GLO1A_ORYSJ
ID GLO1A_ORYSJ Reviewed; 301 AA.
AC Q9AV39; Q7XCJ4;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Very-long-chain aldehyde decarbonylase GL1-10 {ECO:0000305};
DE EC=4.1.99.5 {ECO:0000250|UniProtKB:F4HVY0};
DE AltName: Full=Protein GLOSSY 1-10 {ECO:0000303|PubMed:19322663};
GN Name=GL1-10 {ECO:0000303|PubMed:19322663};
GN OrderedLocusNames=LOC_Os10g39810 {ECO:0000312|EMBL:AAP54879.1},
GN Os10g0545200 {ECO:0000312|EMBL:BAF27120.1};
GN ORFNames=OSJNBa0001O14.3 {ECO:0000312|EMBL:AAK20047.1},
GN OSNPB_100545200 {ECO:0000312|EMBL:BAT11897.1};
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=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
RN [2]
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 [3]
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 [4]
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 [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}.
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DR EMBL; AC025783; AAK20047.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP54879.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF27120.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT11897.1; -; Genomic_DNA.
DR EMBL; AK098884; BAG93792.1; -; mRNA.
DR EMBL; AK121804; BAH00667.1; -; mRNA.
DR RefSeq; XP_015614342.1; XM_015758856.1.
DR AlphaFoldDB; Q9AV39; -.
DR STRING; 4530.OS10T0545200-01; -.
DR PaxDb; Q9AV39; -.
DR PRIDE; Q9AV39; -.
DR EnsemblPlants; Os10t0545200-01; Os10t0545200-01; Os10g0545200.
DR EnsemblPlants; Os10t0545200-02; Os10t0545200-02; Os10g0545200.
DR GeneID; 4349278; -.
DR Gramene; Os10t0545200-01; Os10t0545200-01; Os10g0545200.
DR Gramene; Os10t0545200-02; Os10t0545200-02; Os10g0545200.
DR KEGG; osa:4349278; -.
DR eggNOG; KOG0873; Eukaryota.
DR HOGENOM; CLU_047036_5_3_1; -.
DR InParanoid; Q9AV39; -.
DR OMA; YGGVAHH; -.
DR OrthoDB; 1493916at2759; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
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: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..301
FT /note="Very-long-chain aldehyde decarbonylase GL1-10"
FT /id="PRO_0000445884"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 131..265
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
SQ SEQUENCE 301 AA; 34409 MW; A3B06016BEFA4D67 CRC64;
MLPYATAAEA EAALGRAMTA AESLWFRYSA GIPDYVLFWH NILFLFVVFT LAPLPVALLE
LRAPAAVGPF KLQPKVRLSR EEFFRCYRDV MRLFFLVIGP LQLVSYPTVK MVGIHTGLPL
PSLGEMAAQL LVYFLVEDYL NYWIHRLLHG EWGYEKIHRV HHEFTAPIGF AAPYAHWAEV
LILGIPSFVG PALAPGHMIT FWLWIVLRQM EAIETHSGFD FPFNLTKYIP FYGGAEYHDY
HHYVGRQSQS NFASVFTYCD YLYGTDKGYR YHKAYQAKMK ALGQTEGEKA DSNGLSYAKL
D
