IPCS3_ARATH
ID IPCS3_ARATH Reviewed; 289 AA.
AC Q56Y01; F4IKQ0; Q84RI9;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Phosphatidylinositol:ceramide inositolphosphotransferase 3;
DE EC=2.7.8.-;
DE AltName: Full=Inositol-phosphorylceramide synthase 3;
DE Short=AtIPCS3;
DE Short=IPC synthase 3;
DE AltName: Full=Protein ERH1-like1;
DE AltName: Full=Sphingolipid synthase 3;
GN Name=IPCS3; Synonyms=ERHL1; OrderedLocusNames=At2g29525; ORFNames=F16P2.49;
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] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RX PubMed=12481096; DOI=10.1104/pp.010207;
RA Xiao Y.-L., Malik M., Whitelaw C.A., Town C.D.;
RT "Cloning and sequencing of cDNAs for hypothetical genes from chromosome 2
RT of Arabidopsis.";
RL Plant Physiol. 130:2118-2128(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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).
CC -!- FUNCTION: Catalyzes the transfer of the phosphorylinositol group from
CC phosphatidylinositol (PI) to phytoceramide, an essential step in
CC sphingolipid biosynthesis. {ECO:0000269|PubMed:20309609}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q56Y01-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q56Y01-2; Sequence=VSP_044382, VSP_044383;
CC Name=3;
CC IsoId=Q56Y01-3; Sequence=VSP_044380, VSP_044381;
CC -!- TISSUE SPECIFICITY: Mostly expressed in stems and flowers, and, to a
CC lower extent, in leaves, roots and siliques.
CC {ECO:0000269|PubMed:20309609}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX820662; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC004561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; AEC08263.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08264.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08265.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62493.1; -; Genomic_DNA.
DR EMBL; AY231431; AAO86859.1; -; mRNA.
DR EMBL; BX820662; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK221522; BAD94812.1; -; mRNA.
DR RefSeq; NP_001189633.1; NM_001202704.1. [Q56Y01-1]
DR RefSeq; NP_001318312.1; NM_001336212.1. [Q56Y01-1]
DR RefSeq; NP_850134.2; NM_179803.4. [Q56Y01-1]
DR RefSeq; NP_973560.1; NM_201831.2. [Q56Y01-2]
DR AlphaFoldDB; Q56Y01; -.
DR STRING; 3702.AT2G29525.1; -.
DR PaxDb; Q56Y01; -.
DR PRIDE; Q56Y01; -.
DR ProteomicsDB; 228824; -. [Q56Y01-1]
DR EnsemblPlants; AT2G29525.1; AT2G29525.1; AT2G29525. [Q56Y01-1]
DR EnsemblPlants; AT2G29525.2; AT2G29525.2; AT2G29525. [Q56Y01-2]
DR EnsemblPlants; AT2G29525.3; AT2G29525.3; AT2G29525. [Q56Y01-1]
DR EnsemblPlants; AT2G29525.4; AT2G29525.4; AT2G29525. [Q56Y01-1]
DR GeneID; 817501; -.
DR Gramene; AT2G29525.1; AT2G29525.1; AT2G29525. [Q56Y01-1]
DR Gramene; AT2G29525.2; AT2G29525.2; AT2G29525. [Q56Y01-2]
DR Gramene; AT2G29525.3; AT2G29525.3; AT2G29525. [Q56Y01-1]
DR Gramene; AT2G29525.4; AT2G29525.4; AT2G29525. [Q56Y01-1]
DR KEGG; ath:AT2G29525; -.
DR Araport; AT2G29525; -.
DR TAIR; locus:504956063; AT2G29525.
DR eggNOG; KOG3058; Eukaryota.
DR InParanoid; Q56Y01; -.
DR OMA; WLIAFVQ; -.
DR OrthoDB; 599210at2759; -.
DR PhylomeDB; Q56Y01; -.
DR BRENDA; 2.7.1.227; 399.
DR PRO; PR:Q56Y01; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q56Y01; baseline and differential.
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; IBA:GO_Central.
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: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 2: Evidence at transcript level;
KW Alternative splicing; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..289
FT /note="Phosphatidylinositol:ceramide
FT inositolphosphotransferase 3"
FT /id="PRO_0000419957"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 249..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /evidence="ECO:0000250"
FT ACT_SITE 222
FT /evidence="ECO:0000250"
FT ACT_SITE 226
FT /evidence="ECO:0000250"
FT VAR_SEQ 160..170
FT /note="VLLINFPDGVI -> FLMELYMVVEI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12481096"
FT /id="VSP_044380"
FT VAR_SEQ 171..289
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12481096"
FT /id="VSP_044381"
FT VAR_SEQ 247..251
FT /note="EMAER -> GKLAQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_044382"
FT VAR_SEQ 252..289
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_044383"
SQ SEQUENCE 289 AA; 32981 MW; F6307FADAFDCB3CC CRC64;
MPVYVDREAP KLWRRIYSEA TLEASLLAEK WKLVLAGLVF QYIHGLAAHG VHYLHRPGPT
LQDAGFFILP ALGQDKAFFS ETVFVTIFGS FILWTFHPFV SHSKKICTVL IWCRVFVYLA
ASQSLRIITF FATQLPGPNY HCREGSKLAK IPPPKNVLEV LLINFPDGVI YGCGDLIFSS
HTIFTLVFVR TYQRYGTRRW IKHLAWLMAV IQSILIIASR KHYTVDIVVA WYTVNLVMFY
VDSKLPEMAE RSSGPSPTPL LPLSTKDSKN KSKEDHQRLL NENNVADDH
