GLO18_ORYSJ
ID GLO18_ORYSJ Reviewed; 268 AA.
AC Q69L93; B9FV34;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Very-long-chain aldehyde decarbonylase GL1-8 {ECO:0000305};
DE EC=4.1.99.5 {ECO:0000250|UniProtKB:F4HVY0};
DE AltName: Full=Protein GLOSSY 1-8 {ECO:0000303|PubMed:19322663};
GN Name=GL1-8 {ECO:0000303|PubMed:19322663};
GN OrderedLocusNames=LOC_Os07g01150 {ECO:0000305},
GN Os07g0101500 {ECO:0000312|EMBL:BAF20592.1};
GN ORFNames=B1026C12.22 {ECO:0000312|EMBL:BAD31829.1},
GN OSNPB_070101500 {ECO:0000312|EMBL:BAS99681.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19322663; DOI=10.1007/s11103-009-9483-0;
RA Islam M.A., Du H., Ning J., Ye H., Xiong L.;
RT "Characterization of Glossy1-homologous genes in rice involved in leaf wax
RT accumulation and drought resistance.";
RL Plant Mol. Biol. 70:443-456(2009).
CC -!- FUNCTION: Aldehyde decarbonylase involved in the conversion of
CC aldehydes to alkanes. Core component of a very-long-chain alkane
CC synthesis complex. {ECO:0000250|UniProtKB:F4HVY0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty aldehyde + H(+) + 2 NADPH + O2 = a long-
CC chain alkane + formate + H2O + 2 NADP(+); Xref=Rhea:RHEA:21440,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:17176, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:83563; EC=4.1.99.5;
CC Evidence={ECO:0000250|UniProtKB:F4HVY0};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:F4HVY0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:F4HVY0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:F4HVY0}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:19322663}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEE66421.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP005869; BAD31829.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF20592.1; -; Genomic_DNA.
DR EMBL; AP014963; BAS99681.1; -; Genomic_DNA.
DR EMBL; CM000144; EEE66421.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK071749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015646592.1; XM_015791106.1.
DR RefSeq; XP_015646593.1; XM_015791107.1.
DR AlphaFoldDB; Q69L93; -.
DR SMR; Q69L93; -.
DR STRING; 4530.OS07T0101500-01; -.
DR PaxDb; Q69L93; -.
DR PRIDE; Q69L93; -.
DR EnsemblPlants; Os07t0101500-01; Os07t0101500-01; Os07g0101500.
DR GeneID; 4342171; -.
DR Gramene; Os07t0101500-01; Os07t0101500-01; Os07g0101500.
DR KEGG; osa:4342171; -.
DR eggNOG; KOG0873; Eukaryota.
DR HOGENOM; CLU_047036_5_3_1; -.
DR InParanoid; Q69L93; -.
DR OMA; EIMFYYA; -.
DR OrthoDB; 1493916at2759; -.
DR PlantReactome; R-OSA-1119286; Cholesterol biosynthesis II (via 24,25-dihydrolanosterol).
DR PlantReactome; R-OSA-1119439; Cholesterol biosynthesis III (via desmosterol).
DR PlantReactome; R-OSA-1119559; Cholesterol biosynthesis I.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:1990465; F:aldehyde oxygenase (deformylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0000254; F:C-4 methylsterol oxidase activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0009924; F:octadecanal decarbonylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0080065; P:4-alpha-methyl-delta7-sterol oxidation; IBA:GO_Central.
DR GO; GO:1901700; P:response to oxygen-containing compound; IEA:UniProt.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lyase; Membrane; NADP; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..268
FT /note="Very-long-chain aldehyde decarbonylase GL1-8"
FT /id="PRO_0000445880"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 114..249
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT CONFLICT 233
FT /note="S -> P (in Ref. 5; AK071749)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 268 AA; 31298 MW; 523B389FD2174146 CRC64;
MMAAAGLESA WEYLITHFSE FQLASIGTFL LHESVFFLSG LPSLLFERLG LFSKYKIQKK
SNTPDYQNRC VVRLVLYHVC VNLPLTILSY RTFKFMGLRS TLPLPHWTVV VSQVLFFFVL
EDFIFYWGHR ALHTKWLYQH VHSVHHEYAT PFGLTSEYAH PAEILFLGFA TVAGPALTGP
HLFTLWVWMV LRVLETVEAH SGYHFPWSPS NFLPLYGGAE FHDYHHRVLY TKSGNYSSTF
IYMDWLFGTD KDYRKTKALE EKERTKHL
