AUR1_CANAL
ID AUR1_CANAL Reviewed; 471 AA.
AC O13332; A0A1D8PN38; Q5A1Q1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Inositol phosphorylceramide synthase;
DE Short=IPC synthase;
DE EC=2.-.-.-;
DE AltName: Full=Aureobasidin A resistance protein homolog;
DE AltName: Full=Phosphatidylinositol:ceramide phosphoinositol transferase;
GN Name=AUR1; OrderedLocusNames=CAALFM_C501240WA;
GN ORFNames=CaO19.1945, CaO19.9500;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TIMM 0136;
RA Kondo A., Hashida-Okado T., Takesako K., Kato I.;
RT "Cloning of AUR1 homolog on Candida albicans.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=19047657; DOI=10.1128/aac.00633-08;
RA Aeed P.A., Young C.L., Nagiec M.M., Elhammer A.P.;
RT "Inhibition of inositol phosphorylceramide synthase by the cyclic peptide
RT aureobasidin A.";
RL Antimicrob. Agents Chemother. 53:496-504(2009).
CC -!- FUNCTION: Catalyzes the addition of a phosphorylinositol group onto
CC ceramide to form inositol phosphorylceramide, an essential step in
CC sphingolipid biosynthesis. {ECO:0000269|PubMed:19047657}.
CC -!- ACTIVITY REGULATION: Inhibited by aureobasidin A (AbA), khafrefungin
CC and rustmicin. {ECO:0000269|PubMed:19047657}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=130 uM for phosphatidylinositol {ECO:0000269|PubMed:19047657};
CC KM=3.3 uM for C(6)-NBD-ceramide {ECO:0000269|PubMed:19047657};
CC Vmax=1864 pmol/min/mg enzyme for phosphatidylinositol
CC {ECO:0000269|PubMed:19047657};
CC Vmax=884 pmol/min/mg enzyme for C(6)-NBD-ceramide
CC {ECO:0000269|PubMed:19047657};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AUR1 family. {ECO:0000305}.
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DR EMBL; AF013799; AAB67233.1; -; Genomic_DNA.
DR EMBL; CP017627; AOW29559.1; -; Genomic_DNA.
DR RefSeq; XP_715708.1; XM_710615.2.
DR AlphaFoldDB; O13332; -.
DR STRING; 237561.O13332; -.
DR BindingDB; O13332; -.
DR ChEMBL; CHEMBL1641343; -.
DR DrugBank; DB14058; Basifungin.
DR PRIDE; O13332; -.
DR GeneID; 3642617; -.
DR KEGG; cal:CAALFM_C501240WA; -.
DR CGD; CAL0000178882; AUR1.
DR VEuPathDB; FungiDB:C5_01240W_A; -.
DR eggNOG; ENOG502QPQM; Eukaryota.
DR HOGENOM; CLU_030747_2_0_1; -.
DR InParanoid; O13332; -.
DR OMA; MSHCFPQ; -.
DR OrthoDB; 1104835at2759; -.
DR BRENDA; 2.7.1.227; 1096.
DR SABIO-RK; O13332; -.
DR PRO; PR:O13332; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070916; C:inositol phosphoceramide synthase complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045140; F:inositol phosphoceramide synthase activity; ISS:CGD.
DR GO; GO:0006673; P:inositol phosphoceramide metabolic process; IBA:GO_Central.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006665; P:sphingolipid metabolic process; ISS:CGD.
DR InterPro; IPR026841; Aur1/Ipt1.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF14378; PAP2_3; 1.
DR SMART; SM00014; acidPPc; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Golgi apparatus; Lipid metabolism; Membrane;
KW Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..471
FT /note="Inositol phosphorylceramide synthase"
FT /id="PRO_0000064764"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..77
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..168
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..258
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..304
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 398..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 365
FT /note="I -> V (in Ref. 1; AAB67233)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="S -> Q (in Ref. 1; AAB67233)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="P -> S (in Ref. 1; AAB67233)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 53458 MW; 0CFE68ABF7125A7A CRC64;
MASSILRSKI IQKPYQLFHY YFLSEKAPGS TVSDLNFDTN IQTSLRKLKH HHWTVGEIFH
YGFLVSILFF VFVVFPASFF IKLPIILAFA TCFLIPLTSQ FFLPALPVFT WLALYFTCAK
IPQEWKPAIT VKVLPAMETI LYGDNLSNVL ATITTGVLDI LAWLPYGIIH FSFPFVLAAI
IFLFGPPTAL RSFGFAFGYM NLLGVLIQMA FPAAPPWYKN LHGLEPANYS MHGSPGGLGR
IDKLLGVDMY TTGFSNSSII FGAFPSLHSG CCIMEVLFLC WLFPRFKFVW VTYASWLWWS
TMYLTHHYFV DLIGGAMLSL TVFEFTKYKY LPKNKEGLFC RWSYTEIEKI DIQEIDPLSY
NYIPINSNDN ESRLYTRVYQ ESQVSPPSRA ETPEAFEMSN FSRSRQSSKT QVPLSNLTNN
DQVPGINEED EEEEGDEISS STPSVFEDEP QGSTYAASSA TSVDDLDSKR N
