IPCS2_ARATH
ID IPCS2_ARATH Reviewed; 305 AA.
AC Q9SH93; B9DHT1;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Phosphatidylinositol:ceramide inositolphosphotransferase 2 {ECO:0000305};
DE EC=2.7.1.227 {ECO:0000269|PubMed:19001565};
DE AltName: Full=Inositol-phosphorylceramide synthase 2 {ECO:0000303|PubMed:20309609};
DE Short=AtIPCS2 {ECO:0000303|PubMed:20309609};
DE Short=IPC synthase 2 {ECO:0000303|PubMed:20309609};
DE AltName: Full=Protein ENHANCING RPW8-MEDIATED HR-LIKE CELL DEATH 1 {ECO:0000303|PubMed:19001565};
DE AltName: Full=Sphingolipid synthase 2 {ECO:0000305};
GN Name=IPCS2 {ECO:0000303|PubMed:20309609};
GN Synonyms=ERH1 {ECO:0000303|PubMed:19001565};
GN OrderedLocusNames=At2g37940 {ECO:0000312|Araport:AT2G37940};
GN ORFNames=T8P21.15 {ECO:0000305};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
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] OF 64-305.
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 FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION BY GOLOVINOMYCES
RP CICHORACEARUM AND PSEUDOMONAS SYRINGAE.
RC STRAIN=cv. Columbia;
RX PubMed=19001565; DOI=10.1105/tpc.108.060053;
RA Wang W., Yang X., Tangchaiburana S., Ndeh R., Markham J.E., Tsegaye Y.,
RA Dunn T.M., Wang G.-L., Bellizzi M., Parsons J.F., Morrissey D., Bravo J.E.,
RA Lynch D.V., Xiao S.;
RT "An inositolphosphorylceramide synthase is involved in regulation of plant
RT programmed cell death associated with defense in Arabidopsis.";
RL Plant Cell 20:3163-3179(2008).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20309609; DOI=10.1007/s11103-010-9626-3;
RA Mina J.G., Okada Y., Wansadhipathi-Kannangara N.K., Pratt S.,
RA Shams-Eldin H., Schwarz R.T., Steel P.G., Fawcett T., Denny P.W.;
RT "Functional analyses of differentially expressed isoforms of the
RT Arabidopsis inositol phosphorylceramide synthase.";
RL Plant Mol. Biol. 73:399-407(2010).
RN [7]
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 [8]
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: Catalyzes the transfer of the phosphorylinositol group from
CC phosphatidylinositol (PI) to phytoceramide, an essential step in
CC sphingolipid biosynthesis (PubMed:19001565, PubMed:20309609). May play
CC an important role in modulating plant programmed cell death (PCD)
CC associated with defense (e.g. toward Golovinomyces cichoracearum) by
CC promoting sphingolipid metabolism and thus regulating ceramide
CC accumulation (PubMed:19001565). {ECO:0000269|PubMed:19001565,
CC ECO:0000269|PubMed:20309609}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + an N-
CC (2R-hydroxy-very-long-chain fatty acyl)-(R)-4-hydroxysphingoid base =
CC a 1,2-diacyl-sn-glycerol + a 1D-myo-inositol-1-phospho-N-[(R)-2-
CC hydroxy-very-long-chain fatty acyl]-(R)-4-hydroxysphingoid base;
CC Xref=Rhea:RHEA:64536, ChEBI:CHEBI:17815, ChEBI:CHEBI:57880,
CC ChEBI:CHEBI:155886, ChEBI:CHEBI:155926; EC=2.7.1.227;
CC Evidence={ECO:0000269|PubMed:19001565};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64537;
CC Evidence={ECO:0000269|PubMed:19001565};
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:19001565}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:19001565}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19001565}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, stems, flowers and
CC siliques. {ECO:0000269|PubMed:19001565, ECO:0000269|PubMed:20309609}.
CC -!- INDUCTION: By powdery mildew (e.g. Golovinomyces cichoracearum and
CC Pseudomonas syringae) inoculation. {ECO:0000269|PubMed:19001565}.
CC -!- DISRUPTION PHENOTYPE: Constitutive RPW8-mediated HR-like cell death
CC characterized by salicylic acid (SA) accumulation, enhanced
CC transcription of RPW8 and RPW8-dependent spontaneous HR-like cell death
CC (SHL) in leaf tissues. Reduced plant stature. Sphingolipid (e.g.
CC ceramides and hydroxyceramides) accumulation associated with a reduced
CC inositol-phosphorylceramide synthase (IPCS) activity.
CC {ECO:0000269|PubMed:19001565}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000305}.
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DR EMBL; CP002685; AEC09468.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62302.1; -; Genomic_DNA.
DR EMBL; AF325083; AAK17151.1; -; mRNA.
DR EMBL; AY058059; AAL24167.1; -; mRNA.
DR EMBL; AY090297; AAL90958.1; -; mRNA.
DR EMBL; AK317636; BAH20298.1; -; mRNA.
DR PIR; A84799; A84799.
DR RefSeq; NP_001324467.1; NM_001336682.1.
DR RefSeq; NP_565875.1; NM_129350.4.
DR AlphaFoldDB; Q9SH93; -.
DR BioGRID; 3715; 13.
DR IntAct; Q9SH93; 13.
DR STRING; 3702.AT2G37940.1; -.
DR PaxDb; Q9SH93; -.
DR PRIDE; Q9SH93; -.
DR ProteomicsDB; 238949; -.
DR EnsemblPlants; AT2G37940.1; AT2G37940.1; AT2G37940.
DR EnsemblPlants; AT2G37940.2; AT2G37940.2; AT2G37940.
DR GeneID; 818371; -.
DR Gramene; AT2G37940.1; AT2G37940.1; AT2G37940.
DR Gramene; AT2G37940.2; AT2G37940.2; AT2G37940.
DR KEGG; ath:AT2G37940; -.
DR Araport; AT2G37940; -.
DR TAIR; locus:2065629; AT2G37940.
DR eggNOG; KOG3058; Eukaryota.
DR HOGENOM; CLU_078641_1_0_1; -.
DR InParanoid; Q9SH93; -.
DR OMA; WFMAIIQ; -.
DR OrthoDB; 599210at2759; -.
DR PhylomeDB; Q9SH93; -.
DR BioCyc; ARA:AT2G37940-MON; -.
DR BioCyc; MetaCyc:AT2G37940-MON; -.
DR BRENDA; 2.7.1.227; 399.
DR PRO; PR:Q9SH93; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SH93; baseline and differential.
DR Genevisible; Q9SH93; AT.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0047493; F:ceramide cholinephosphotransferase activity; IBA:GO_Central.
DR GO; GO:0045140; F:inositol phosphoceramide synthase activity; IDA:TAIR.
DR GO; GO:0033188; F:sphingomyelin synthase activity; IBA:GO_Central.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEP:TAIR.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IDA:TAIR.
DR InterPro; IPR045221; Sphingomyelin_synth-like.
DR InterPro; IPR025749; Sphingomyelin_synth-like_dom.
DR PANTHER; PTHR21290; PTHR21290; 1.
DR Pfam; PF14360; PAP2_C; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Plant defense; Reference proteome; Sphingolipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..305
FT /note="Phosphatidylinositol:ceramide
FT inositolphosphotransferase 2"
FT /id="PRO_0000419956"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 180
FT /evidence="ECO:0000250|UniProtKB:Q86VZ5"
FT ACT_SITE 221
FT /evidence="ECO:0000250|UniProtKB:Q86VZ5"
FT ACT_SITE 225
FT /evidence="ECO:0000250|UniProtKB:Q86VZ5"
SQ SEQUENCE 305 AA; 34996 MW; FE3F9001E710F1AF CRC64;
MTLYIRRESS KLWKRFCSEI STEIGLLAEN WKYLLAGLIC QYIHGLAAKG VHYIHRPGPT
LQDLGFFLLP ELGQERSYIS ETVFTSVFLS FFLWTFHPFI LKTKKIYTVL IWCRVLAFLV
ACQFLRVITF YSTQLPGPNY HCREGSKVSR LPWPKSALEV LEINPHGVMY GCGDLIFSSH
MIFTLVFVRT YQKYGTKRFI KLFGWLTAIV QSLLIIASRK HYSVDVVVAW YTVNLVVFCL
DKKLPELPDR TAVLLPVISK DRTKEENHKL LNGNGVDPAD WRPRAQVNGK IDSNGVHTDN
TMNGA
