CER2_ARATH
ID CER2_ARATH Reviewed; 421 AA.
AC Q39048;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein ECERIFERUM 2;
GN Name=CER2; OrderedLocusNames=At4g24510; ORFNames=F22K18.290;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=8820603; DOI=10.1046/j.1365-313x.1996.09020137.x;
RA Negruk V., Yang P., Subramanian M., McNevin J.P., Lemieux B.;
RT "Molecular cloning and characterization of the CER2 gene of Arabidopsis
RT thaliana.";
RL Plant J. 9:137-145(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9390429; DOI=10.1104/pp.115.3.925;
RA Xia Y., Nikolau B.J., Schnable P.S.;
RT "Developmental and hormonal regulation of the arabidopsis CER2 gene that
RT codes for a nuclear-localized protein required for the normal accumulation
RT of cuticular waxes.";
RL Plant Physiol. 115:925-937(1997).
RN [3]
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 [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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17376164; DOI=10.1111/j.1365-313x.2007.03054.x;
RA Lai C., Kunst L., Jetter R.;
RT "Composition of alkyl esters in the cuticular wax on inflorescence stems of
RT Arabidopsis thaliana cer mutants.";
RL Plant J. 50:189-196(2007).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 C28 fatty acid elongation in stem. Despite its classification as a
CC BAHD acyltransferase based on sequence homology, CER2 does not seem to
CC share the catalytic mechanism of the members of the BAHD family.
CC {ECO:0000269|PubMed:17376164, ECO:0000269|PubMed:22930748,
CC ECO:0000269|PubMed:23384041}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the epidermis of stems
CC and young siliques. Expressed in flowers. {ECO:0000269|PubMed:23384041,
CC ECO:0000269|PubMed:8820603}.
CC -!- DISRUPTION PHENOTYPE: Bright green and glossy stems and siliques due to
CC low abundance of cuticular wax. Increased levels of C26 and C28
CC alcohols and disappearance of C29 alkane and C30 alcohol in the stem
CC wax. {ECO:0000269|PubMed:17376164, ECO:0000269|PubMed:8820603,
CC ECO:0000269|PubMed:9390429}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; X93080; CAA63618.1; -; Genomic_DNA.
DR EMBL; U40849; AAB17946.1; -; Genomic_DNA.
DR EMBL; BT026481; ABH04588.1; -; mRNA.
DR EMBL; AL035356; CAA23012.1; -; Genomic_DNA.
DR EMBL; AL161561; CAB79361.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84918.1; -; Genomic_DNA.
DR EMBL; AY087262; AAM64817.1; -; mRNA.
DR PIR; T05583; T05583.
DR RefSeq; NP_194182.1; NM_118584.3.
DR AlphaFoldDB; Q39048; -.
DR SMR; Q39048; -.
DR BioGRID; 13842; 10.
DR STRING; 3702.AT4G24510.1; -.
DR iPTMnet; Q39048; -.
DR PaxDb; Q39048; -.
DR PRIDE; Q39048; -.
DR ProteomicsDB; 220610; -.
DR EnsemblPlants; AT4G24510.1; AT4G24510.1; AT4G24510.
DR GeneID; 828553; -.
DR Gramene; AT4G24510.1; AT4G24510.1; AT4G24510.
DR KEGG; ath:AT4G24510; -.
DR Araport; AT4G24510; -.
DR TAIR; locus:2005499; AT4G24510.
DR eggNOG; ENOG502QQYP; Eukaryota.
DR HOGENOM; CLU_049517_0_0_1; -.
DR InParanoid; Q39048; -.
DR OMA; TNVITIC; -.
DR OrthoDB; 720734at2759; -.
DR PhylomeDB; Q39048; -.
DR PRO; PR:Q39048; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q39048; baseline and differential.
DR Genevisible; Q39048; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IDA:TAIR.
DR GO; GO:0010025; P:wax biosynthetic process; IMP:TAIR.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW Acetylation; Cell wall biogenesis/degradation; Endoplasmic reticulum;
KW Nucleus; Reference proteome.
FT CHAIN 1..421
FT /note="Protein ECERIFERUM 2"
FT /id="PRO_0000424432"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 421 AA; 47238 MW; 99C0CAE2A2EB6E19 CRC64;
MEGSPVTSVR LSSVVPASVV GENKPRQLTP MDLAMKLHYV RAVYFFKGAR DFTVADVKNT
MFTLQSLLQS YHHVSGRIRM SDNDNDTSAA AIPYIRCNDS GIRVVEANVE EFTVEKWLEL
DDRSIDHRFL VYDHVLGPDL TFSPLVFLQI TQFKCGGLCI GLSWAHILGD VFSASTFMKT
LGQLVSGHAP TKPVYPKTPE LTSHARNDGE AISIEKIDSV GEYWLLTNKC KMGRHIFNFS
LNHIDSLMAK YTTRDQPFSE VDILYALIWK SLLNIRGETN TNVITICDRK KSSTCWNEDL
VISVVEKNDE MVGISELAAL IAGEKREENG AIKRMIEQDK GSSDFFTYGA NLTFVNLDEI
DMYELEINGG KPDFVNYTIH GVGDKGVVLV FPKQNFARIV SVVMPEEDLA KLKEEVTNMI
I
