ARE2_SACU7
ID ARE2_SACU7 Reviewed; 650 AA.
AC Q876L2;
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 2;
DE EC=2.3.1.-;
DE AltName: Full=Sterol-ester synthase 2;
GN Name=ARE2;
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; AY144799; AAO32363.1; -; Genomic_DNA.
DR AlphaFoldDB; Q876L2; -.
DR SMR; Q876L2; -.
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..650
FT /note="Sterol O-acyltransferase 2"
FT /id="PRO_0000207650"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 575..595
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 630..650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 41..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 531..537
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT ACT_SITE 587
FT /evidence="ECO:0000250|UniProtKB:P35610"
SQ SEQUENCE 650 AA; 74610 MW; 2F1B6654C6D9BC86 CRC64;
MDKNKDLLEN EQFLRIQKLN ASDAGKRQSI LVDNEDELYG LTSSNNSCAS EHEGEGEGED
ERPATTSSAP TQNHSAGDVA FIPGKTAEED TETVTKVVES DDQVFRTHVQ TLSSKGKSRY
RKGSSNFISF FDDMAFENRP SILDGSVNDP FKTKFVGPTL EKEIRKREKE LMAMRKNLHH
GKPAPDADAA DAPALTTTTT TTTSATSPET VVTIETTILS SNFSGLYVAF WMAIAFGAVK
ALIDYYYQHN GSFKDSEILK FMTTNLSTVA LIDLIMYLST FFVVGIQYLC KWGVLNWSST
GWAFTSIYEL LFVGFYMYLT ENILKLHWLS KIFLFLHSLV LLMKMHSFAF YNGYLWGIKQ
ELQFSKSALA KYKDSVNDPD VVDALEKSCE FCSFELNSQS LNDQTQKFPN NINVSNFFMF
TMFPTLIYQI EYPRTKEIRW VYVLEKICAI FGTIFLMMID AQILMHPVAM RALDVRNSEW
TGILDRLLKW AGLLVDIVPG FIVMYILDFY LIWDAILNCV AELTRFGDRY FYGDWWNCVS
WADFSRIWNI PVHKFLLRHV YHSSMSSFKL NKSQATLMTF FLSSVVHELA MYVIFKRLRF
YLFFFQMLQV PLVALTNTKY MKDRTVIGNV IFWLGICMGP SVMCTLYLTF