IPCS1_ARATH
ID IPCS1_ARATH Reviewed; 305 AA.
AC Q9M325; Q94AC2;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Phosphatidylinositol:ceramide inositolphosphotransferase 1;
DE EC=2.7.8.-;
DE AltName: Full=Inositol-phosphorylceramide synthase 1;
DE Short=AtIPCS1;
DE Short=IPC synthase 1;
DE AltName: Full=Protein ERH1-like2;
DE AltName: Full=Sphingolipid synthase 1;
GN Name=IPCS1; Synonyms=ERHL2; OrderedLocusNames=At3g54020;
GN ORFNames=F5K20.320;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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 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 -!- TISSUE SPECIFICITY: Expressed at low levels in roots, leaves, stems,
CC flowers and siliques. {ECO:0000269|PubMed:20309609}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000305}.
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DR EMBL; AL132960; CAB88364.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79176.1; -; Genomic_DNA.
DR EMBL; AY048287; AAK82549.1; -; mRNA.
DR EMBL; AY139802; AAM98108.1; -; mRNA.
DR PIR; T45942; T45942.
DR RefSeq; NP_190970.1; NM_115262.3.
DR AlphaFoldDB; Q9M325; -.
DR BioGRID; 9886; 22.
DR IntAct; Q9M325; 25.
DR STRING; 3702.AT3G54020.1; -.
DR PaxDb; Q9M325; -.
DR PRIDE; Q9M325; -.
DR ProteomicsDB; 238948; -.
DR EnsemblPlants; AT3G54020.1; AT3G54020.1; AT3G54020.
DR GeneID; 824569; -.
DR Gramene; AT3G54020.1; AT3G54020.1; AT3G54020.
DR KEGG; ath:AT3G54020; -.
DR Araport; AT3G54020; -.
DR TAIR; locus:2084455; AT3G54020.
DR eggNOG; KOG3058; Eukaryota.
DR HOGENOM; CLU_078641_1_0_1; -.
DR InParanoid; Q9M325; -.
DR OMA; QINGMIM; -.
DR OrthoDB; 599210at2759; -.
DR PhylomeDB; Q9M325; -.
DR BRENDA; 2.7.1.227; 399.
DR PRO; PR:Q9M325; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M325; 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 Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..305
FT /note="Phosphatidylinositol:ceramide
FT inositolphosphotransferase 1"
FT /id="PRO_0000419955"
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 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 266..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..305
FT /note="Polar 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 CONFLICT 16
FT /note="F -> Y (in Ref. 3; AAK82549)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="L -> R (in Ref. 3; AAK82549)"
FT /evidence="ECO:0000305"
FT CONFLICT 38..42
FT /note="LLCQY -> ILCQD (in Ref. 3; AAK82549)"
FT /evidence="ECO:0000305"
FT CONFLICT 49..53
FT /note="RGVHY -> KGGHD (in Ref. 3; AAK82549)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="P -> T (in Ref. 3; AAK82549)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="D -> H (in Ref. 3; AAK82549)"
FT /evidence="ECO:0000305"
FT CONFLICT 83..97
FT /note="VFTCVFLSFFLWTFH -> AVTCGFPSVFLGTSQ (in Ref. 3;
FT AAK82549)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 34857 MW; D17DCC56CCA333C2 CRC64;
MTLYIRREAS KLWRRFCSEI TTEIGLLAEN WKYLLAGLLC QYIHGLAARG VHYIHRPGPT
LQDSGFFVLP ELGQDKGFIS ETVFTCVFLS FFLWTFHPFI VKSKKIYTVL IWCRVLAFLV
ACQFLRVITF YSTQLPGPNY HCREGSELAR LPRPHNVLEV LLLNFPRGVI YGCGDLIFSS
HMIFTLVFVR TYQKYGSKRF IKLLGWVIAI LQSLLIIASR KHYTVDVVVA WYTVNLVVFF
LDKKLPELPD RTTALLPVIS KDRTKEESHK LLNGNGVDPA DRRPRAQVNG KDSNGGHTDN
ATNGT
