LOH3_ARATH
ID LOH3_ARATH Reviewed; 308 AA.
AC Q6NQI8; C0Z2Q8; Q9FZ69; Q9LMZ0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ceramide synthase 1 LOH3 {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:21883234, ECO:0000269|PubMed:26635357};
DE AltName: Full=Protein LONGEVITY ASSURANCE GENE ONE HOMOLOG 3 {ECO:0000303|PubMed:26276842};
DE Short=LAG One Homolog 3 {ECO:0000303|PubMed:21666002};
DE Short=LAG1 homolog 3 {ECO:0000305};
DE Short=LAG1 longevity assurance homolog 3 {ECO:0000305};
GN Name=LOH3 {ECO:0000303|PubMed:21666002, ECO:0000303|PubMed:25822663};
GN Synonyms=LAC1 {ECO:0000303|PubMed:15037448};
GN OrderedLocusNames=At1g13580 {ECO:0000312|Araport:AT1G13580};
GN ORFNames=F13B4.7 {ECO:0000312|EMBL:AAF99825.1},
GN F21F23.1 {ECO:0000312|EMBL:AAF81284.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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); active on a broad substrate spectrum, both
CC regarding chain lengths of fatty acids and the sphingoid base, such as
CC long-chain base (LCB) phytosphingosine (t18:0) (PubMed:21883234,
CC PubMed:26635357, PubMed:21666002, PubMed:26276842). Mediates resistance
CC to sphinganine-analog mycotoxins (SAMs, e.g. fumonisin B(1)) by
CC restoring the sphingolipid biosynthesis (PubMed:26276842). Could
CC salvage the transport of GPI-anchored proteins from the endoplasmic
CC reticulum to the Golgi apparatus in ceramides-depleted cells after SAM
CC exposure (By similarity). Contributes to hypoxic conditions tolerance
CC (e.g. submergences), especially in the dark, by promoting the formation
CC of very-long-chain (VLC) ceramide species (22:1, 24:1 and 26:1) and of
CC VLC unsaturated ceramides, which are modulating CTR1-mediated ethylene
CC signaling leading to endoplasmic reticulum (ER)-to-nucleus
CC translocation of EIN2 and EIN3 (PubMed:25822663).
CC {ECO:0000250|UniProtKB:Q9M6A3, ECO:0000269|PubMed:21666002,
CC ECO:0000269|PubMed:21883234, ECO:0000269|PubMed:25822663,
CC ECO:0000269|PubMed:26276842, 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=a sphingoid base + tetracosanoyl-CoA = an N-tetracosanoyl-
CC sphingoid base + CoA + H(+); Xref=Rhea:RHEA:65632, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:65052, ChEBI:CHEBI:84410,
CC ChEBI:CHEBI:157596; Evidence={ECO:0000269|PubMed:21666002,
CC ECO:0000269|PubMed:21883234, ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65633;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R)-hydroxysphinganine + hexadecanoyl-CoA = CoA + H(+) + N-
CC hexadecanoyl-(4R)-hydroxysphinganine; Xref=Rhea:RHEA:64008,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64124, ChEBI:CHEBI:65107;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64009;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R)-hydroxysphinganine + octadecanoyl-CoA = CoA + H(+) + N-
CC octadecanoyl-(4R)-hydroxysphinganine; Xref=Rhea:RHEA:64000,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:64124, ChEBI:CHEBI:67035;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64001;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R)-hydroxysphinganine + eicosanoyl-CoA = CoA + H(+) + N-
CC eicosanoyl-(4R)-hydroxysphinganine; Xref=Rhea:RHEA:65604,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380,
CC ChEBI:CHEBI:64124, ChEBI:CHEBI:67029;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65605;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R)-hydroxysphinganine + docosanoyl-CoA = CoA + H(+) + N-
CC docosanoyl-(4R)-hydroxysphinganine; Xref=Rhea:RHEA:65608,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:64124,
CC ChEBI:CHEBI:65059, ChEBI:CHEBI:67024;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65609;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=sphing-4-enine + tetracosanoyl-CoA = CoA + H(+) + N-
CC tetracosanoyl-sphing-4-enine; Xref=Rhea:RHEA:37115,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57756,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:72965;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37116;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sphinga-(4E,8Z)-dienine + tetracosanoyl-CoA = CoA + H(+) + N-
CC tetracosanoylsphinga-(4E,8Z)-dienine; Xref=Rhea:RHEA:65628,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052,
CC ChEBI:CHEBI:157606, ChEBI:CHEBI:157626;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65629;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sphinga-(4E,8E)-dienine + tetracosanoyl-CoA = CoA + H(+) + N-
CC tetracosanoylsphinga-(4E,8E)-dienine; Xref=Rhea:RHEA:65636,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052,
CC ChEBI:CHEBI:72758, ChEBI:CHEBI:157628;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65637;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R)-hydroxysphing-(8Z)-enine + tetracosanoyl-CoA = CoA + H(+)
CC + N-tetracosanoyl-(4R)-hydroxysphing-(8Z)-enine;
CC Xref=Rhea:RHEA:65640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:157607, ChEBI:CHEBI:157621;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65641;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R)-hydroxysphing-(8E)-enine + tetracosanoyl-CoA = CoA + H(+)
CC + N-tetracosanoyl-(4R)-hydroxysphing-(8E)-enine;
CC Xref=Rhea:RHEA:65644, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:83175, ChEBI:CHEBI:157620;
CC Evidence={ECO:0000269|PubMed:21666002, ECO:0000269|PubMed:21883234,
CC ECO:0000269|PubMed:26635357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65645;
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=23 uM for phytosphingosine (t18:0) {ECO:0000269|PubMed:26635357};
CC Vmax=395 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NQI8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NQI8-2; Sequence=VSP_013449, VSP_013450;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously at low levels
CC (PubMed:21883234). Not observed in pollen (PubMed:25794895).
CC {ECO:0000269|PubMed:21883234, ECO:0000269|PubMed:25794895}.
CC -!- DISRUPTION PHENOTYPE: No visible impact on ceramide and
CC glucosylceramide species with C(14) to C(28) fatty acids
CC (PubMed:21883234). The double mutant loh1 loh3 is embryonically lethal
CC (PubMed:21883234, PubMed:21666002). Rare viable loh1 loh3 seedlings
CC have a complete absence of very-long-chain fatty acid (VLCFA) in
CC sphingolipids and exhibit strong dwarf phenotype and altered lateral
CC root outgrowth associated with disrupted early endosomes and an
CC impaired polar auxin transport due to abnormal localization of auxin
CC transporters in the plasma membrane; these phenotypes are in part
CC restored by external auxin (NAA) (PubMed:21666002). Better resistance
CC to submergence under light conditions, but increased sensitivity to
CC dark submergence associated with declined levels of unsaturated very-
CC long-chain (VLC) ceramide species (22:1, 24:1 and 26:1)
CC (PubMed:25822663). The double mutant loh1 loh3, lacking (VLC)
CC ceramides, have an impaired tolerance to both dark and light
CC submergences (PubMed:25822663). {ECO:0000269|PubMed:21666002,
CC ECO:0000269|PubMed:21883234, ECO:0000269|PubMed:25822663}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
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DR EMBL; AC027134; AAF99825.1; -; Genomic_DNA.
DR EMBL; AC027656; AAF81284.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29036.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29037.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29038.1; -; Genomic_DNA.
DR EMBL; BT010465; AAQ65088.1; -; mRNA.
DR EMBL; AK318872; BAH56987.1; -; mRNA.
DR PIR; H86268; H86268.
DR RefSeq; NP_001031037.1; NM_001035960.2. [Q6NQI8-1]
DR RefSeq; NP_001184985.1; NM_001198056.2. [Q6NQI8-1]
DR RefSeq; NP_172815.2; NM_101228.2. [Q6NQI8-2]
DR AlphaFoldDB; Q6NQI8; -.
DR SMR; Q6NQI8; -.
DR BioGRID; 23159; 9.
DR IntAct; Q6NQI8; 9.
DR STRING; 3702.AT1G13580.3; -.
DR iPTMnet; Q6NQI8; -.
DR PaxDb; Q6NQI8; -.
DR PRIDE; Q6NQI8; -.
DR ProteomicsDB; 250716; -. [Q6NQI8-1]
DR EnsemblPlants; AT1G13580.1; AT1G13580.1; AT1G13580. [Q6NQI8-2]
DR EnsemblPlants; AT1G13580.2; AT1G13580.2; AT1G13580. [Q6NQI8-1]
DR EnsemblPlants; AT1G13580.3; AT1G13580.3; AT1G13580. [Q6NQI8-1]
DR GeneID; 837919; -.
DR Gramene; AT1G13580.1; AT1G13580.1; AT1G13580. [Q6NQI8-2]
DR Gramene; AT1G13580.2; AT1G13580.2; AT1G13580. [Q6NQI8-1]
DR Gramene; AT1G13580.3; AT1G13580.3; AT1G13580. [Q6NQI8-1]
DR KEGG; ath:AT1G13580; -.
DR Araport; AT1G13580; -.
DR TAIR; locus:2010022; AT1G13580.
DR eggNOG; KOG1607; Eukaryota.
DR HOGENOM; CLU_028277_5_0_1; -.
DR InParanoid; Q6NQI8; -.
DR OMA; FRIAYRF; -.
DR PhylomeDB; Q6NQI8; -.
DR BioCyc; MetaCyc:MON-20774; -.
DR BRENDA; 2.3.1.297; 399.
DR PRO; PR:Q6NQI8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NQI8; baseline and differential.
DR Genevisible; Q6NQI8; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Alternative splicing; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..308
FT /note="Ceramide synthase 1 LOH3"
FT /id="PRO_0000185520"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 73..287
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LJK3"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LJK3"
FT VAR_SEQ 237..239
FT /note="SYE -> RFV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_013449"
FT VAR_SEQ 240..308
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_013450"
FT CONFLICT 175
FT /note="S -> G (in Ref. 4; BAH56987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 36549 MW; 8BA12E36050A6B50 CRC64;
MGLLESVKSI NWEHESSPVY QDFRVLPLFA VFFPSIRFLL DRFVFEKLAK YLIYGKHRQD
MGDDTTERKK KIRKFKESAW KCVYYLSAEI LALSVTYNEP WFMNTKYFWV GPGDQTWPDQ
QTKLKLKLLY MFVAGFYTYS IFALVFWETR RSDFGVSMGH HIATLILIVL SYVCSFSRVG
SVVLALHDAS DVFLEVGKMS KYSGAERIAS FSFILFVLSW IILRLIYYPF WILWSTSYEV
VLELDKDKHP IEGPIYYYMF NTLLYCLLVL HIYWWVLMYR MLVKQIQDRG KLSEDVRSDS
EGEDEHED
