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Alkaline ceramidase (AlkCDase) (Alkaline CDase) (AtACER) (EC 3.5.1.-) (Acyl-CoA independent ceramide synthase 1) (AtCES1) (Alkaline ceramidase YPC1) (AtYPC1) (Alkaline dihydroceramidase ACER) (Alkaline phytoceramidase) (aPHC)

 ACER_ARATH              Reviewed;         255 AA.
Q94IB9; O49638;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
07-JUN-2017, entry version 103.
RecName: Full=Alkaline ceramidase {ECO:0000303|PubMed:25619405};
Short=AlkCDase {ECO:0000303|PubMed:25619405};
Short=Alkaline CDase {ECO:0000303|PubMed:25619405};
Short=AtACER {ECO:0000303|PubMed:25619405};
EC=3.5.1.- {ECO:0000305};
AltName: Full=Acyl-CoA independent ceramide synthase 1 {ECO:0000303|PubMed:23505340};
Short=AtCES1 {ECO:0000303|PubMed:23505340};
AltName: Full=Alkaline ceramidase YPC1 {ECO:0000303|PubMed:18643979};
Short=AtYPC1 {ECO:0000303|PubMed:18643979};
AltName: Full=Alkaline dihydroceramidase ACER {ECO:0000305};
AltName: Full=Alkaline phytoceramidase {ECO:0000305};
Short=aPHC {ECO:0000305};
Name=ACER {ECO:0000303|PubMed:25619405};
Synonyms=CES1 {ECO:0000303|PubMed:23505340},
YPC1 {ECO:0000303|PubMed:18643979};
OrderedLocusNames=At4g22330 {ECO:0000312|Araport:AT4G22330};
ORFNames=T10I14.160 {ECO:0000312|EMBL:CAA16783.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Morimoto Y., Nishiura H., Tamura K., Mori J., Imai H.;
"Cloning and characterization of an Arabidopsis gene encoding an
enzyme involved in ceramide formation.";
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
SUBCELLULAR LOCATION.
PubMed=18643979; DOI=10.1111/j.1365-313X.2008.03596.x;
Marion J., Bach L., Bellec Y., Meyer C., Gissot L., Faure J.D.;
"Systematic analysis of protein subcellular localization and
interaction using high-throughput transient transformation of
Arabidopsis seedlings.";
Plant J. 56:169-179(2008).
[6]
REVIEW.
PubMed=23505340; DOI=10.1199/tab.0161;
Li-Beisson Y., Shorrosh B., Beisson F., Andersson M.X., Arondel V.,
Bates P.D., Baud S., Bird D., Debono A., Durrett T.P., Franke R.B.,
Graham I.A., Katayama K., Kelly A.A., Larson T., Markham J.E.,
Miquel M., Molina I., Nishida I., Rowland O., Samuels L., Schmid K.M.,
Wada H., Welti R., Xu C., Zallot R., Ohlrogge J.;
"Acyl-lipid metabolism.";
Arabidopsis Book 11:E0161-E0161(2013).
[7]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=25619405; DOI=10.1111/tpj.12769;
Wu J.-X., Li J., Liu Z., Yin J., Chang Z.-Y., Rong C., Wu J.-L.,
Bi F.-C., Yao N.;
"The Arabidopsis ceramidase AtACER functions in disease resistance and
salt tolerance.";
Plant J. 81:767-780(2015).
-!- FUNCTION: Hydrolyzes only phytoceramide into phytosphingosine and
free fatty acid (PubMed:25619405). Does not have reverse activity
(By similarity). Affects plant morphogenesis. Required for the
formation of wax layer that ensure cuticle permeability.
Implicated in abscisic acid (ABA)-mediated stomatal closure.
Involved in both biotic and abiotic stresses. Promotes salt
resistance and defenses responses toward pathogenic bacteria (e.g.
P.syringae) and against the fungal toxin fumonisin B1 (FB1)
(PubMed:25619405). {ECO:0000250|UniProtKB:Q9NUN7,
ECO:0000269|PubMed:25619405}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:18643979, ECO:0000269|PubMed:25619405}; Multi-
pass membrane protein {ECO:0000255}. Golgi apparatus membrane
{ECO:0000269|PubMed:25619405}; Multi-pass membrane protein
{ECO:0000255}.
-!- TISSUE SPECIFICITY: Mostly expressed in roots, shoot meristems and
pollen, and, to a lower extent, in mature leaves.
{ECO:0000269|PubMed:25619405}.
-!- DISRUPTION PHENOTYPE: Pleiotropic phenotypes, including reduction
of leaf size, dwarfing, small flowers and an irregular wax layer.
The abnormal wax layer is associated with higher water loss and
rapid chlorophyll leaching due to an increased cuticle
permeability. Increased phytoceramides levels and decreased long
chain bases. Increased sensitivity to salt stress. Increased
susceptibility to the pathogenic bacteria P.syringae with reduced
pathogenesis-related (PR) genes induction. Reduced sensitivity to
abscisic acid (ABA) leading to impaired stomatal closure
regulation. Increased sensitivity to the fungal toxin fumonisin B1
(FB1)-induced cell death. {ECO:0000269|PubMed:25619405}.
-!- SIMILARITY: Belongs to the alkaline ceramidase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA16783.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB79188.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AB063253; BAB60897.1; -; mRNA.
EMBL; AL021712; CAA16783.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161557; CAB79188.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE84594.1; -; Genomic_DNA.
EMBL; BT008549; AAP40376.1; -; mRNA.
EMBL; BT008652; AAP40465.1; -; mRNA.
PIR; T04914; T04914.
RefSeq; NP_567660.1; NM_118359.4.
UniGene; At.23408; -.
UniGene; At.25097; -.
STRING; 3702.AT4G22330.1; -.
EnsemblPlants; AT4G22330.1; AT4G22330.1; AT4G22330.
GeneID; 828328; -.
Gramene; AT4G22330.1; AT4G22330.1; AT4G22330.
KEGG; ath:AT4G22330; -.
Araport; AT4G22330; -.
TAIR; locus:2132110; AT4G22330.
eggNOG; KOG2329; Eukaryota.
eggNOG; ENOG4111RPN; LUCA.
HOGENOM; HOG000192011; -.
KO; K04711; -.
OMA; VFHQVMY; -.
OrthoDB; EOG09360KZL; -.
Reactome; R-ATH-1660661; Sphingolipid de novo biosynthesis.
PRO; PR:Q94IB9; -.
Proteomes; UP000006548; Chromosome 4.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006672; P:ceramide metabolic process; IEA:InterPro.
GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
GO; GO:0009814; P:defense response, incompatible interaction; IMP:TAIR.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
GO; GO:0002238; P:response to molecule of fungal origin; IMP:UniProtKB.
GO; GO:0009651; P:response to salt stress; IMP:TAIR.
GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:TAIR.
GO; GO:0030104; P:water homeostasis; IMP:UniProtKB.
GO; GO:0010025; P:wax biosynthetic process; IMP:UniProtKB.
InterPro; IPR008901; Ceramidase.
Pfam; PF05875; Ceramidase; 1.
2: Evidence at transcript level;
Abscisic acid signaling pathway; Complete proteome;
Developmental protein; Endoplasmic reticulum; Golgi apparatus;
Hydrolase; Membrane; Plant defense; Reference proteome;
Stress response; Transmembrane; Transmembrane helix.
CHAIN 1 255 Alkaline ceramidase.
/FTId=PRO_0000439758.
TOPO_DOM 1 28 Lumenal. {ECO:0000255}.
TRANSMEM 29 49 Helical. {ECO:0000255}.
TOPO_DOM 50 60 Cytoplasmic. {ECO:0000255}.
TRANSMEM 61 81 Helical. {ECO:0000255}.
TOPO_DOM 82 91 Lumenal. {ECO:0000255}.
TRANSMEM 92 112 Helical. {ECO:0000255}.
TOPO_DOM 113 118 Cytoplasmic. {ECO:0000255}.
TRANSMEM 119 139 Helical. {ECO:0000255}.
TRANSMEM 140 160 Helical. {ECO:0000255}.
TOPO_DOM 161 169 Cytoplasmic. {ECO:0000255}.
TRANSMEM 170 192 Helical. {ECO:0000255}.
TOPO_DOM 193 205 Lumenal. {ECO:0000255}.
TRANSMEM 206 226 Helical. {ECO:0000255}.
TOPO_DOM 227 255 Cytoplasmic. {ECO:0000255}.
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


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