LOH1_ARATH
ID LOH1_ARATH Reviewed; 310 AA.
AC Q9LDF2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Ceramide synthase LOH1 {ECO:0000303|PubMed:25822663};
DE Short=CS1 {ECO:0000303|PubMed:23505340};
DE Short=CSII {ECO:0000303|PubMed:23499054};
DE EC=2.3.1.- {ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234, ECO:0000269|PubMed:26635357};
DE AltName: Full=Protein LONGEVITY ASSURANCE GENE ONE HOMOLOG 1 {ECO:0000303|PubMed:26276842};
DE Short=LAG One Homolog 1 {ECO:0000303|PubMed:21666002};
DE Short=LAG1 homolog 1 {ECO:0000303|PubMed:10781105};
DE Short=LAG1 longevity assurance homolog 1 {ECO:0000303|PubMed:10781105};
GN Name=LOH1 {ECO:0000303|PubMed:21666002, ECO:0000303|PubMed:25822663};
GN Synonyms=LAG1 {ECO:0000303|PubMed:10781105};
GN OrderedLocusNames=At3g25540 {ECO:0000312|Araport:AT3G25540};
GN ORFNames=MWL2.19 {ECO:0000312|EMBL:BAB01323.1};
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].
RC STRAIN=cv. Columbia;
RX PubMed=10781105; DOI=10.1073/pnas.97.9.4961;
RA Brandwagt B.F., Mesbah L.A., Takken F.L.W., Laurent P.L., Kneppers T.J.A.,
RA Hille J., Nijkamp H.J.J.;
RT "A longevity assurance gene homolog of tomato mediates resistance to
RT Alternaria alternata f. sp. lycopersici toxins and fumonisin B1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4961-4966(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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 FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=cv. Columbia;
RX PubMed=21883234; DOI=10.1111/j.1469-8137.2011.03852.x;
RA Ternes P., Feussner K., Werner S., Lerche J., Iven T., Heilmann I.,
RA Riezman H., Feussner I.;
RT "Disruption of the ceramide synthase LOH1 causes spontaneous cell death in
RT Arabidopsis thaliana.";
RL New Phytol. 192:841-854(2011).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Columbia;
RX PubMed=21666002; DOI=10.1105/tpc.110.080473;
RA Markham J.E., Molino D., Gissot L., Bellec Y., Hematy K., Marion J.,
RA Belcram K., Palauqui J.-C., Satiat-Jeunemaitre B., Faure J.-D.;
RT "Sphingolipids containing very-long-chain fatty acids define a secretory
RT pathway for specific polar plasma membrane protein targeting in
RT Arabidopsis.";
RL Plant Cell 23:2362-2378(2011).
RN [7]
RP REVIEW ON SPHINGOLIPIDS.
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 [8]
RP REVIEW ON SPHINGOLIPIDS.
RX PubMed=23499054; DOI=10.1016/j.pbi.2013.02.009;
RA Markham J.E., Lynch D.V., Napier J.A., Dunn T.M., Cahoon E.B.;
RT "Plant sphingolipids: function follows form.";
RL Curr. Opin. Plant Biol. 16:350-357(2013).
RN [9]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=25794895; DOI=10.1016/j.phytochem.2015.02.019;
RA Luttgeharm K.D., Kimberlin A.N., Cahoon R.E., Cerny R.L., Napier J.A.,
RA Markham J.E., Cahoon E.B.;
RT "Sphingolipid metabolism is strikingly different between pollen and leaf in
RT Arabidopsis as revealed by compositional and gene expression profiling.";
RL Phytochemistry 115:121-129(2015).
RN [10]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=26276842; DOI=10.1104/pp.15.00987;
RA Luttgeharm K.D., Chen M., Mehra A., Cahoon R.E., Markham J.E., Cahoon E.B.;
RT "Overexpression of Arabidopsis ceramide synthases differentially affects
RT growth, sphingolipid metabolism, programmed cell death, and mycotoxin
RT resistance.";
RL Plant Physiol. 169:1108-1117(2015).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=25822663; DOI=10.1371/journal.pgen.1005143;
RA Xie L.-J., Chen Q.-F., Chen M.-X., Yu L.-J., Huang L., Chen L., Wang F.-Z.,
RA Xia F.-N., Zhu T.-R., Wu J.-X., Yin J., Liao B., Shi J., Zhang J.-H.,
RA Aharoni A., Yao N., Shu W., Xiao S.;
RT "Unsaturation of very-long-chain ceramides protects plant from hypoxia-
RT induced damages by modulating ethylene signaling in Arabidopsis.";
RL PLoS Genet. 11:e1005143-e1005143(2015).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RX PubMed=26635357; DOI=10.1042/bj20150824;
RA Luttgeharm K.D., Cahoon E.B., Markham J.E.;
RT "Substrate specificity, kinetic properties and inhibition by fumonisin B1
RT of ceramide synthase isoforms from Arabidopsis.";
RL Biochem. J. 473:593-603(2016).
RN [13]
RP REVIEW.
RX PubMed=32407692; DOI=10.1016/j.tplants.2020.03.007;
RA Mortimer J.C., Scheller H.V.;
RT "Synthesis and function of complex sphingolipid glycosylation.";
RL Trends Plant Sci. 25:522-524(2020).
CC -!- FUNCTION: Essential for plant growth, promotes cell division in root
CC meristems (PubMed:21666002, PubMed:21883234, PubMed:26276842).
CC Catalyzes the biosynthesis of ceramide sphingolipids with C(16) to
CC C(28) fatty acids, structural membrane lipids involved in membrane
CC trafficking (e.g. early endosomes) and cell polarity (e.g. polar auxin
CC transport related proteins); mostly active with t18:0 and saturated
CC very long saturated fatty acids (C24:0 and C26:0), such as long-chain
CC base (LCB) phytosphingosine (t18:0), lignoceroyl- and hexacosanoyl-CoAs
CC (PubMed:21883234, PubMed:26635357, PubMed:21666002, PubMed:26276842).
CC Mediates resistance to sphinganine-analog mycotoxins (SAMs, e.g.
CC fumonisin B(1)) by restoring the sphingolipid biosynthesis (By
CC similarity). Could salvage the transport of GPI-anchored proteins from
CC the endoplasmic reticulum to the Golgi apparatus in ceramides-depleted
CC cells after SAM exposure (By similarity). May prevent precocious cell
CC death by delaying PR1 accumulation during aging (PubMed:21883234).
CC Contributes to hypoxic conditions tolerance (e.g. submergences),
CC especially in the dark, by promoting the formation of very-long-chain
CC (VLC) ceramide species (22:1, 24:1 and 26:1) and of VLC unsaturated
CC ceramides, which are modulating CTR1-mediated ethylene signaling
CC leading to endoplasmic reticulum (ER)-to-nucleus translocation of EIN2
CC and EIN3 (PubMed:25822663). {ECO:0000250|UniProtKB:Q9M6A3,
CC ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:25822663, ECO:0000269|PubMed:26276842,
CC ECO:0000269|PubMed:26635357}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R)-hydroxysphinganine + a fatty acyl-CoA = an N-acyl-(4R)-4-
CC hydroxysphinganine + CoA + H(+); Xref=Rhea:RHEA:35651,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:31998, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:64124, ChEBI:CHEBI:77636;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35652;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R)-hydroxysphinganine + hexacosanoyl-CoA = CoA + H(+) + N-
CC hexacosanoyl-(4R)-hydroxysphinganine; Xref=Rhea:RHEA:33339,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:52980, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:64124, ChEBI:CHEBI:64868;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33340;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R)-hydroxysphinganine + tetracosanoyl-CoA = CoA + H(+) + N-
CC tetracosanoyl-(4R)-hydroxysphinganine; Xref=Rhea:RHEA:33595,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:52979, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:64124, ChEBI:CHEBI:65052;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33596;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC -!- ACTIVITY REGULATION: Inhibited by the mycotoxin fumonisin B(1), a
CC sphingosine analog mycotoxins produced by pathogenic fungi
CC (PubMed:26276842, PubMed:26635357). Repressed by divalent cation such
CC as magnesium Mg(2+), copper Cu(2+), zinc Zn(2+), manganese Mn(2+),
CC calcium Ca(2+) and cobalt Co(2+) (PubMed:26635357).
CC {ECO:0000269|PubMed:26276842, ECO:0000269|PubMed:26635357}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.9 uM for phytosphingosine (t18:0) {ECO:0000269|PubMed:26635357};
CC Vmax=273 pmol/min/mg enzyme with phytosphingosine (t18:0) as
CC substrate {ECO:0000269|PubMed:26635357};
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:21666002,
CC ECO:0000269|PubMed:21883234, ECO:0000269|PubMed:26635357}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8C172}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously at high levels
CC (PubMed:21883234). Not observed in pollen (PubMed:25794895).
CC {ECO:0000269|PubMed:21883234, ECO:0000269|PubMed:25794895}.
CC -!- DISRUPTION PHENOTYPE: Elevated levels of free trihydroxy sphingoid
CC bases as well as ceramide and glucosylceramide species with C(16) fatty
CC acid, but reduced levels of species with C(20) to C(28) fatty acids
CC (PubMed:21883234, PubMed:25822663). Spontaneous cell death accompanied
CC by an enhanced PR1 expression at advanced age (PubMed:21883234). The
CC double mutant loh1 loh3 is embryonically lethal (PubMed:21883234,
CC PubMed:21666002). Rare viable loh1 loh3 seedlings have a complete
CC absence of very-long-chain fatty acid (VLCFA) in sphingolipids and
CC exhibit strong dwarf phenotype and altered lateral root outgrowth
CC associated with disrupted early endosomes and an impaired polar auxin
CC transport due to abnormal localization of auxin transporters in the
CC plasma membrane; these phenotypes are in part restored by external
CC auxin (NAA) (PubMed:21666002). Better resistance to submergence under
CC light conditions, but increased sensitivity to dark submergence
CC associated with declined levels of unsaturated very-long-chain (VLC)
CC ceramide species (22:1, 24:1 and 26:1) (PubMed:25822663). The double
CC mutant loh1 loh3, lacking (VLC), have an impaired tolerance to both
CC dark and light submergences (PubMed:25822663).
CC {ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:25822663}.
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DR EMBL; AF198179; AAF66102.1; -; mRNA.
DR EMBL; AB025639; BAB01323.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77023.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM66003.1; -; Genomic_DNA.
DR EMBL; AF360152; AAK25862.1; -; mRNA.
DR EMBL; AY142597; AAN13166.1; -; mRNA.
DR RefSeq; NP_001319643.1; NM_001338755.1.
DR RefSeq; NP_566769.1; NM_113450.5.
DR AlphaFoldDB; Q9LDF2; -.
DR SMR; Q9LDF2; -.
DR STRING; 3702.AT3G25540.1; -.
DR iPTMnet; Q9LDF2; -.
DR PaxDb; Q9LDF2; -.
DR PRIDE; Q9LDF2; -.
DR ProteomicsDB; 237069; -.
DR EnsemblPlants; AT3G25540.1; AT3G25540.1; AT3G25540.
DR EnsemblPlants; AT3G25540.3; AT3G25540.3; AT3G25540.
DR GeneID; 822140; -.
DR Gramene; AT3G25540.1; AT3G25540.1; AT3G25540.
DR Gramene; AT3G25540.3; AT3G25540.3; AT3G25540.
DR KEGG; ath:AT3G25540; -.
DR Araport; AT3G25540; -.
DR TAIR; locus:2094528; AT3G25540.
DR eggNOG; KOG1607; Eukaryota.
DR HOGENOM; CLU_028277_5_0_1; -.
DR InParanoid; Q9LDF2; -.
DR OMA; YSCDITF; -.
DR OrthoDB; 987268at2759; -.
DR PhylomeDB; Q9LDF2; -.
DR BioCyc; MetaCyc:MON-20773; -.
DR BRENDA; 2.3.1.297; 399.
DR PRO; PR:Q9LDF2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LDF2; baseline and differential.
DR Genevisible; Q9LDF2; AT.
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:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0050291; F:sphingosine N-acyltransferase activity; IGI:TAIR.
DR GO; GO:0046513; P:ceramide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0010256; P:endomembrane system organization; IMP:UniProtKB.
DR GO; GO:2000012; P:regulation of auxin polar transport; IMP:UniProtKB.
DR GO; GO:0006665; P:sphingolipid metabolic process; IDA:UniProtKB.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IGI:TAIR.
DR InterPro; IPR016439; Lag1/Lac1-like.
DR InterPro; IPR006634; TLC-dom.
DR PANTHER; PTHR12560; PTHR12560; 1.
DR Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR PIRSF; PIRSF005225; LAG1_LAC1; 1.
DR SMART; SM00724; TLC; 1.
DR PROSITE; PS50922; TLC; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..310
FT /note="Ceramide synthase LOH1"
FT /id="PRO_0000185518"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 76..289
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LJK3"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LJK3"
SQ SEQUENCE 310 AA; 36498 MW; B3E1F2D5D3A4AEAD CRC64;
MGLFESVKSI DWEQESFPTY QDLGFLPLFA VFFPTIRFLL DRFVFEKLAS LVIYGRMSTN
KSDNIKDRKK NSPKVRKFKE SAWKCIYYLS AELLALSVTY NEPWFSNTLY FWIGPGDQIW
PDQPMKMKLK FLYMFAAGFY TYSIFALVFW ETRRSDFGVS MGHHITTLVL IVLSYICRLT
RAGSVILALH DASDVFLEIG KMSKYCGAES LASISFVLFA LSWVVLRLIY YPFWILWSTS
YQIIMTVDKE KHPNGPILYY MFNTLLYFLL VLHIFWWVLI YRMLVKQVQD RGKLSEDVRS
DSESDDEHED
