GLO16_ORYSJ
ID GLO16_ORYSJ Reviewed; 635 AA.
AC Q6K3D8;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Very-long-chain aldehyde decarbonylase GL1-6 {ECO:0000305};
DE EC=4.1.99.5 {ECO:0000250|UniProtKB:F4HVY0};
DE AltName: Full=Protein GLOSSY 1-6 {ECO:0000303|PubMed:19322663};
GN Name=GL1-6 {ECO:0000303|PubMed:19322663};
GN OrderedLocusNames=LOC_Os02g56920 {ECO:0000305},
GN Os02g0814200 {ECO:0000312|EMBL:BAF10404.1};
GN ORFNames=OJ1293_E04.17 {ECO:0000312|EMBL:BAD21663.1},
GN OsJ_08848 {ECO:0000312|EMBL:EAZ25056.1},
GN OSJNBa0053L11.39 {ECO:0000312|EMBL:BAD22402.1},
GN OSNPB_020814200 {ECO:0000312|EMBL:BAS81546.1};
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, INDUCTION BY DROUGHT; COLD AND SALT STRESS, GENE
RP 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 in germinating seeds and shoots.
CC {ECO:0000269|PubMed:19322663}.
CC -!- INDUCTION: Induced by drought, cold and salt stress.
CC {ECO:0000269|PubMed:19322663}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP004120; BAD21663.1; -; Genomic_DNA.
DR EMBL; AP005691; BAD22402.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF10404.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS81546.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ25056.1; -; Genomic_DNA.
DR EMBL; AK068166; BAG90785.1; -; mRNA.
DR RefSeq; XP_015624738.1; XM_015769252.1.
DR AlphaFoldDB; Q6K3D8; -.
DR STRING; 4530.OS02T0814200-01; -.
DR PaxDb; Q6K3D8; -.
DR PRIDE; Q6K3D8; -.
DR EnsemblPlants; Os02t0814200-01; Os02t0814200-01; Os02g0814200.
DR GeneID; 4331117; -.
DR Gramene; Os02t0814200-01; Os02t0814200-01; Os02g0814200.
DR KEGG; osa:4331117; -.
DR eggNOG; ENOG502QR3T; Eukaryota.
DR HOGENOM; CLU_017842_1_0_1; -.
DR InParanoid; Q6K3D8; -.
DR OMA; VCENWLP; -.
DR OrthoDB; 331955at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q6K3D8; baseline and differential.
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:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; 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 InterPro; IPR006694; Fatty_acid_hydroxylase.
DR InterPro; IPR021940; Uncharacterised_Wax2_C.
DR Pfam; PF04116; FA_hydroxylase; 1.
DR Pfam; PF12076; Wax2_C; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lyase; Membrane; NADP; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..635
FT /note="Very-long-chain aldehyde decarbonylase GL1-6"
FT /id="PRO_0000445877"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 139..273
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
SQ SEQUENCE 635 AA; 71639 MW; 9BE976744DE2AD82 CRC64;
MASKPGPLTQ WPWHNLGNYK YALVAPSAAY STYRFVTASS AAERDLLNFM VFPMLLLRLL
YGQLWITVSR HQTARSKHKI VNKSLDFEQI DRERNWDDQI ILTALVFYLV SATMPQAQVA
PWWSTKGMVV TAVLHAGPVE FLYYWLHRAL HHHWLYARYH SHHHASIVTE PITSVIHPFA
EEVVYFVLLA IPILSTVATG TVSVVTANGY LVYIDFMNYL GHCNFELVPK CLFHVFPPLK
YLLYTPSFHS LHHTQFRTNY SLFMPVYDYI YGTTDKSSDE LYERTLQGRD EAAWRPDVVH
LTHLTTPESV FHNRLGFAAV ASNPLGAAAS GHLLRAASAV ASPLLSLFAS TFRSEANRLD
KLNIETWVIP RFTSHYTSKS DGYKVSRLIE KAVSDAEASG ARVLTLGLLN QGYDLNRNGE
LYVVRKPSLK TKIVDGTSLA VAAVLNMIPQ GTKDVLLLGN ANKISLVLTL SLCKREIQVR
MVNKELYECL KQQLQPEMQE HLVLSCSYSS KVWLVGDGVT DEEQMKAQKG SHFVPYSQFP
PNKARNDCVY HCTPALLVPE SFENLHVCEN WLPRRVMSAW RAAGIVHALE KWDGHECGGR
VTGVQKAWSA ALARGFRPYD DHHHPGITHD GRGGL
