GLO13_ORYSJ
ID GLO13_ORYSJ Reviewed; 618 AA.
AC Q67WQ7; O04693;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Very-long-chain aldehyde decarbonylase GL1-3 {ECO:0000305};
DE EC=4.1.99.5 {ECO:0000250|UniProtKB:F4HVY0};
DE AltName: Full=Protein GLOSSY 1-3 {ECO:0000303|PubMed:19322663};
DE AltName: Full=Protein GLOSSY l {ECO:0000303|PubMed:9112770};
GN Name=GL1-3 {ECO:0000303|PubMed:19322663};
GN Synonyms=GL1 {ECO:0000303|PubMed:9112770};
GN OrderedLocusNames=LOC_Os06g44300 {ECO:0000305},
GN Os06g0653000 {ECO:0000312|EMBL:BAF20151.1};
GN ORFNames=OsJ_22195 {ECO:0000312|EMBL:EEE66138.1},
GN OSJNBa0085J13.13 {ECO:0000312|EMBL:BAD37412.1},
GN OSNPB_060653000 {ECO:0000312|EMBL:BAS98921.1};
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 [MRNA] OF 63-618.
RC STRAIN=cv. Nipponbare;
RX PubMed=9112770; DOI=10.1104/pp.113.4.1091;
RA Hansen J.D., Pyee J., Xia Y., Wen T.-J., Robertson D.S., Kolattukudy P.E.,
RA Nikolau B.J., Schnable P.S.;
RT "The glossy1 locus of maize and an epidermis-specific cDNA from Kleinia
RT odora define a class of receptor-like proteins required for the normal
RT accumulation of cuticular waxes.";
RL Plant Physiol. 113:1091-1100(1997).
RN [6]
RP TISSUE SPECIFICITY, INDUCTION BY SALT STRESS AND ABSCISIC ACID, 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 stamens.
CC {ECO:0000269|PubMed:19322663}.
CC -!- INDUCTION: Induced by salt stress and abscisic acid (ABA).
CC {ECO:0000269|PubMed:19322663}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD37412.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF20151.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS98921.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EEE66138.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP003565; BAD37412.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008212; BAF20151.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014962; BAS98921.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000143; EEE66138.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK070469; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U57338; AAB87722.1; -; mRNA.
DR PIR; T04146; T04146.
DR RefSeq; XP_015641638.1; XM_015786152.1.
DR AlphaFoldDB; Q67WQ7; -.
DR SMR; Q67WQ7; -.
DR STRING; 4530.OS06T0653000-01; -.
DR PaxDb; Q67WQ7; -.
DR PRIDE; Q67WQ7; -.
DR GeneID; 4341702; -.
DR KEGG; osa:4341702; -.
DR eggNOG; ENOG502S53G; Eukaryota.
DR HOGENOM; CLU_017842_2_0_1; -.
DR InParanoid; Q67WQ7; -.
DR OrthoDB; 771394at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
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:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
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..618
FT /note="Very-long-chain aldehyde decarbonylase GL1-3"
FT /id="PRO_0000445872"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 127..267
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT CONFLICT 185..199
FT /note="APLAGAFMAGHGSVS -> PHLQGLHGGTRLRE (in Ref. 5;
FT AAB87722)"
FT /evidence="ECO:0000305"
FT CONFLICT 206..226
FT /note="LLFDYLRSMGYSNVEVISHKT -> SSSTTPVHGVQQRRGHLTQD (in
FT Ref. 5; AAB87722)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="L -> F (in Ref. 5; AAB87722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 618 AA; 69812 MW; ED0F6FAA90255FFD CRC64;
MAISMASPLS SWPWAFLGSY KYLLYGPVVG KVVQEWREQG RLPLGTSWCL HLILLLALRS
LTMLFFTRRR RVVDDGVDFR QIDTEWDWDN MVIMQTLIAA VLVTSRVFPA TSDLSAWDLR
GWAIAVVLHV AVSEPAFYWA HRALHLGPLF SRYHSLHHSF QATQALTAGF VTPLESLILT
LVAWAPLAGA FMAGHGSVSL VYGHILLFDY LRSMGYSNVE VISHKTFQDF PFLRYLIYTP
SYLSLHHREK DSNFCLFMPL FDALGGTLNP KSWQLQKEVD LGKNHRVPDF VFLVHVVDVV
SSMHVPFAFR ACSSLPFATH LVLLPLWPIA FGFMLLQWFC SKTFTVSFYK LRGFLHQTWS
VPRYGFQYFI PSAKKGINEM IELAILRADK MGVKVLSLAA LNKNEALNGG GTLFVRKHPD
LRVRVVHGNT LTAAVILNEI PGDVAEVFLT GATSKLGRAI ALYLCRKKIR VLMLTLSTER
FMNIQREAPA EFQQYLVQVT KYQAAQNCKT WIVGKWLSPR EQRWAPAGTH FHQFVVPPII
GFRRDCTYGK LAAMRLPEDV EGLGTCEYTM GRGVVHACHA GGVVHFLEGW DHHEVGAIDV
DRIDAVWNAA LRHGLTPA
