AUR1_SCHPO
ID AUR1_SCHPO Reviewed; 422 AA.
AC Q10142; P79014;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Inositol phosphorylceramide synthase catalytic subunit aur1;
DE Short=IPC synthase catalytic subunit aur1;
DE EC=2.-.-.-;
DE AltName: Full=Aureobasidin A resistance protein homolog;
DE AltName: Full=Phosphatidylinositol:ceramide phosphoinositol transferase;
GN Name=aur1; ORFNames=SPAC3H8.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-240.
RC STRAIN=JY745;
RX PubMed=9472078; DOI=10.1007/s002940050306;
RA Hashida-Okado T., Yasumoto R., Endo M., Takesako K., Kato I.;
RT "Isolation and characterization of the aureobasidin A-resistant gene,
RT aur1R, on Schizosaccharomyces pombe: roles of Aur1p+ in cell
RT morphogenesis.";
RL Curr. Genet. 33:38-45(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Catalytic component of the inositol phosphorylceramide
CC synthase which catalyzes the addition of a phosphorylinositol group
CC onto ceramide to form inositol phosphorylceramide, an essential step in
CC sphingolipid biosynthesis. {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Inhibited by aureobasidin A (AbA).
CC -!- SUBUNIT: Component of the inositol phosphorylceramide synthase complex
CC composed of at least aur1 and kei1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AUR1 family. {ECO:0000305}.
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DR EMBL; AB000821; BAA19190.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA93163.1; -; Genomic_DNA.
DR PIR; T38764; T38764.
DR RefSeq; NP_592999.1; NM_001018398.2.
DR AlphaFoldDB; Q10142; -.
DR BioGRID; 280046; 1.
DR STRING; 4896.SPAC3H8.06.1; -.
DR iPTMnet; Q10142; -.
DR PaxDb; Q10142; -.
DR PRIDE; Q10142; -.
DR EnsemblFungi; SPAC3H8.06.1; SPAC3H8.06.1:pep; SPAC3H8.06.
DR GeneID; 2543632; -.
DR KEGG; spo:SPAC3H8.06; -.
DR PomBase; SPAC3H8.06; aur1.
DR VEuPathDB; FungiDB:SPAC3H8.06; -.
DR eggNOG; ENOG502QPQM; Eukaryota.
DR HOGENOM; CLU_030747_2_0_1; -.
DR InParanoid; Q10142; -.
DR OMA; CWCTMYL; -.
DR PhylomeDB; Q10142; -.
DR PRO; PR:Q10142; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070916; C:inositol phosphoceramide synthase complex; ISO:PomBase.
DR GO; GO:0030173; C:integral component of Golgi membrane; NAS:PomBase.
DR GO; GO:0045140; F:inositol phosphoceramide synthase activity; ISO:PomBase.
DR GO; GO:0006673; P:inositol phosphoceramide metabolic process; ISS:PomBase.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; ISO:PomBase.
DR InterPro; IPR026841; Aur1/Ipt1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF14378; PAP2_3; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Golgi apparatus; Lipid metabolism; Membrane; Phosphoprotein;
KW Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..422
FT /note="Inositol phosphorylceramide synthase catalytic
FT subunit aur1"
FT /id="PRO_0000064765"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..159
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..245
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 275..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 386..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 240
FT /note="G->C: In aur1-1; AbA resistant."
FT /evidence="ECO:0000269|PubMed:9472078"
SQ SEQUENCE 422 AA; 47444 MW; C24EC4E3423E442E CRC64;
MSALSTLKKR LAACNRASQY KLETSLNPMP TFRLLRNTKW SWTHLQYVFL AGNLIFACIV
IESPGFWGKF GIACLLAIAL TVPLTRQIFF PAIVIITWAI LFYSCRFIPE RWRPPIWVRV
LPTLENILYG SNLSSLLSKT THSILDILAW VPYGVMHYSA PFIISFILFI FAPPGTLPVW
ARTFGYMNLF GVLIQMAFPC SPPWYENMYG LEPATYAVRG SPGGLARIDA LFGTSIYTDG
FSNSPVVFGA FPSLHAGWAM LEALFLSHVF PRYRFCFYGY VLWLCWCTMY LTHHYFVDLV
GGMCLAIICF VFAQKLRLPQ LQTGKILRWE YEFVIHGHGL SEKTSNSLAR TGSPYLLGRD
SFTQNPNAVA FMSGLNNMEL ANTDHEWSVG SSSPEPLPSP AADLIDRPAS TTSSIFDASH
LP
