CER26_ARATH
ID CER26_ARATH Reviewed; 428 AA.
AC Q9SVM9;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Protein ECERIFERUM 26;
DE AltName: Full=CER2-like protein 1;
DE Short=CER2-like1;
GN Name=CER26; OrderedLocusNames=At4g13840; ORFNames=F18A5.230;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22930748; DOI=10.1104/pp.112.201640;
RA Haslam T.M., Manas-Fernandez A., Zhao L., Kunst L.;
RT "Arabidopsis ECERIFERUM2 is a component of the fatty acid elongation
RT machinery required for fatty acid extension to exceptional lengths.";
RL Plant Physiol. 160:1164-1174(2012).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23384041; DOI=10.1111/tpj.12060;
RA Pascal S., Bernard A., Sorel M., Pervent M., Vile D., Haslam R.P.,
RA Napier J.A., Lessire R., Domergue F., Joubes J.;
RT "The Arabidopsis cer26 mutant, like the cer2 mutant, is specifically
RT affected in the very long chain fatty acid elongation process.";
RL Plant J. 73:733-746(2013).
CC -!- FUNCTION: Involved in biosynthesis of the epicuticular wax. Plays a
CC role in very-long-chain fatty acid (VLCFA) biosynthesis and is required
CC for C30 fatty acid elongation in leaf. Despite its classification as a
CC BAHD acyltransferase based on sequence homology, CER26 does not seem to
CC share the catalytic mechanism of the members of the BAHD family.
CC {ECO:0000269|PubMed:22930748, ECO:0000269|PubMed:23384041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23384041}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves.
CC {ECO:0000269|PubMed:22930748, ECO:0000269|PubMed:23384041}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have increased levels of C29 alkane and
CC reduced levels of C31 alkane in the rosette leaf wax.
CC {ECO:0000269|PubMed:22930748, ECO:0000269|PubMed:23384041}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AL035528; CAB36848.1; -; Genomic_DNA.
DR EMBL; AL161537; CAB78426.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83332.1; -; Genomic_DNA.
DR EMBL; AF446369; AAL48240.1; -; mRNA.
DR EMBL; BT000594; AAN18163.1; -; mRNA.
DR EMBL; AK226224; BAE98388.1; -; mRNA.
DR PIR; T05253; T05253.
DR RefSeq; NP_193120.1; NM_117458.4.
DR AlphaFoldDB; Q9SVM9; -.
DR SMR; Q9SVM9; -.
DR BioGRID; 12315; 4.
DR STRING; 3702.AT4G13840.1; -.
DR iPTMnet; Q9SVM9; -.
DR PaxDb; Q9SVM9; -.
DR PRIDE; Q9SVM9; -.
DR ProteomicsDB; 220609; -.
DR EnsemblPlants; AT4G13840.1; AT4G13840.1; AT4G13840.
DR GeneID; 827018; -.
DR Gramene; AT4G13840.1; AT4G13840.1; AT4G13840.
DR KEGG; ath:AT4G13840; -.
DR Araport; AT4G13840; -.
DR TAIR; locus:2119480; AT4G13840.
DR eggNOG; ENOG502QQYP; Eukaryota.
DR HOGENOM; CLU_049517_0_0_1; -.
DR InParanoid; Q9SVM9; -.
DR OMA; IYVQMTR; -.
DR OrthoDB; 720734at2759; -.
DR PhylomeDB; Q9SVM9; -.
DR BRENDA; 2.3.1.199; 399.
DR PRO; PR:Q9SVM9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SVM9; baseline and differential.
DR Genevisible; Q9SVM9; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010025; P:wax biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Cytoplasm; Reference proteome.
FT CHAIN 1..428
FT /note="Protein ECERIFERUM 26"
FT /id="PRO_0000424433"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 47455 MW; C85B31043E9C9B40 CRC64;
MGRSQEQGQG QGPVHSIRLS TVGATRPTET GTTHEPTGLD LAMKLHYLKA AYIYSAETAR
DLTVRHLKEA MFMLFDQIAW TTGRFSRRDS GRPYIKCNDC GTRFVEGQCN LTVEEWLSKP
DRSVDEFLVY HHPIGPELTF SPLIYVQMTR FKCGGLGLGL SWANIIGDAF SLFYAFNLWA
KAITGEKIYA PTTPSIGERR FQSPNPTVKD PVSIKRVEPV GDLWVTPNDK KLANYCFNLS
VADQISPHFP AKGDDSIPVF EILAGIIWKC IAKVRVEPKP VTVTIIKKDP NDLKLNAIRN
SQVISSVSVD FPVAEATVEE LVKAMGEAKD ERCGIEEIGE SCDGNLDFVV YGAKLTFLDL
TGEDLYEAKV MGKSPESVYC NVEGIGEEGL VVVYAAAKSE ERVVTVTLPE EEMERVKLEF
KKFGLIAP
