GLO15_ORYSJ
ID GLO15_ORYSJ Reviewed; 621 AA.
AC Q7XDI3; Q9FWK6;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Very-long-chain aldehyde decarbonylase GL1-5 {ECO:0000305};
DE EC=4.1.99.5 {ECO:0000250|UniProtKB:F4HVY0};
DE AltName: Full=Protein GLOSSY 1-5 {ECO:0000303|PubMed:19322663};
DE AltName: Full=Protein WAX-DEFICIENT ANTHER 1 {ECO:0000303|PubMed:17138699};
GN Name=GL1-5 {ECO:0000303|PubMed:19322663};
GN Synonyms=WDA1 {ECO:0000303|PubMed:17138699};
GN OrderedLocusNames=LOC_Os10g33250 {ECO:0000312|EMBL:AAP54228.1},
GN Os10g0471100 {ECO:0000312|EMBL:BAF26740.1};
GN ORFNames=OsJ_31858 {ECO:0000312|EMBL:EEE51118.1},
GN OSJNBa0079L16.17 {ECO:0000312|EMBL:AAG21908.1},
GN OSNPB_100471100 {ECO:0000312|EMBL:BAT11256.1};
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 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 [6]
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND CATALYTIC ACTIVITY.
RX PubMed=17138699; DOI=10.1105/tpc.106.042044;
RA Jung K.-H., Han M.-J., Lee D.-Y., Lee Y.-S., Schreiber L., Franke R.,
RA Faust A., Yephremov A., Saedler H., Kim Y.-W., Hwang I., An G.;
RT "Wax-deficient anther1 is involved in cuticle and wax production in rice
RT anther walls and is required for pollen development.";
RL Plant Cell 18:3015-3032(2006).
RN [8]
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 (PubMed:17138699). Core component of a very-long-
CC chain alkane synthesis complex (By similarity). Required for the
CC biosynthesis of very-long-chain fatty acids (including polyesters) in
CC cuticles, anther tapetum and pollen exine (PubMed:17138699).
CC {ECO:0000250|UniProtKB:F4HVY0, ECO:0000269|PubMed:17138699}.
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:0000269|PubMed:17138699};
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 panicles, developing spikelets,
CC stamens and hulls and, at low levels, in roots, developing seeds, flag
CC leaves and seedling shoots (PubMed:19322663, PubMed:17138699). Strongly
CC expressed in the epidermal cells of anthers (PubMed:17138699).
CC {ECO:0000269|PubMed:17138699, ECO:0000269|PubMed:19322663}.
CC -!- DEVELOPMENTAL STAGE: In developing spikelets, expressed in all floral
CC organs from the premeiosis stage to the heading stage. Also present in
CC the outer and inner epidermis and trichomes of the palea/lemma,
CC lodicules, stigmas, and anthers. In anthers at the vacuolated pollen
CC stage, expressed strongly in the epidermis but only weakly in the
CC tapetum, endothecium, and connective tissue. In vegetative tissue,
CC confinde to collar regions (between the leaf sheath and the leaf blade)
CC and the base of shoots. {ECO:0000269|PubMed:17138699}.
CC -!- INDUCTION: Induced by salt stress and abscisic acid (ABA).
CC {ECO:0000269|PubMed:19322663}.
CC -!- DISRUPTION PHENOTYPE: Male-sterile plants characterized by small and
CC white anthers lacking mature pollen grains. Defects in the biosynthesis
CC of very-long-chain fatty acids (including polyesters) in cuticles and
CC in the innermost layer of the anther wall (the tapetum). Lack of
CC epicuticular wax crystals in the outer layer of the anther and severely
CC retarded microspore development and finally disrupted as a result of
CC defective pollen exine formation. {ECO:0000269|PubMed:17138699}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK100751; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC026815; AAG21908.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP54228.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF26740.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT11256.1; -; Genomic_DNA.
DR EMBL; CM000147; EEE51118.1; -; Genomic_DNA.
DR EMBL; AK100751; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q7XDI3; -.
DR STRING; 4530.OS10T0471100-01; -.
DR PaxDb; Q7XDI3; -.
DR PRIDE; Q7XDI3; -.
DR EnsemblPlants; Os10t0471100-01; Os10t0471100-01; Os10g0471100.
DR Gramene; Os10t0471100-01; Os10t0471100-01; Os10g0471100.
DR eggNOG; ENOG502QR3T; Eukaryota.
DR HOGENOM; CLU_017842_1_0_1; -.
DR InParanoid; Q7XDI3; -.
DR OMA; MIRNNCC; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000007752; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR ExpressionAtlas; Q7XDI3; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:Gramene.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0043668; C:exine; IMP:Gramene.
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:0048653; P:anther development; IMP:Gramene.
DR GO; GO:0048658; P:anther wall tapetum development; IMP:UniProtKB.
DR GO; GO:0042335; P:cuticle development; IMP:UniProtKB.
DR GO; GO:0010143; P:cutin biosynthetic process; IDA:Gramene.
DR GO; GO:0010584; P:pollen exine formation; IMP:UniProtKB.
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 GO; GO:0010025; P:wax biosynthetic process; IDA:Gramene.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Lyase; Membrane; NADP; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..621
FT /note="Very-long-chain aldehyde decarbonylase GL1-5"
FT /id="PRO_0000445875"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 138..272
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT CONFLICT 348
FT /note="S -> P (in Ref. 6; AK100751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 621 AA; 71216 MW; A676944A135052F3 CRC64;
MATNPGLFTE WPWKKLGSFK YVLLAPWVAH GWYEVATKGW REVDLGYIAI LPSLLLRMLH
NQAWITISRL QNARGRRQIV RRGIEFDQVD RERNWDDQII LSGILLYLGA LYVPGGQHLP
LWRTDGAGLI ALLHAGPVEF LYYWFHRALH HHFLYTHYHS HHHSSIVTEP ITSVIHPFAE
LVAYELLFSI PLIACALTGT ASIIAFEMYL IYIDFMNNMG HCNFELVPSW LFTWFPPLKY
LMYTPSFHSL HHTQFRTNYS LFMPFYDYIY NTMDKSSDTL YENSLKNNEE EEAVDVVHLT
HLTTLHSIYH MRPGFAEFAS RPYVSRWYMR MMWPLSWLSM VLTWTYGSSF TVERNVMKKI
RMQSWAIPRY SFHYGLDWEK EAINDLIEKA VCEADKNGAK VVSLGLLNQA HTLNKSGEQY
LLKYPKLGAR IVDGTSLAAA VVVNSIPQGT DQVILAGNVS KVARAVAQAL CKKNIKVTMT
NKQDYHLLKP EIPETVADNL SFSKTGTAKV WLIGDGLDSA EQFRAQKGTL FIPYSQFPPK
MVRKDSCSYS TTPAMAVPKT LQNVHSCENW LPRRVMSAWR IAGILHALEG WNEHECGDKV
LDMDKVWSAA IMHGFCPVAQ G
