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
//