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Database: UniProt
Entry: Q2TZG3_ASPOR
LinkDB: Q2TZG3_ASPOR
Original site: Q2TZG3_ASPOR 
ID   Q2TZG3_ASPOR            Unreviewed;       669 AA.
AC   Q2TZG3;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   RecName: Full=diacylglycerol O-acyltransferase {ECO:0000256|ARBA:ARBA00013244};
DE            EC=2.3.1.20 {ECO:0000256|ARBA:ARBA00013244};
GN   ORFNames=AO090011000863 {ECO:0000313|EMBL:BAE65302.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE65302.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE65302.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- FUNCTION: Sterol O-acyltransferase that catalyzes the formation of
CC       stery esters. {ECO:0000256|ARBA:ARBA00023568}.
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC       Sterol o-acyltransferase subfamily. {ECO:0000256|ARBA:ARBA00009010}.
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DR   EMBL; AP007171; BAE65302.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2TZG3; -.
DR   STRING; 510516.Q2TZG3; -.
DR   EnsemblFungi; BAE65302; BAE65302; AO090011000863.
DR   HOGENOM; CLU_018190_3_0_1; -.
DR   OrthoDB; 9612at2759; -.
DR   Proteomes; UP000006564; Chromosome 7.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.20.120.550; Membrane associated eicosanoid/glutathione metabolism-like domain; 1.
DR   InterPro; IPR023352; MAPEG-like_dom_sf.
DR   InterPro; IPR004299; MBOAT_fam.
DR   InterPro; IPR001129; Membr-assoc_MAPEG.
DR   InterPro; IPR014371; Oat_ACAT_DAG_ARE.
DR   PANTHER; PTHR10408:SF7; DIACYLGLYCEROL O-ACYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR10408; STEROL O-ACYLTRANSFERASE; 1.
DR   Pfam; PF01124; MAPEG; 1.
DR   Pfam; PF03062; MBOAT; 1.
DR   SUPFAM; SSF161084; MAPEG domain-like; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006564};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        86..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        352..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        530..553
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        611..630
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        642..663
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   669 AA;  75918 MW;  4219793EC26E31FE CRC64;
     MNLRLIIENS MKYGVLICIR CHDYRKQDVI LGSMLFVIVP CQLFIAYVLE LAVAGRVKET
     VGRKKKDKSA EDGEREQREF RTIWRFALSF HILNTLLNLA VTSYVVYYYI HHPGIGTLCE
     VHAIIVALKN WSYAFTNRDL REAMLNPSAE SALPEIYSSC PYPRNITLGN LVYFWLAPTL
     VYQPVYPRSP EIRWSFVGKR MFEFTSLSIF IWLLSAQYAA PVLRNSIDKI AVMDITSIFE
     RVMKLSTISL IIWLAGFFAL FQSFLNALAE VLRFGDREFY LDWWNSSSLG MYWRSWNRPV
     YLFMKRHVYS PLIGRGYSPL TASTVVFLVS ALLHELLVGI PTHNMIGTEM PCECVALVGM
     LFQLPLIAIT APLEKMKDPS GKVIGNSIFW VSFCVVGQPL GALLYFFAWQ AKCEMFSRPP
     LFKSGTVVTI LIKLFSESLG RVRRRKYTYL IWMPPLALYF DWLSICNREA LKFNVIHHSC
     LGNVNTDVGS SALRMEINFA EFLTSKNPAL FMLLDPTAPR ENNQKINQHA VIGVALGAIP
     VLSFIHGLVV SGFRKEAKVP YPHTYATVEQ CKSNAKAEQF NCAQRAHANF LENAPQTILY
     TLVAGLKYPQ LATALGAVWF VARSLFLYGY VYSGKPQGKG RFLGGFFWLV QGALWGLSVF
     GVGKDLISF
//
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