ID A0A1Y3C029_HELAN Unreviewed; 665 AA.
AC A0A1Y3C029;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5 {ECO:0000256|RuleBase:RU003404};
DE EC=7.1.1.2 {ECO:0000256|RuleBase:RU003404};
GN ORFNames=HannXRQ_MTg0579361 {ECO:0000313|EMBL:OTF84715.1};
OS Helianthus annuus (Common sunflower).
OG Mitochondrion {ECO:0000313|EMBL:OTF84715.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232 {ECO:0000313|EMBL:OTF84715.1, ECO:0000313|Proteomes:UP000215914};
RN [1] {ECO:0000313|Proteomes:UP000215914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RX PubMed=28538728; DOI=10.1038/nature22380;
RA Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA Vincourt P., Rieseberg L.H., Langlade N.B.;
RT "The sunflower genome provides insights into oil metabolism, flowering and
RT Asterid evolution.";
RL Nature 546:148-152(2017).
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:0000256|RuleBase:RU003404}.
CC -!- FUNCTION: This protein is one of the chains of the nonenzymatic
CC membrane component (F0) of mitochondrial ATPase.
CC {ECO:0000256|ARBA:ARBA00002351}.
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:0000256|RuleBase:RU003404};
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c. {ECO:0000256|ARBA:ARBA00011648}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ATPase C chain family.
CC {ECO:0000256|ARBA:ARBA00006704}.
CC -!- SIMILARITY: Belongs to the complex I subunit 5 family.
CC {ECO:0000256|ARBA:ARBA00008200, ECO:0000256|RuleBase:RU003404}.
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DR EMBL; CM007908; OTF84715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3C029; -.
DR STRING; 4232.A0A1Y3C029; -.
DR InParanoid; A0A1Y3C029; -.
DR OMA; LTMFMAG; -.
DR Proteomes; UP000215914; Mitochondrion.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0009579; C:thylakoid; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR CDD; cd18182; ATP-synt_Fo_c_ATP5G3; 1.
DR Gene3D; 1.20.20.10; F1F0 ATP synthase subunit C; 1.
DR HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR InterPro; IPR000454; ATP_synth_F0_csu.
DR InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR NCBIfam; TIGR01974; NDH_I_L; 1.
DR PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR PANTHER; PTHR42829:SF3; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR Pfam; PF00137; ATP-synt_C; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR PRINTS; PR01434; NADHDHGNASE5.
DR SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 3: Inferred from homology;
KW CF(0) {ECO:0000256|ARBA:ARBA00022547};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003404};
KW Mitochondrion {ECO:0000256|RuleBase:RU003404, ECO:0000313|EMBL:OTF84715.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003404};
KW Reference proteome {ECO:0000313|Proteomes:UP000215914};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003404};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU003404};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003404};
KW Ubiquinone {ECO:0000256|RuleBase:RU003404}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 61..87
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 214..237
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 258..281
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 395..413
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 433..452
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 464..486
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 524..541
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 561..580
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 600..621
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 641..663
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT DOMAIN 21..83
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
FT DOMAIN 250..296
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 314..602
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 665 AA; 72642 MW; B8F7A91E1FE699E8 CRC64;
MKKKKREEND QLEMLEGAKL IGAGAATIAS AGAAIGIGNV LSSSIHSVAR NPSLAKQSFG
YAILGFALTE AIASFAPMMA FLISSVFRSK NQRKKPPEAR GAVLKQKNGD KEEMIQIQEK
KSRIGSQVRR KEASPRKCSA PRFFCRWGLH LVTHSFGRAF LGRRSILNHR PLCHCLIFGC
LITLEIMYLL IIFLPLLGSS VAGFFGRFLG SEGTAIMTTT CVSFSSILSL IAFYEVAPGA
SACYLRIAPW ISSEMFDASW GFFGDLMLIV VTSISSLVHL YSISYMSEDP HSPRFMCYLS
IPTFFMPMLV TGDNSLQLFL GWEGVGLASY LLIHFWFTRL QADKAAIKAM LVNRVGDFGL
APGISGCFTL FQTVDFSTIF ACASVPRNSW ISRNMRLNAI TLICILLLIG AAGKSAQIGS
HTWSPDAMEG PTPVSALIHA ATMVTAGVFM IARCSPLFEY PPTALIVITF AGAMTSFLAA
TTGILQNDLK RVIAYSTCSQ LGYMIFACGI SNYSVSVFHL MNHAFFKALL FLSAGSVIHA
MSDEQDMRKM GGLASSFPFT YAMMLMGSLS LIGFPFPTGF YSKDVILELA YTKYTISGNF
AFWLGSVSVL FTSYYSFRSL FLTFLGPTNS FGRDILRCHD APIPMAIPLI LLALGSLFVG
YLAKV
//
