GLO12_ORYSJ
ID GLO12_ORYSJ Reviewed; 628 AA.
AC Q6ETL8; A0A0P0VFI0;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Very-long-chain aldehyde decarbonylase GL1-2 {ECO:0000305};
DE EC=4.1.99.5 {ECO:0000250|UniProtKB:F4HVY0};
DE AltName: Full=Protein GLOSSY 1-2 {ECO:0000303|PubMed:19322663};
GN Name=GL1-2 {ECO:0000303|PubMed:19322663};
GN OrderedLocusNames=LOC_Os02g08230 {ECO:0000305},
GN Os02g0178800 {ECO:0000312|EMBL:BAF07994.1};
GN ORFNames=OSNPB_020178800 {ECO:0000312|EMBL:BAS77283.1},
GN P0544B02.10 {ECO:0000312|EMBL:BAD28002.1};
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 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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY DROUGHT
RP AND ABSCISIC ACID, 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 (By similarity). Required for the formation of wax
CC layers conferring cuticular permeability and drought tolerance
CC (PubMed:19322663). {ECO:0000250|UniProtKB:F4HVY0,
CC ECO:0000269|PubMed:19322663}.
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 in germinating seeds, radicals and
CC leaves. {ECO:0000269|PubMed:19322663}.
CC -!- INDUCTION: Induced by drought and abscisic acid (ABA).
CC {ECO:0000269|PubMed:19322663}.
CC -!- DISRUPTION PHENOTYPE: Early leaf-rolling at the reproductive stage.
CC Reduced wax accumulation (lower total proportions of aldehydes, fatty
CC acids, alkanes and alcohol) in leaf cuticle leading to an increased
CC cuticular permeability (e.g. chlorophyll leaching) and a subsequent
CC altered drought resistance due to rapid water loss.
CC {ECO:0000269|PubMed:19322663}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR EMBL; AP004840; BAD28002.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF07994.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS77283.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS77284.1; -; Genomic_DNA.
DR EMBL; AK066569; BAG90034.1; -; mRNA.
DR RefSeq; XP_015623214.1; XM_015767728.1.
DR AlphaFoldDB; Q6ETL8; -.
DR SMR; Q6ETL8; -.
DR STRING; 4530.OS02T0178800-01; -.
DR PaxDb; Q6ETL8; -.
DR PRIDE; Q6ETL8; -.
DR EnsemblPlants; Os02t0178800-01; Os02t0178800-01; Os02g0178800.
DR GeneID; 4328496; -.
DR Gramene; Os02t0178800-01; Os02t0178800-01; Os02g0178800.
DR KEGG; osa:4328496; -.
DR eggNOG; ENOG502S53G; Eukaryota.
DR HOGENOM; CLU_017842_2_0_1; -.
DR InParanoid; Q6ETL8; -.
DR OMA; PAQNCKT; -.
DR OrthoDB; 771394at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
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:0046184; P:aldehyde biosynthetic process; IMP:UniProtKB.
DR GO; GO:0043447; P:alkane biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0010025; P:wax biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR021940; Uncharacterised_Wax2_C.
DR Pfam; PF04116; FA_hydroxylase; 1.
DR Pfam; PF12076; Wax2_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lyase; Membrane; NADP; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..628
FT /note="Very-long-chain aldehyde decarbonylase GL1-2"
FT /id="PRO_0000445870"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 137..277
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
SQ SEQUENCE 628 AA; 71015 MW; 74619278DD15A201 CRC64;
MAAPPLSSWP WASLGSYKYV LYGAVVWKVA EEWRQQGAAP VGSWWLHLLL LFAARGLTYQ
FWFSYGNMLF FTRRRRVVPD SVDFRQVDAE WDWDNFLLLQ TLIGATLVGS PAVARQQLLL
PSLKQAWDPR GWAIALLLHV LVAEPLFYWA HRALHRAPLF SRYHAAHHHA SVTTPLTAGF
GTPLESLLLT VVIGVPLAGA FLMGVGSVGL VYGHVLLFDF LRSMGYSNVE VISPRVFQAV
PLLRYLIYTP TYLSLHHREK DSNFCLFMPI FDLLGGTLNH KSWELQKEVY LGKNDQAPDF
VFLAHVVDIM ASMHVPFVLR SCSSTPFANH FVLLPFWPVA FGFMLLMWCC SKTFLVSSYR
LRGNLHQMWT VPRYGFQYFI PAAKKGINEQ IELAILRADR MGVKVLSLAA LNKNEALNGG
GTLFVNKHPE LRVRVVHGNT LTAAVILNEI PSNVKDVFLT GATSKLGRAI ALYLCRKKIR
VLMLTLSSER FLKIQREAPA EFQQYLVQVT KYQPAQNCKT WLVGKWLSPR EQRWAPAGTH
FHQFVVPPII GFRRDCTYGK LAAMRLPKDV QGLGYCEYTM ERGVVHACHA GGVVHFLEGW
EHHEVGAIDV DRIDVVWKAA LKHGLTPA
