NOXC_DICDI
ID NOXC_DICDI Reviewed; 1142 AA.
AC Q54F44; Q86MX0;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Superoxide-generating NADPH oxidase heavy chain subunit C;
DE EC=1.-.-.-;
DE AltName: Full=NADPH oxidase C;
DE AltName: Full=Superoxide-generating NADPH oxidase flavocytochrome C;
GN Name=noxC; ORFNames=DDB_G0291117;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15950752; DOI=10.1016/j.bbamcr.2005.02.004;
RA Lardy B., Bof M., Aubry L., Paclet M.H., Morel F., Satre M., Klein G.;
RT "NADPH oxidase homologs are required for normal cell differentiation and
RT morphogenesis in Dictyostelium discoideum.";
RL Biochim. Biophys. Acta 1744:199-212(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Critical component of the membrane-bound oxidase that
CC generates superoxide. It is the terminal component of a respiratory
CC chain that transfers single electrons from cytoplasmic NADPH across the
CC plasma membrane to molecular oxygen on the exterior (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- SUBUNIT: Composed of a heavy chain and a light chain. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed during development. Low expression
CC starts at 8 hours development, and increases sharply in fruiting
CC bodies. {ECO:0000269|PubMed:15950752}.
CC -!- DISRUPTION PHENOTYPE: Prevents formation of fruiting bodies.
CC {ECO:0000269|PubMed:15950752}.
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DR EMBL; AY224390; AAO72635.1; -; Genomic_DNA.
DR EMBL; AAFI02000175; EAL61883.1; -; Genomic_DNA.
DR RefSeq; XP_635387.1; XM_630295.1.
DR AlphaFoldDB; Q54F44; -.
DR SMR; Q54F44; -.
DR STRING; 44689.DDB0191391; -.
DR PaxDb; Q54F44; -.
DR ABCD; Q54F44; 4 sequenced antibodies.
DR EnsemblProtists; EAL61883; EAL61883; DDB_G0291117.
DR GeneID; 8627994; -.
DR KEGG; ddi:DDB_G0291117; -.
DR dictyBase; DDB_G0291117; noxC.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_277635_0_0_1; -.
DR InParanoid; Q54F44; -.
DR PhylomeDB; Q54F44; -.
DR Reactome; R-DDI-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-DDI-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR Reactome; R-DDI-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q54F44; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; ISS:dictyBase.
DR GO; GO:0043020; C:NADPH oxidase complex; ISS:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:dictyBase.
DR GO; GO:0020037; F:heme binding; ISS:dictyBase.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; ISS:dictyBase.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IGI:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR GO; GO:0042554; P:superoxide anion generation; ISS:dictyBase.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00466; GP91PHOX.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW Calcium; Coiled coil; Electron transport; FAD; Flavoprotein; Heme; Iron;
KW Membrane; Metal-binding; NADP; Oxidoreductase; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1142
FT /note="Superoxide-generating NADPH oxidase heavy chain
FT subunit C"
FT /id="PRO_0000361529"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 667..687
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 720..740
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 754..774
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 462..497
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 506..541
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 622..766
FT /note="Ferric oxidoreductase"
FT DOMAIN 794..942
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 135..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 172..246
FT /evidence="ECO:0000255"
FT BINDING 519
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 521
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 523
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 525
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 530
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 665
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 679
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 755
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 768
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 849..855
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT CONFLICT 224..225
FT /note="NN -> II (in Ref. 1; AAO72635)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1142 AA; 132499 MW; EE780670085977A9 CRC64;
MEKQKNISIK KFANPLSFPH EFRTNLHKST FLDASLLELP NISVDKTKNE NNFSITDKIL
MESLKENEFK IREFIKNQES GNRVLMIDKN SLKELFNIND NQALDLIFNQ YVQSTRPNLI
RKSSNSSLNI DLKKEIKKKT KKSRKSFSRN SKLNNNDSKI DDKNDNYIDK INDINNFNSD
IEEIFKKKKE IENTLKIPIG GNSFPIPVEF NNNNNNNNNN NNNNNNNYNN NIDNNNNNNN
NNNNNNINNC NNNNINNDNN NNNNNDNDNN NINTVDNHDD DIINNSNNFN KNEYPSSNIS
PISPKSSISS FPTNLNNSIN NTGSMVSDSL SSCRNSISSS SIDSSVASIP ITIQSIDFED
KNIKSDQFKI ISKSNIENTI ETNPIPPFNQ TNNQCEVQLQ SHSLPTILKQ PHIYKSKSFS
SSINSNSKIK KIKKSRSFEI ESKINLFDVI NHIYLNLSKV GSEEQKITSV FKLYDIYDKG
FISRDDLKEV LNYRTKQNGL KFQDFTMESL IDHIFQQFDK NMDGYIDFEE FKSELTINNE
NKVKEKEENT NYNFKEENIG IYTEKESFHS LKRYLKIEGS KLFFISLFFI INSILVITSF
LNVHANNKRA IELFGPGVYI TRIAAQLIEF NAAIILMTMC KQLFTMIRNT KFKFLFPVDK
YMTFHKLIGY TLIIASFLHT IGWIVGMAVA TGKPDNIFYD CLAPHFKFRP TVWEMIFNSL
PGVTGFIMIS FLIIMAILSL KIIRKSNFEL FYYSHHLFIG FYVLLILHGT MGWIRPPTFW
KWFIVPGFFY TVDRSFRLFK RTHRVEVLDY CLKNERVINL TFSKPPSFDY KPGQYLLINV
PHISKLQWHP FTMTSSPLED KIYVHIRVTG NWTKKLFRWL SIKKQLQQQQ QLYNNIKQQN
VLPDGSNFII NNNNNIDQID LEIGLKPFRI NIDGPFGSSS QYALKQKQVI LVGAGIGVSP
MASLLKDISL KKQRLQLLNQ GDQIALEQSK NEITTKFGLG NLEKVHFFWL NRDQHSFQWF
EDLLIDISTN GNSNLPKISI NTFNTRVFPK NDVRVFMLWN GLDKLFKAQG LDPTTNLPFK
THWGRPNWDT IFQYYSKKYS GESISVFCCG PSQLSKELYE KCRYYTCLKT GGTKFYFHKE
NF
