GLO14_ORYSJ
ID GLO14_ORYSJ Reviewed; 619 AA.
AC Q6K9F6; B9F151;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Very-long-chain aldehyde decarbonylase GL1-4 {ECO:0000305};
DE EC=4.1.99.5 {ECO:0000250|UniProtKB:F4HVY0};
DE AltName: Full=Protein GLOSSY 1-4 {ECO:0000303|PubMed:19322663};
GN Name=GL1-4 {ECO:0000303|PubMed:19322663};
GN OrderedLocusNames=LOC_Os02g40784 {ECO:0000305},
GN Os02g0621300 {ECO:0000312|EMBL:BAF09373.1};
GN ORFNames=OJ1234_B11.10 {ECO:0000312|EMBL:BAD21539.1},
GN OJ1372_D06.35 {ECO:0000312|EMBL:BAD21579.1},
GN OSNPB_020621300 {ECO:0000312|EMBL:BAS79824.1};
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, AND DEVELOPMENTAL STAGE.
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 [7]
RP TISSUE SPECIFICITY, INDUCTION BY COLD AND ABSCISIC ACID, GENE FAMILY, AND
RP 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 at low levels, with higher
CC accumulation in developing panicles, shoots and flag leaves.
CC {ECO:0000269|PubMed:17138699, ECO:0000269|PubMed:19322663}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout panicle development. In
CC mature spikelets, present at low levels in anthers and palea/lemma, and
CC barely detectable in the ovaries and lodicules.
CC {ECO:0000269|PubMed:17138699}.
CC -!- INDUCTION: Induced by cold and abscisic acid (ABA).
CC {ECO:0000269|PubMed:19322663}.
CC -!- MISCELLANEOUS: Identified as LOC_Os02g40780 in PubMed:17138699.
CC {ECO:0000305|PubMed:17138699}.
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; AP004053; BAD21539.1; -; Genomic_DNA.
DR EMBL; AP004059; BAD21579.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09373.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79824.1; -; Genomic_DNA.
DR EMBL; CM000139; EEE57393.1; -; Genomic_DNA.
DR EMBL; AK066386; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015627618.1; XM_015772132.1.
DR AlphaFoldDB; Q6K9F6; -.
DR STRING; 4530.OS02T0621300-01; -.
DR PaxDb; Q6K9F6; -.
DR PRIDE; Q6K9F6; -.
DR EnsemblPlants; Os02t0621300-01; Os02t0621300-01; Os02g0621300.
DR GeneID; 4330012; -.
DR Gramene; Os02t0621300-01; Os02t0621300-01; Os02g0621300.
DR KEGG; osa:4330012; -.
DR eggNOG; ENOG502QR3T; Eukaryota.
DR HOGENOM; CLU_017842_1_0_1; -.
DR InParanoid; Q6K9F6; -.
DR OMA; SIYSFFM; -.
DR OrthoDB; 331955at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; 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:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009409; P:response to cold; 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..619
FT /note="Very-long-chain aldehyde decarbonylase GL1-4"
FT /id="PRO_0000445873"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 138..272
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT CONFLICT 8..14
FT /note="LTEWPWH -> FYEWALD (in Ref. 4; EEE57393)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="D -> G (in Ref. 5; AK066386)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 71523 MW; 615EAB63D4500537 CRC64;
MATRPGPLTE WPWHRLGNFK YVVMAPVVAH GARRVMRNGW GDLDIAFSLI LPSLLLRMIH
NQIWISLSRY QTARSKHRIV DRGIEFDQVD RERGWDDQIL FNGLVFYAGY LAMPSVRRMP
VWRTDGAVVT ALVHTGPVEF LYYWFHRALH HHFLYSRYHS HHHASIVTEP ITSVIHPFAE
HVVYFILFAI PILSTIYLGN VSAMGIVGYI AYIDFMNNMG HCNFELVPEW IFQIFPPLKY
LIYTPSFHSL HHTQFRTNYS LFMPFYDYIY NTMDKSSDEL YESSLKGTEE TPDLVHLTHM
TNLQSAYHLR IGIASIASKP YSDSAWYMWT LWPLAWLSMV LAWIYGSSAF VVERIKLNKM
KMQTWALPRY NFQYGLTWER EPINDLIEKA ILDADMKGVK VISLGLLNQA KQLNGNGELF
RQKYPKLGVR IIDGSGLATA VVLKSIPSDA KKVFLRTGTS KIARAIAIAL CDRGVQVIMN
EKEVYHMLKS QIPENRASYL KLSSDNVPQL WIVHNIDDNE QKMAPKGTIF IPISQFPLKK
LRKDCTYMST PAMRIPEEMK NIHSCENWLP RRVMSAWHIA GILHALEGWN MHECGDEMMD
IEKSWSAAIR HGFLPLTKA
