.1; -; Genomic_DNA.
DR EMBL; AF020969; AAB81771.1; -; Genomic_DNA.
DR EMBL; AF020972; AAB81774.1; -; Genomic_DNA.
DR EMBL; AF020974; AAB81776.1; -; Genomic_DNA.
DR EMBL; AF020975; AAB81777.1; -; Genomic_DNA.
DR EMBL; AF020976; AAB81778.1; -; Genomic_DNA.
DR EMBL; AF020977; AAB81779.1; -; Genomic_DNA.
DR EMBL; AF020978; AAB81780.1; -; Genomic_DNA.
DR EMBL; AF020979; AAB81781.1; -; Genomic_DNA.
DR EMBL; AF020981; AAB81783.1; -; Genomic_DNA.
DR EMBL; AF020982; AAB81784.1; -; Genomic_DNA.
DR EMBL; AF020983; AAB81785.1; -; Genomic_DNA.
DR EMBL; AF020984; AAB81786.1; -; Genomic_DNA.
DR EMBL; AF020985; AAB81787.1; -; Genomic_DNA.
DR EMBL; AF020986; AAB81788.1; -; Genomic_DNA.
DR EMBL; AF020987; AAB81789.1; -; Genomic_DNA.
DR EMBL; AF020990; AAB81792.1; -; Genomic_DNA.
DR EMBL; AF020994; AAB81796.1; -; Genomic_DNA.
DR EMBL; AF020995; AAB81797.1; -; Genomic_DNA.
DR EMBL; AF020996; AAB81798.1; -; Genomic_DNA.
DR EMBL; AF020997; AAB81799.1; -; Genomic_DNA.
DR EMBL; AF021000; AAB81802.1; -; Genomic_DNA.
DR EMBL; AF021001; AAB81803.1; -; Genomic_DNA.
DR EMBL; AF021004; AAB81806.1; -; Genomic_DNA.
DR EMBL; AF021005; AAB81807.1; -; Genomic_DNA.
DR EMBL; AF021006; AAB81808.1; -; Genomic_DNA.
DR EMBL; AF021007; AAB81809.1; -; Genomic_DNA.
DR EMBL; AF021008; AAB81810.1; -; Genomic_DNA.
DR EMBL; AF021009; AAB81811.1; -; Genomic_DNA.
DR EMBL; AF021010; AAB81812.1; -; Genomic_DNA.
DR PIR; T12176; T12176.
DR PIR; T12178; T12178.
DR PIR; T12179; T12179.
DR PIR; T30246; T30246.
DR AlphaFoldDB; P51899; -.
DR SMR; P51899; -.
DR VEuPathDB; VectorBase:AARA21_001647; -.
DR Proteomes; UP000075840; Unassembled WGS sequence.
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 GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR PANTHER; PTHR42829; PTHR42829; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_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..>384
FT /note="NADH-ubiquinone oxidoreductase chain 5"
FT /id="PRO_0000118053"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 5
FT /note="V -> I (in strain: Arzag)"
FT VARIANT 32
FT /note="M -> T (in strain: Arzag)"
FT VARIANT 188
FT /note="G -> S (in haplotype 19)"
FT VARIANT 239
FT /note="D -> N (in haplotype 10)"
FT VARIANT 253
FT /note="V -> I (in haplotype 15)"
FT VARIANT 377..378
FT /note="VN -> MK (in haplotype 26)"
FT NON_TER 384
SQ SEQUENCE 384 AA; 43646 MW; 464692B6AD5E6297 CRC64;
MNYLVNYCKI SFYFLMSISL SLFLISLKFL LMDLVYFIEW EILSLQSMSI VMTFLFDWMS
LMFMSFVLLI SSLVIFYSNQ YMEEDYNINR FILLVLMFVM SMMMLIISPN LISILLGWDG
LGLVSYCLVI YFQNVKSYNA GMLTALSNRI GDVALLLAIA WMLNYGSWNY IFYLDMMKNN
IEMMIIGGLV MLAAMTKSAQ IPFSSWLPAA MAAPTPVSAL VHSSTLVTAG VYLLIRFNDV
LMNWWMAQFL LLVSGLTMFM AGLGANFEFD LKKIIALSTL SQLGLMMSIL SMGFYKLAFF
HLLTHALFKA LLFMCAGSII HNMKNSQDIR MMGSLSMSMP LTCSCFNVAN LALCGMPFLA
GFYSKDLILE MVMLSYVNVF SFFL
