ID   ARE2_CANAX              Reviewed;         609 AA.
AC   P84285;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Sterol O-acyltransferase 2;
DE            EC=2.3.1.- {ECO:0000269|PubMed:15184069};
DE   AltName: Full=ASAT;
DE   AltName: Full=Sterol-ester synthase;
GN   Name=ARE2 {ECO:0000303|PubMed:15184069};
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE, FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP   AND INDUCTION.
RC   STRAIN=ATCC 10231 / CBS 6431 / CIP 48.72 / DSM 1386 / NBRC 1594;
RX   PubMed=15184069; DOI=10.1016/j.bbrc.2004.05.076;
RA   Kim K.-Y., Shin Y.-K., Park J.-C., Kim J.-H., Yang H., Han D.-M.,
RA   Paik Y.-K.;
RT   "Molecular cloning and biochemical characterization of Candida albicans
RT   acyl-CoA:sterol acyltransferase, a potential target of antifungal agents.";
RL   Biochem. Biophys. Res. Commun. 319:911-919(2004).
CC   -!- FUNCTION: Sterol O-acyltransferase that catalyzes the formation of
CC       stery esters. {ECO:0000269|PubMed:15184069}.
CC   -!- ACTIVITY REGULATION: Inhibited by the protoberberine derivative HWY-289
CC       in a non-competitive manner. Inhibited by miconazole. Not inhibited by
CC       CI-976, polyoxin D, amphotericin B or nikkomycin Z.
CC       {ECO:0000269|PubMed:15184069}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:15184069}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- INDUCTION: Transcription is induced by HWY-289, but not by CI-976. HWY-
CC       289 may deplete protein levels causing an increase in transcription.
CC       {ECO:0000269|PubMed:15184069}.
CC   -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC       Sterol o-acyltransferase subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P84285; -.
DR   VEuPathDB; FungiDB:C2_06940C_A; -.
DR   VEuPathDB; FungiDB:CAWG_05792; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004772; F:sterol O-acyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008203; P:cholesterol metabolic process; IDA:UniProtKB.
DR   InterPro; IPR004299; MBOAT_fam.
DR   InterPro; IPR014371; Oat_ACAT_DAG_ARE.
DR   PANTHER; PTHR10408; PTHR10408; 1.
DR   Pfam; PF03062; MBOAT; 1.
DR   PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Endoplasmic reticulum; Membrane; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..609
FT                   /note="Sterol O-acyltransferase 2"
FT                   /id="PRO_0000207649"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        451..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        534..554
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        589..609
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           490..496
FT                   /note="FYXDWWN motif"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        546
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
SQ   SEQUENCE   609 AA;  71347 MW;  884CD6EEAD9C7430 CRC64;
     MGRTNTSDQL NAISDKNTKR KSLALDNEYH NNSSSEDDSS KIELSYTIPD NNNIISQETT
     TSVEDVLSLS SAPQNELRLR KQKSNNQDSP VDLNGVIVDV SKREKIFLKR KRQIDNKHGS
     DKSKYLSRFN DITFKAKSST IFESDEFYKT DFFGMYVLFW LATAFAMVNN LIHTYFENST
     PILQWTVVKV FKRDLFKVGL VDLAMYLSTY FAFFVQYACK NGYLSWKKVG WWLQAAFDGL
     FLFFWLWIAS EYCLDFPWIA KVFLVLHSLV FIMKMHSYAF YNGYLWSIYK EGLYSEKYLD
     KLTNGKVTLP KGHTKNETEK VLQESIAFTK YELEYQSHAT TENPDDHHVF DIDQTDKSIA
     KLQQEGLIKF PQNITLFNYF EYSMFPTLVY TLNFPRTKRI RWSYVFGKTF GIFGLIFLMI
     LIAENNLYPI VLRCEIARKL PVSERIPQYF FLLMDMIPPF LMVYLFTFFL IWDAILNAIA
     ELSKFADRDF YGPWWSCTDF SEFANQWNRC VHKFLLRHVY HSSISAFDVN KQSAAIITFL
     LSSLVHELVM YVIFGTLRGY LLLFQMSQIP LIIMSRSKFM KDKKVLGNII CWFGFISGPS
     IICTLYLVF