CER1_ARATH
ID CER1_ARATH Reviewed; 625 AA.
AC F4HVY0; F4HVX9; O22681; O23679; Q0WV76; Q39045;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Very-long-chain aldehyde decarbonylase CER1 {ECO:0000305};
DE EC=4.1.99.5 {ECO:0000269|PubMed:21386033, ECO:0000269|PubMed:22773744};
DE AltName: Full=Protein ECERIFERUM 1;
GN Name=CER1; OrderedLocusNames=At1g02205; ORFNames=T7I23.10;
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] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8718622; DOI=10.2307/3870155;
RA Aarts M.G., Keijzer C.J., Stiekema W.J., Pereira A.;
RT "Molecular characterization of the CER1 gene of arabidopsis involved in
RT epicuticular wax biosynthesis and pollen fertility.";
RL Plant Cell 7:2115-2127(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Landsberg erecta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP INDUCTION BY ABIOTIC STRESSES.
RX PubMed=19819982; DOI=10.1104/pp.109.141911;
RA Kosma D.K., Bourdenx B., Bernard A., Parsons E.P., Lue S., Joubes J.,
RA Jenks M.A.;
RT "The impact of water deficiency on leaf cuticle lipids of Arabidopsis.";
RL Plant Physiol. 151:1918-1929(2009).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND INDUCTION.
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 [9]
RP FUNCTION, SUBUNIT, INTERACTION WITH CER3; CYTB5-B; CYTB5-C; CYTB5-D AND
RP CYTB5-E, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-146; HIS-159 AND
RP HIS-248.
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: Aldehyde decarbonylase involved in the conversion of
CC aldehydes to alkanes. Core component of a very-long-chain alkane
CC synthesis complex. Involved in epicuticular wax biosynthesis and pollen
CC fertility. {ECO:0000269|PubMed:21386033, ECO:0000269|PubMed:22773744,
CC ECO:0000269|PubMed:8718622}.
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:21386033, ECO:0000269|PubMed:22773744};
CC -!- SUBUNIT: Homodimer. Interacts with CER3, CYTB5-B, CYTB5-C, CYTB5-D and
CC CYTB5-E. {ECO:0000269|PubMed:22773744}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19892830, ECO:0000269|PubMed:22773744}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:19892830,
CC ECO:0000269|PubMed:22773744}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=F4HVY0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4HVY0-2; Sequence=VSP_044264;
CC Name=3;
CC IsoId=F4HVY0-3; Sequence=VSP_044263;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, stems, leaves, flowers,
CC fruits and siliques. Not detected in roots, pollen and seeds. Expressed
CC in trichomes, cotyledons, shoot apical meristem and leaf primordia.
CC Preferentially associated with young leaves rather than mature leaves.
CC Expressed in the epidermis of the stem and caulines leaves, in the
CC carpels and the sepals. {ECO:0000269|PubMed:21386033,
CC ECO:0000269|PubMed:8718622}.
CC -!- INDUCTION: Down regulated by cold and dark stresses. Up-regulated by
CC low humidity, osmotic stress and abscisic acid treatment. No effet of
CC methyl jasmonate, GA3, salicylic acid, cytokinin or auxin treatments.
CC {ECO:0000269|PubMed:19819982, ECO:0000269|PubMed:21386033}.
CC -!- DISRUPTION PHENOTYPE: Glossy stem and fruit and reduced fertility due
CC to the inability of the pollen grains to rehydrate on the stigma
CC surface. Disappearance of the wax crystals. Decreased C29, C31 and C33
CC alkane contents. Increased susceptibility to soil water deficit.
CC {ECO:0000269|PubMed:21386033, ECO:0000269|PubMed:8718622}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24374.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA11024.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA11024.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D64155; BAA11024.1; ALT_SEQ; mRNA.
DR EMBL; U40489; AAB87721.1; -; mRNA.
DR EMBL; U89959; AAC24374.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27400.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27401.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27402.1; -; Genomic_DNA.
DR EMBL; AK226895; BAE98972.1; -; mRNA.
DR RefSeq; NP_001184890.1; NM_001197961.1. [F4HVY0-2]
DR RefSeq; NP_171723.2; NM_100101.4. [F4HVY0-1]
DR RefSeq; NP_850932.2; NM_180601.2. [F4HVY0-3]
DR AlphaFoldDB; F4HVY0; -.
DR BioGRID; 22842; 7.
DR STRING; 3702.AT1G02205.3; -.
DR PaxDb; F4HVY0; -.
DR PRIDE; F4HVY0; -.
DR ProteomicsDB; 224474; -. [F4HVY0-1]
DR EnsemblPlants; AT1G02205.1; AT1G02205.1; AT1G02205. [F4HVY0-3]
DR EnsemblPlants; AT1G02205.2; AT1G02205.2; AT1G02205. [F4HVY0-1]
DR EnsemblPlants; AT1G02205.3; AT1G02205.3; AT1G02205. [F4HVY0-2]
DR GeneID; 837602; -.
DR Gramene; AT1G02205.1; AT1G02205.1; AT1G02205. [F4HVY0-3]
DR Gramene; AT1G02205.2; AT1G02205.2; AT1G02205. [F4HVY0-1]
DR Gramene; AT1G02205.3; AT1G02205.3; AT1G02205. [F4HVY0-2]
DR KEGG; ath:AT1G02205; -.
DR Araport; AT1G02205; -.
DR TAIR; locus:2827068; AT1G02205.
DR eggNOG; ENOG502QR3T; Eukaryota.
DR InParanoid; F4HVY0; -.
DR OMA; TEHECGE; -.
DR OrthoDB; 331955at2759; -.
DR PhylomeDB; F4HVY0; -.
DR BioCyc; MetaCyc:AT1G02205-MON; -.
DR PRO; PR:F4HVY0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HVY0; baseline and differential.
DR Genevisible; F4HVY0; 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; 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:0043447; P:alkane biosynthetic process; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; 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; IPR021940; Uncharacterised_Wax2_C.
DR Pfam; PF04116; FA_hydroxylase; 1.
DR Pfam; PF12076; Wax2_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Lyase; Membrane; NADP;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..625
FT /note="Very-long-chain aldehyde decarbonylase CER1"
FT /id="PRO_0000419614"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 138..272
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..173
FT /note="MATKPGVLTDWPWTPLGSFKYIVIAPWAVHSTYRFVTDDPEKRDLGYFLVFP
FT FLLFRILHNQVWISLSRYYTSSGKRRIVDKGIDFNQVDRETNWDDQILFNGVLFYIGIN
FT LLPEAKQLPWWRTDGVLMAALIHTGPVEFLYYWLHKALHHHFLYSRYHSHHHSSIVTEP
FT ITS -> MGFDQMYAA (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_044263"
FT VAR_SEQ 509
FT /note="N -> NKGFWV (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044264"
FT MUTAGEN 146
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22773744"
FT MUTAGEN 159
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22773744"
FT MUTAGEN 248
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22773744"
FT CONFLICT 114..116
FT /note="PEA -> AEG (in Ref. 2; AAB87721)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="A -> G (in Ref. 2; AAB87721)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="L -> V (in Ref. 2; AAB87721)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="L -> V (in Ref. 2; AAB87721)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="I -> R (in Ref. 1; BAA11024 and 2; AAB87721)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="A -> P (in Ref. 2; AAB87721)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="R -> S (in Ref. 1; BAA11024 and 2; AAB87721)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="N -> D (in Ref. 1; BAA11024)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="M -> T (in Ref. 1; BAA11024 and 2; AAB87721)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="Q -> K (in Ref. 1; BAA11024 and 2; AAB87721)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="H -> R (in Ref. 1; BAA11024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 72406 MW; 334088F60BF6F938 CRC64;
MATKPGVLTD WPWTPLGSFK YIVIAPWAVH STYRFVTDDP EKRDLGYFLV FPFLLFRILH
NQVWISLSRY YTSSGKRRIV DKGIDFNQVD RETNWDDQIL FNGVLFYIGI NLLPEAKQLP
WWRTDGVLMA ALIHTGPVEF LYYWLHKALH HHFLYSRYHS HHHSSIVTEP ITSVIHPFAE
HIAYFILFAI PLLTTLLTKT ASIISFAGYI IYIDFMNNMG HCNFELIPKR LFHLFPPLKF
LCYTPSYHSL HHTQFRTNYS LFMPLYDYIY GTMDESTDTL YEKTLERGDD IVDVVHLTHL
TTPESIYHLR IGLASFASYP FAYRWFMRLL WPFTSLSMIF TLFYARLFVA ERNSFNKLNL
QSWVIPRYNL QYLLKWRKEA INNMIEKAIL EADKKGVKVL SLGLMNQGEE LNRNGEVYIH
NHPDMKVRLV DGSRLAAAVV INSVPKATTS VVMTGNLTKV AYTIASALCQ RGVQVSTLRL
DEYEKIRSCV PQECRDHLVY LTSEALSSNK VWLVGEGTTR EEQEKATKGT LFIPFSQFPL
KQLRRDCIYH TTPALIVPKS LVNVHSCENW LPRKAMSATR VAGILHALEG WEMHECGTSL
LLSDLDQVWE ACLSHGFQPL LLPHH
