ACER_ARATH
ID ACER_ARATH Reviewed; 255 AA.
AC Q94IB9; O49638;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Alkaline ceramidase {ECO:0000303|PubMed:25619405};
DE Short=AlkCDase {ECO:0000303|PubMed:25619405};
DE Short=Alkaline CDase {ECO:0000303|PubMed:25619405};
DE Short=AtACER {ECO:0000303|PubMed:25619405};
DE EC=3.5.1.- {ECO:0000305};
DE AltName: Full=Acyl-CoA independent ceramide synthase 1 {ECO:0000303|PubMed:23505340};
DE Short=AtCES1 {ECO:0000303|PubMed:23505340};
DE AltName: Full=Alkaline ceramidase YPC1 {ECO:0000303|PubMed:18643979};
DE Short=AtYPC1 {ECO:0000303|PubMed:18643979};
DE AltName: Full=Alkaline dihydroceramidase ACER {ECO:0000305};
DE AltName: Full=Alkaline phytoceramidase {ECO:0000305};
DE Short=aPHC {ECO:0000305};
GN Name=ACER {ECO:0000303|PubMed:25619405};
GN Synonyms=CES1 {ECO:0000303|PubMed:23505340},
GN YPC1 {ECO:0000303|PubMed:18643979};
GN OrderedLocusNames=At4g22330 {ECO:0000312|Araport:AT4G22330};
GN ORFNames=T10I14.160 {ECO:0000312|EMBL:CAA16783.1};
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].
RA Morimoto Y., Nishiura H., Tamura K., Mori J., Imai H.;
RT "Cloning and characterization of an Arabidopsis gene encoding an enzyme
RT involved in ceramide formation.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=18643979; DOI=10.1111/j.1365-313x.2008.03596.x;
RA Marion J., Bach L., Bellec Y., Meyer C., Gissot L., Faure J.D.;
RT "Systematic analysis of protein subcellular localization and interaction
RT using high-throughput transient transformation of Arabidopsis seedlings.";
RL Plant J. 56:169-179(2008).
RN [6]
RP REVIEW.
RX PubMed=23505340; DOI=10.1199/tab.0161;
RA Li-Beisson Y., Shorrosh B., Beisson F., Andersson M.X., Arondel V.,
RA Bates P.D., Baud S., Bird D., Debono A., Durrett T.P., Franke R.B.,
RA Graham I.A., Katayama K., Kelly A.A., Larson T., Markham J.E., Miquel M.,
RA Molina I., Nishida I., Rowland O., Samuels L., Schmid K.M., Wada H.,
RA Welti R., Xu C., Zallot R., Ohlrogge J.;
RT "Acyl-lipid metabolism.";
RL Arabidopsis Book 11:E0161-E0161(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=25619405; DOI=10.1111/tpj.12769;
RA Wu J.-X., Li J., Liu Z., Yin J., Chang Z.-Y., Rong C., Wu J.-L., Bi F.-C.,
RA Yao N.;
RT "The Arabidopsis ceramidase AtACER functions in disease resistance and salt
RT tolerance.";
RL Plant J. 81:767-780(2015).
CC -!- FUNCTION: Hydrolyzes only phytoceramide into phytosphingosine and free
CC fatty acid (PubMed:25619405). Does not have reverse activity (By
CC similarity). Affects plant morphogenesis. Required for the formation of
CC wax layer that ensure cuticle permeability. Implicated in abscisic acid
CC (ABA)-mediated stomatal closure. Involved in both biotic and abiotic
CC stresses. Promotes salt resistance and defenses responses toward
CC pathogenic bacteria (e.g. P.syringae) and against the fungal toxin
CC fumonisin B1 (FB1) (PubMed:25619405). {ECO:0000250|UniProtKB:Q9NUN7,
CC ECO:0000269|PubMed:25619405}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18643979, ECO:0000269|PubMed:25619405}; Multi-pass
CC membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:25619405}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, shoot meristems and
CC pollen, and, to a lower extent, in mature leaves.
CC {ECO:0000269|PubMed:25619405}.
CC -!- DISRUPTION PHENOTYPE: Pleiotropic phenotypes, including reduction of
CC leaf size, dwarfing, small flowers and an irregular wax layer. The
CC abnormal wax layer is associated with higher water loss and rapid
CC chlorophyll leaching due to an increased cuticle permeability.
CC Increased phytoceramides levels and decreased long chain bases.
CC Increased sensitivity to salt stress. Increased susceptibility to the
CC pathogenic bacteria P.syringae with reduced pathogenesis-related (PR)
CC genes induction. Reduced sensitivity to abscisic acid (ABA) leading to
CC impaired stomatal closure regulation. Increased sensitivity to the
CC fungal toxin fumonisin B1 (FB1)-induced cell death.
CC {ECO:0000269|PubMed:25619405}.
CC -!- SIMILARITY: Belongs to the alkaline ceramidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16783.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79188.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB063253; BAB60897.1; -; mRNA.
DR EMBL; AL021712; CAA16783.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161557; CAB79188.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84594.1; -; Genomic_DNA.
DR EMBL; BT008549; AAP40376.1; -; mRNA.
DR EMBL; BT008652; AAP40465.1; -; mRNA.
DR PIR; T04914; T04914.
DR RefSeq; NP_567660.1; NM_118359.4.
DR AlphaFoldDB; Q94IB9; -.
DR SMR; Q94IB9; -.
DR STRING; 3702.AT4G22330.1; -.
DR PaxDb; Q94IB9; -.
DR PRIDE; Q94IB9; -.
DR ProteomicsDB; 244523; -.
DR EnsemblPlants; AT4G22330.1; AT4G22330.1; AT4G22330.
DR GeneID; 828328; -.
DR Gramene; AT4G22330.1; AT4G22330.1; AT4G22330.
DR KEGG; ath:AT4G22330; -.
DR Araport; AT4G22330; -.
DR TAIR; locus:2132110; AT4G22330.
DR eggNOG; KOG2329; Eukaryota.
DR HOGENOM; CLU_063293_3_1_1; -.
DR InParanoid; Q94IB9; -.
DR OMA; IMFEPLR; -.
DR OrthoDB; 969354at2759; -.
DR PhylomeDB; Q94IB9; -.
DR BRENDA; 3.5.1.23; 399.
DR PRO; PR:Q94IB9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94IB9; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IDA:TAIR.
DR GO; GO:0006672; P:ceramide metabolic process; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0098542; P:defense response to other organism; IMP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:TAIR.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0002238; P:response to molecule of fungal origin; IMP:UniProtKB.
DR GO; GO:0031667; P:response to nutrient levels; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:TAIR.
DR GO; GO:0030104; P:water homeostasis; IMP:UniProtKB.
DR GO; GO:0010025; P:wax biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR008901; ACER.
DR InterPro; IPR044219; ACER_plant.
DR PANTHER; PTHR46852; PTHR46852; 1.
DR Pfam; PF05875; Ceramidase; 1.
PE 2: Evidence at transcript level;
KW Abscisic acid signaling pathway; Developmental protein;
KW Endoplasmic reticulum; Golgi apparatus; Hydrolase; Membrane; Metal-binding;
KW Plant defense; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..255
FT /note="Alkaline ceramidase"
FT /id="PRO_0000439758"
FT TOPO_DOM 1..28
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..91
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..205
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
SQ SEQUENCE 255 AA; 29744 MW; E4C81FA8ABC2F71E CRC64;
MADGISSFWG PVTSTIECCE MNYAYSSYIA EFYNTISNVP GILLALIGLV NALRQRFEKR
FSILHISNMI LAIGSMLYHA TLQHVQQQSD ETPMVWEILL YMYILYSPDW HYRSTMPTFL
FLYGAAFAIV HAYLRFGIGF KVHYVILCLL CIPRMYKYYI HTEDTAAKRI AKWYVATILV
GSICWFCDRV FCKTISQWPV NPQGHALWHV FMSFNSYCAN TFLMFCRAQQ RGWNPKVKYF
LGVLPYVKIE KPKTQ
