ID   ARE1_SACU7              Reviewed;         623 AA.
AC   Q876L3;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Sterol O-acyltransferase 1;
DE            EC=2.3.1.-;
DE   AltName: Full=Sterol-ester synthase 1;
GN   Name=ARE1;
OS   Saccharomyces uvarum (strain ATCC 76518 / CBS 7001 / CLIB 283 / NBRC 10550
OS   / MCYC 623 / NCYC 2669 / NRRL Y-11845) (Yeast) (Saccharomyces bayanus var.
OS   uvarum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=659244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=623-6C / CBS 9787 / CLIB 533;
RX   PubMed=12594514; DOI=10.1038/nature01419;
RA   Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.;
RT   "Yeast genome duplication was followed by asynchronous differentiation of
RT   duplicated genes.";
RL   Nature 421:848-852(2003).
CC   -!- FUNCTION: Sterol O-acyltransferase that catalyzes the formation of
CC       stery esters. {ECO:0000250|UniProtKB:P25628}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P25628}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC       Sterol o-acyltransferase subfamily. {ECO:0000305}.
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DR   EMBL; AY144798; AAO32362.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q876L3; -.
DR   SMR; Q876L3; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
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   3: Inferred from homology;
KW   Acyltransferase; Endoplasmic reticulum; Membrane; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..623
FT                   /note="Sterol O-acyltransferase 1"
FT                   /id="PRO_0000207647"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        422..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        548..568
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        603..623
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          20..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           504..510
FT                   /note="FYXDWWN motif"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   COMPBIAS        23..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        560
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
SQ   SEQUENCE   623 AA;  71794 MW;  86635C60C4741A35 CRC64;
     MTEAKELLQD ERFLKIQELN SAEPSKRHSV TYDNVILPQE SVEVSPRSST TSLEEPATTT
     ATGVAVAAAA AAAEKKKKKK GEDGDDEQDE QAEEKYPVDP RMQKYLSHLK SKSRTRVHRK
     DASKYVSFFG DVSFDPRPTL LDSAVNVPFQ TTFKGPVLEK QLKGLQQTKK GEVAAAAATA
     ATAATAAAAP PGKKLESNFS GIYVFAWMFM GWIAFRSCMD YYVSHEGGFA SMEIVQYMTS
     DLFTIALLDL ALFLSTFFVV FVHWLVKLGF IRWKWTGFVA VSLFELCFIP VSFPVYVYYF
     HFSWVTRIFL FLHSVVLLMK AHSFAFYNGY LWDIKNELEF SSNKLNKFKE SLSPETKDIL
     QKSCDFCLFE LNYQTKDNDF PNNISCSNYF MFCMFPVLVY QINYPRTSHI RWRYVLEKFC
     AIMGTIFLMM VTAQIFMHPV AMRCIEYHDT PSFGGWVPAV KQWLFLLFEM IPGFSVLYML
     TFYMIWDALL NCVAELTRFA DRYFYGDWWN CVSFEEFSRI WNVPVHKFLL RHVYHSSMGA
     LHFSKAQATL FTFLLSAVFH EIAMFAIFKE VRGYLFLFQL SQFAWTALSN TKFLRSRPQL
     SNVVFTFGVC TGPSMIMTLY LTL