CER3_ARATH
ID CER3_ARATH Reviewed; 632 AA.
AC Q8H1Z0; Q94B63; Q9FJN4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Very-long-chain aldehyde decarbonylase CER3 {ECO:0000305};
DE EC=4.1.99.5 {ECO:0000250|UniProtKB:F4HVY0};
DE AltName: Full=Protein ECERIFERUM 3;
DE AltName: Full=Protein FACELESS POLLEN 1;
DE AltName: Full=Protein WAX2;
DE AltName: Full=Protein YORE-YORE;
GN Name=CER3; Synonyms=FLP1, WAX2, YRE; OrderedLocusNames=At5g57800;
GN ORFNames=MTI20.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. C24;
RX PubMed=12724542; DOI=10.1105/tpc.010926;
RA Chen X., Goodwin S.M., Boroff V.L., Liu X., Jenks M.A.;
RT "Cloning and characterization of the WAX2 gene of Arabidopsis involved in
RT cuticle membrane and wax production.";
RL Plant Cell 15:1170-1185(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=12974811; DOI=10.1046/j.1365-313x.2003.01854.x;
RA Kurata T., Kawabata-Awai C., Sakuradani E., Shimizu S., Okada K., Wada T.;
RT "The YORE-YORE gene regulates multiple aspects of epidermal cell
RT differentiation in Arabidopsis.";
RL Plant J. 36:55-66(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=14756310; DOI=10.1023/b:plan.0000009269.97773.70;
RA Ariizumi T., Hatakeyama K., Hinata K., Sato S., Kato T., Tabata S.,
RA Toriyama K.;
RT "A novel male-sterile mutant of Arabidopsis thaliana, faceless pollen-1,
RT produces pollen with a smooth surface and an acetolysis-sensitive exine.";
RL Plant Mol. Biol. 53:107-116(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 443-632.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP IDENTIFICATION, MUTAGENESIS OF ALA-408, AND DISRUPTION PHENOTYPE.
RX PubMed=17624331; DOI=10.1016/j.febslet.2007.06.065;
RA Rowland O., Lee R., Franke R., Schreiber L., Kunst L.;
RT "The CER3 wax biosynthetic gene from Arabidopsis thaliana is allelic to
RT WAX2/YRE/FLP1.";
RL FEBS Lett. 581:3538-3544(2007).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=19892830; DOI=10.1093/pcp/pcp152;
RA Kamigaki A., Kondo M., Mano S., Hayashi M., Nishimura M.;
RT "Suppression of peroxisome biogenesis factor 10 reduces cuticular wax
RT accumulation by disrupting the ER network in Arabidopsis thaliana.";
RL Plant Cell Physiol. 50:2034-2046(2009).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=21386033; DOI=10.1104/pp.111.172320;
RA Bourdenx B., Bernard A., Domergue F., Pascal S., Leger A., Roby D.,
RA Pervent M., Vile D., Haslam R.P., Napier J.A., Lessire R., Joubes J.;
RT "Overexpression of Arabidopsis ECERIFERUM1 promotes wax very-long-chain
RT alkane biosynthesis and influences plant response to biotic and abiotic
RT stresses.";
RL Plant Physiol. 156:29-45(2011).
RN [10]
RP FUNCTION, INTERACTION WITH CER1, AND MUTAGENESIS OF HIS-147; HIS-161 AND
RP HIS-250.
RC STRAIN=cv. Columbia;
RX PubMed=22773744; DOI=10.1105/tpc.112.099796;
RA Bernard A., Domergue F., Pascal S., Jetter R., Renne C., Faure J.D.,
RA Haslam R.P., Napier J.A., Lessire R., Joubes J.;
RT "Reconstitution of plant alkane biosynthesis in yeast demonstrates that
RT Arabidopsis ECERIFERUM1 and ECERIFERUM3 are core components of a very-long-
RT chain alkane synthesis complex.";
RL Plant Cell 24:3106-3118(2012).
CC -!- FUNCTION: Involved in cuticule membrane and wax production, and in the
CC typhine and sporopollenin biosynthesis of pollen. Core components of a
CC very-long-chain alkane synthesis complex. May be the fatty acid
CC reductase responsible for aldehyde formation.
CC {ECO:0000269|PubMed:12724542, ECO:0000269|PubMed:12974811,
CC ECO:0000269|PubMed:14756310, ECO:0000269|PubMed:22773744}.
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: Interacts with CER1. {ECO:0000269|PubMed:22773744}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19892830}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19892830}.
CC -!- TISSUE SPECIFICITY: Expressed in siliques, stems, flowers and weakly in
CC leaves. Not detected in pollen, seeds and roots, but expressed in
CC lateral root primordia. Specifically found in the L1 layer of the shoot
CC apical meristem and in developing trichomes.
CC {ECO:0000269|PubMed:12724542, ECO:0000269|PubMed:12974811,
CC ECO:0000269|PubMed:14756310, ECO:0000269|PubMed:21386033}.
CC -!- DISRUPTION PHENOTYPE: Plants show postgenital fusion between aerial
CC organs and severe male sterility in low-humidity environments. Altered
CC cuticular waxes, but no effect on cutin load and composition.
CC {ECO:0000269|PubMed:12724542, ECO:0000269|PubMed:12974811,
CC ECO:0000269|PubMed:14756310, ECO:0000269|PubMed:17624331}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK68765.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB08850.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY131334; AAN06975.1; -; mRNA.
DR EMBL; AB116548; BAC81644.1; -; mRNA.
DR EMBL; AB099512; BAD06945.1; -; mRNA.
DR EMBL; AB013396; BAB08850.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96953.1; -; Genomic_DNA.
DR EMBL; AY042825; AAK68765.1; ALT_INIT; mRNA.
DR EMBL; BT002119; AAN72130.1; -; mRNA.
DR RefSeq; NP_200588.2; NM_125164.3.
DR AlphaFoldDB; Q8H1Z0; -.
DR BioGRID; 21133; 1.
DR STRING; 3702.AT5G57800.1; -.
DR PaxDb; Q8H1Z0; -.
DR PRIDE; Q8H1Z0; -.
DR ProteomicsDB; 241227; -.
DR EnsemblPlants; AT5G57800.1; AT5G57800.1; AT5G57800.
DR GeneID; 835889; -.
DR Gramene; AT5G57800.1; AT5G57800.1; AT5G57800.
DR KEGG; ath:AT5G57800; -.
DR Araport; AT5G57800; -.
DR TAIR; locus:2174368; AT5G57800.
DR eggNOG; ENOG502QQ3D; Eukaryota.
DR HOGENOM; CLU_017842_2_0_1; -.
DR InParanoid; Q8H1Z0; -.
DR OMA; AMWAWAK; -.
DR OrthoDB; 771394at2759; -.
DR PhylomeDB; Q8H1Z0; -.
DR BioCyc; ARA:AT5G57800-MON; -.
DR PRO; PR:Q8H1Z0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8H1Z0; baseline and differential.
DR Genevisible; Q8H1Z0; AT.
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; ISS:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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:0043447; P:alkane biosynthetic process; IDA:TAIR.
DR GO; GO:0006723; P:cuticle hydrocarbon biosynthetic process; IMP:TAIR.
DR GO; GO:0048235; P:pollen sperm cell differentiation; IMP:TAIR.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0010025; P:wax biosynthetic process; IMP:TAIR.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Lyase; Membrane; NADP; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..632
FT /note="Very-long-chain aldehyde decarbonylase CER3"
FT /id="PRO_0000300114"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 133..274
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MUTAGEN 147
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:22773744"
FT MUTAGEN 161
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:22773744"
FT MUTAGEN 250
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:22773744"
FT MUTAGEN 408
FT /note="A->T: In cer3-1; reduced wax content."
FT /evidence="ECO:0000269|PubMed:17624331"
SQ SEQUENCE 632 AA; 72289 MW; 9056889F0CB4866C CRC64;
MVAFLSAWPW ENFGNLKYLL YAPLAAQVVY SWVYEEDISK VLWCIHILII CGLKALVHEL
WSVFNNMLFV TRTLRINPKG IDFKQIDHEW HWDNYIILQA IIVSLICYMS PPLMMMINSL
PLWNTKGLIA LIVLHVTFSE PLYYFLHRSF HRNNYFFTHY HSFHHSSPVP HPMTAGNATL
LENIILCVVA GVPLIGCCLF GVGSLSAIYG YAVMFDFMRC LGHCNVEIFS HKLFEILPVL
RYLIYTPTYH SLHHQEMGTN FCLFMPLFDV LGDTQNPNSW ELQKKIRLSA GERKRVPEFV
FLAHGVDVMS AMHAPFVFRS FASMPYTTRI FLLPMWPFTF CVMLGMWAWS KTFLFSFYTL
RNNLCQTWGV PRFGFQYFLP FATKGINDQI EAAILRADKI GVKVISLAAL NKNEALNGGG
TLFVNKHPDL RVRVVHGNTL TAAVILYEIP KDVNEVFLTG ATSKLGRAIA LYLCRRGVRV
LMLTLSMERF QKIQKEAPVE FQNNLVQVTK YNAAQHCKTW IVGKWLTPRE QSWAPAGTHF
HQFVVPPILK FRRNCTYGDL AAMKLPKDVE GLGTCEYTME RGVVHACHAG GVVHMLEGWK
HHEVGAIDVD RIDLVWEAAM KYGLSAVSSL TN
