LOH2_ARATH
ID LOH2_ARATH Reviewed; 296 AA.
AC Q9LJK3; Q9M6A2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ceramide synthase LOH2 {ECO:0000303|PubMed:25822663};
DE Short=CS2 {ECO:0000303|PubMed:23505340};
DE Short=CSI {ECO:0000303|PubMed:23499054};
DE EC=2.3.1.291 {ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234, ECO:0000269|PubMed:26635357};
DE AltName: Full=Protein LONGEVITY ASSURANCE GENE ONE HOMOLOG 2 {ECO:0000303|PubMed:26276842};
DE Short=LAG One Homolog 2 {ECO:0000303|PubMed:21666002};
DE Short=LAG1 homolog 2 {ECO:0000303|PubMed:10781105};
DE Short=LAG1 longevity assurance homolog 2 {ECO:0000303|PubMed:10781105};
GN Name=LOH2 {ECO:0000303|PubMed:21666002, ECO:0000303|PubMed:25822663};
GN Synonyms=LAG1 {ECO:0000303|PubMed:15037448},
GN LAG2 {ECO:0000312|EMBL:AAF66103.1};
GN OrderedLocusNames=At3g19260 {ECO:0000312|Araport:AT3G19260};
GN ORFNames=MVI11.18 {ECO:0000312|EMBL:BAB02967.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-291, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-291, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [9]
RP REVIEW.
RX PubMed=15037448; DOI=10.1093/aob/mch071;
RA Dunn T.M., Lynch D.V., Michaelson L.V., Napier J.A.;
RT "A post-genomic approach to understanding sphingolipid metabolism in
RT Arabidopsis thaliana.";
RL Ann. Bot. 93:483-497(2004).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=18725200; DOI=10.1016/j.bbrc.2008.08.056;
RA Gechev T.S., Ferwerda M.A., Mehterov N., Laloi C., Qureshi M.K., Hille J.;
RT "Arabidopsis AAL-toxin-resistant mutant atr1 shows enhanced tolerance to
RT programmed cell death induced by reactive oxygen species.";
RL Biochem. Biophys. Res. Commun. 375:639-644(2008).
RN [11]
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 [12]
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 [13]
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 [14]
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 [15]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=23617414; DOI=10.1094/mpmi-10-12-0253-r;
RA Mase K., Ishihama N., Mori H., Takahashi H., Kaminaka H., Kodama M.,
RA Yoshioka H.;
RT "Ethylene-responsive AP2/ERF transcription factor MACD1 participates in
RT phytotoxin-triggered programmed cell death.";
RL Mol. Plant Microbe Interact. 26:868-879(2013).
RN [16]
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 [17]
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 [18]
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 [19]
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 [20]
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: Prevents cell division in root meristems and promotes
CC salicylic acid (SA) production and hypersensitive response (HR)
CC (PubMed:26276842). Catalyzes the biosynthesis of ceramide sphingolipids
CC with C(16) 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); accepts only C16:0 fatty acids, but with a
CC wide range of d18 sphingoid bases, such as sphinganine (d18:0) and
CC palmitoyl-CoA (PubMed:21883234, PubMed:26635357, PubMed:21666002,
CC PubMed:26276842). Mediates resistance to sphinganine-analog mycotoxins
CC (SAMs, e.g. fumonisin B(1)) by restoring the sphingolipid biosynthesis
CC (PubMed:26276842). Could salvage the transport of GPI-anchored proteins
CC from the endoplasmic reticulum to the Golgi apparatus in ceramides-
CC depleted cells after SAM exposure (By similarity). Contributes to
CC hypoxic conditions tolerance (e.g. submergences), especially in the
CC dark, by promoting the formation of very-long-chain (VLC) ceramide
CC species (22:1, 24:1 and 26:1) and of VLC unsaturated ceramides, which
CC are modulating CTR1-mediated ethylene signaling leading to endoplasmic
CC reticulum (ER)-to-nucleus translocation of EIN2 and EIN3
CC (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=a sphingoid base + hexadecanoyl-CoA = an N-hexadecanoyl-
CC sphingoid base + CoA + H(+); Xref=Rhea:RHEA:61472, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:84410,
CC ChEBI:CHEBI:144703; EC=2.3.1.291;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61473;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sphinganine = CoA + H(+) + N-
CC hexadecanoylsphinganine; Xref=Rhea:RHEA:36539, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:67042; Evidence={ECO:0000269|PubMed:21666002,
CC ECO:0000269|PubMed:21883234, ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36540;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sphing-4-enine = CoA + H(+) + N-
CC hexadecanoylsphing-4-enine; Xref=Rhea:RHEA:36687, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57756,
CC ChEBI:CHEBI:72959; Evidence={ECO:0000269|PubMed:21666002,
CC ECO:0000269|PubMed:21883234, ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36688;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sphinga-(4E,8E)-dienine = CoA + H(+) + N-
CC hexadecanoylsphinga-(4E,8E)-dienine; Xref=Rhea:RHEA:65620,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:72758, ChEBI:CHEBI:157623;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65621;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sphinga-(4E,8Z)-dienine = CoA + H(+) + N-
CC hexadecanoylsphinga-(4E,8Z)-dienine; Xref=Rhea:RHEA:65624,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:157606, ChEBI:CHEBI:157624;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65625;
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). Activated by divalent cation such
CC as magnesium Mg(2+), zinc Zn(2+), manganese Mn(2+) and calcium Ca(2+)
CC (PubMed:26635357). {ECO:0000269|PubMed:26276842,
CC ECO:0000269|PubMed:26635357}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4 uM for sphinganine (d18:0) {ECO:0000269|PubMed:26635357};
CC Vmax=146 pmol/min/mg enzyme with sphinganine (d18:0) as substrate
CC {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 with highest levels in
CC pollen. {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(20) to
CC C(28) fatty acid, but reduced levels of species with C(16) fatty acids
CC (PubMed:21883234, PubMed:25822663). Better resistance to submergence
CC under 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). Increased
CC susceptibility to AAL-toxin triggering programmed cell death (PCD)
CC (PubMed:18725200, PubMed:23617414). {ECO:0000269|PubMed:18725200,
CC ECO:0000269|PubMed:21883234, ECO:0000269|PubMed:23617414,
CC ECO:0000269|PubMed:25822663}.
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DR EMBL; AF198180; AAF66103.1; -; mRNA.
DR EMBL; AP000419; BAB02967.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76214.1; -; Genomic_DNA.
DR EMBL; AK118029; BAC42661.1; -; mRNA.
DR EMBL; BT008341; AAP37700.1; -; mRNA.
DR EMBL; AY084980; AAM61539.1; -; mRNA.
DR RefSeq; NP_188557.1; NM_112813.2.
DR AlphaFoldDB; Q9LJK3; -.
DR SMR; Q9LJK3; -.
DR BioGRID; 6793; 19.
DR IntAct; Q9LJK3; 19.
DR STRING; 3702.AT3G19260.1; -.
DR iPTMnet; Q9LJK3; -.
DR PaxDb; Q9LJK3; -.
DR PRIDE; Q9LJK3; -.
DR ProteomicsDB; 250751; -.
DR EnsemblPlants; AT3G19260.1; AT3G19260.1; AT3G19260.
DR GeneID; 821460; -.
DR Gramene; AT3G19260.1; AT3G19260.1; AT3G19260.
DR KEGG; ath:AT3G19260; -.
DR Araport; AT3G19260; -.
DR TAIR; locus:2094133; AT3G19260.
DR eggNOG; KOG1607; Eukaryota.
DR HOGENOM; CLU_028277_5_0_1; -.
DR InParanoid; Q9LJK3; -.
DR OMA; IAAAWHF; -.
DR OrthoDB; 987268at2759; -.
DR PhylomeDB; Q9LJK3; -.
DR BioCyc; MetaCyc:MON-20772; -.
DR BRENDA; 2.3.1.24; 399.
DR PRO; PR:Q9LJK3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJK3; baseline and differential.
DR Genevisible; Q9LJK3; 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; IMP:TAIR.
DR GO; GO:0046513; P:ceramide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0010256; P:endomembrane system organization; ISS:UniProtKB.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IMP:TAIR.
DR GO; GO:0002238; P:response to molecule of fungal origin; IMP:TAIR.
DR GO; GO:0006665; P:sphingolipid metabolic process; IDA:UniProtKB.
DR InterPro; IPR016439; Lag1/Lac1-like.
DR InterPro; IPR006634; TLC-dom.
DR PANTHER; PTHR12560; PTHR12560; 1.
DR Pfam; PF03798; TRAM_LAG1_CLN8; 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..296
FT /note="Ceramide synthase LOH2"
FT /id="PRO_0000185519"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 71..278
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754"
FT CONFLICT 290
FT /note="D -> DY (in Ref. 1; AAF66103)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 34699 MW; 82976CAB6DF90581 CRC64;
MESVSSRGGD PVVKPSMEVW HFQIAVYFAF GFFFLRLVLD RYVFQRIALW LLSTGSAPIK
LNDAATRAKI VKCKESLWKL LYYAACDFFV LQVIYHEPWA RDIKLYFHGW PNQELKLSIK
LYYMCQCGFY VYGVAALLAW ETRRKDFAVM MSHHVITIIL LSYSYLTSFF RIGAIILALH
DASDVFMETA KIFKYSEKEF GASVCFALFA VSWLLLRLIY FPFWIIRATS IELLDYLDMT
SAEGTLMYYS FNTMLLMLLV FHIYWWYLIC AMIVRLLKNR GKVGEDIRSD SEDDDD
