ID A0A251SWA3_HELAN Unreviewed; 428 AA.
AC A0A251SWA3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Putative NAD(P)H-quinone oxidoreductase subunit 2 A protein {ECO:0000313|EMBL:OTG02752.1};
GN Name=NU2C1 {ECO:0000313|EMBL:OTG02752.1};
GN ORFNames=HannXRQ_Chr13g0416581 {ECO:0000313|EMBL:OTG02752.1};
OS Helianthus annuus (Common sunflower).
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:OTG02752.1, 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) 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.
CC {ECO:0000256|ARBA:ARBA00003257}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CM007902; OTG02752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251SWA3; -.
DR STRING; 4232.A0A251SWA3; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr09g0379911; CDS:HanXRQr2_Chr09g0379911.1; HanXRQr2_Chr09g0379911.
DR Gramene; mRNA:HanXRQr2_Chr09g0379911; CDS:HanXRQr2_Chr09g0379911.1; HanXRQr2_Chr09g0379911.
DR InParanoid; A0A251SWA3; -.
DR Proteomes; UP000215914; Chromosome 13.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009579; C:thylakoid; IEA:UniProtKB-KW.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR045693; Ndh2_N.
DR PANTHER; PTHR22773:SF116; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 2 A, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR22773; NADH DEHYDROGENASE; 1.
DR Pfam; PF19530; Ndh2_N; 1.
DR Pfam; PF00361; Proton_antipo_M; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000215914};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 266..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..82
FT /note="NAD(P)H-quinone oxidoreductase subunit 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19530"
FT DOMAIN 111..224
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 227..360
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 428 AA; 47425 MW; 773B2D580DFFEB5E CRC64;
MYPNFGLILL LMIDSTSDQK DIPWLYFISS TSLVMSITAL LFRWREEPMI SFSGNFQTNN
FNEIFQFLIL LCSTLCIPLS VEYIECTEMA ITEFLLFILT ATIGGMFLCG ANDLITIFVA
PECFSLCSYL LSGYTKKDVR SNEATMKYLL MGGASSSILV HGFSWLYGSS GGEIELQEIV
NGLINTQMYN SPGISIALIF ITVGIGFKLS PAPSHQWTPD VYEGHDIGNL IAITQTSMKR
MLAYSSIGQI GYVIIGIIVG DSNDGYASMI TYMLFYISMN LGTFACIVLF GLRTGTENIR
DYAGLYTKDP FLALSLALCL LSLGGLPPLA GFFGKLYLFW CGWQAGLYLL VLIGLLTSVV
SIYYYLKIIK LLMTGRNQEI TPHVRNYRRS PLRSNNSIEL SMIVCVIAST IPGISMNPII
AIAQDTLF
//
