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Database: UniProt
Entry: A0A0A0LUN1_CUCSA
LinkDB: A0A0A0LUN1_CUCSA
Original site: A0A0A0LUN1_CUCSA 
ID   A0A0A0LUN1_CUCSA        Unreviewed;       773 AA.
AC   A0A0A0LUN1;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KGN63726.1};
GN   ORFNames=Csa_1G013250 {ECO:0000313|EMBL:KGN63726.1};
OS   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN63726.1, ECO:0000313|Proteomes:UP000029981};
RN   [1] {ECO:0000313|EMBL:KGN63726.1, ECO:0000313|Proteomes:UP000029981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX   PubMed=19881527; DOI=10.1038/ng.475;
RA   Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA   Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA   Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA   Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA   Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA   Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA   Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA   Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA   Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA   Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA   Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA   Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT   "The genome of the cucumber, Cucumis sativus L.";
RL   Nat. Genet. 41:1275-1281(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family.
CC       {ECO:0000256|ARBA:ARBA00007975}.
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DR   EMBL; CM002922; KGN63726.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A0LUN1; -.
DR   STRING; 3659.A0A0A0LUN1; -.
DR   EnsemblPlants; KGN63726; KGN63726; Csa_1G013250.
DR   Gramene; KGN63726; KGN63726; Csa_1G013250.
DR   eggNOG; KOG0039; Eukaryota.
DR   OMA; DENQAIH; -.
DR   Proteomes; UP000029981; Chromosome 1.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IBA:GO_Central.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 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; IPR013623; NADPH_Ox.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR   PANTHER; PTHR11972:SF127; RESPIRATORY BURST OXIDASE HOMOLOG PROTEIN A-LIKE; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   Pfam; PF08414; NADPH_Ox; 1.
DR   PRINTS; PR00466; GP91PHOX.
DR   SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR   SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029981};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        249..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        390..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        430..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          131..166
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          484..589
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   773 AA;  89519 MW;  D4BFFA8D957E0B92 CRC64;
     MELRKTEEKL SVSSSLSSSL SSSSSCSSSY WSSRGENHED RSSKRSPRMR FIDFLRDKEW
     EWKLAEKRFD QLCWICAGNE PAIKSSNFPF CIGMSESQEF AYQLLRALRR RKNWKIDITK
     SEFHILWCHF THSDATTTLF HLCDRNMDGK VTENDIKQII MLTASTNKLS VTHEEGEDYA
     ALVMEELDEE KQGYLELHQF ENLFKISSSN VLSPLNKQSS NKHIWQSHDS FQESIYEAEI
     LLRSRWRRAW TVALWLIICL ALFTWKFIQY RQRKAFEVMG YCLSIAKGAA ETLKFNMALV
     LLPVCRNTIT WLRRNSSLNS VIPFNDNVNF HKLVAGGIVA GVILHGGTHL ACDFPRISGC
     EKSIFKKTIA AQFNYHQPSY VEMLATTESL TGIIMVILMF IAFLLATKWP RRKSTSLPRS
     IQQVTGYNTF WYSHHLFIFV YALLIVHSIF LFLTDKTTEK TTWMYIAVPV LLYSGERIFR
     AIRSCLYEVN VLKARTYSGK VLFLKLSKPE RFKYQSGMYV LIQCPQISPF EWHPYSLTSA
     PQDSHLSVHI RNLGDWSYEL YSLFHEGTFP SKNYPKIFID GPYGAASQDH VKYNNVVLIG
     LGIGATPFMS IMKDIVIKFT EKSNRRGDSG KGNQSTSKTY LYWVTREQSS FDWFKDFMND
     LTFTDQTQLA VEMHNFLTSV YHEGDVRSVL IRAIQALHYT RRGIDIVSKT PVQTHFGRPN
     WINIFSSLAR RHARERIGVF YCGPLALARE LEGLCTKFST KTSTRFVFHK ENY
//
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