ID A0A067PCQ8_PLEOS Unreviewed; 585 AA.
AC A0A067PCQ8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
GN ORFNames=PLEOSDRAFT_1061317 {ECO:0000313|EMBL:KDQ33671.1};
OS Pleurotus ostreatus PC15.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ33671.1, ECO:0000313|Proteomes:UP000027073};
RN [1] {ECO:0000313|Proteomes:UP000027073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC -!- FUNCTION: Sterol O-acyltransferase that catalyzes the formation of
CC stery esters. {ECO:0000256|ARBA:ARBA00023568}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|PIRNR:PIRNR000439}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|PIRNR:PIRNR000439}. 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,
CC ECO:0000256|PIRNR:PIRNR000439}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL198004; KDQ33671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067PCQ8; -.
DR STRING; 1137138.A0A067PCQ8; -.
DR VEuPathDB; FungiDB:PLEOSDRAFT_1061317; -.
DR HOGENOM; CLU_018190_2_0_1; -.
DR InParanoid; A0A067PCQ8; -.
DR OrthoDB; 9612at2759; -.
DR Proteomes; UP000027073; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; STEROL O-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10408:SF9; STEROL O-ACYLTRANSFERASE 1-RELATED; 1.
DR Pfam; PF03062; MBOAT; 1.
DR PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|PIRNR:PIRNR000439};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000439};
KW Reference proteome {ECO:0000313|Proteomes:UP000027073};
KW Transferase {ECO:0000256|PIRNR:PIRNR000439};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 66..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 434..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 510..529
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 535..553
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 565..584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 235..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 522
FT /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ SEQUENCE 585 AA; 65876 MW; 1E5394605BE000F3 CRC64;
MPVDAAPANT RTHSGGFKTS EGTIYVSKPF RSKTSKKLRA LVTFAPRTSV FDTNNATSGQ
NEFRGFFSLF WVSIFLFTIS TYIRSLETNG YILNLHFATM FSRDAITLAI SDAILVASTA
LCVPFAKAIS RGWINYYYTG IILQHTLQAT VLFTTVTWTF NRQWPWVQSG FLTLHSLVMM
MKMHSYMTVN GELKYIHDQA QILEEDLRKR TARLGGYEKA VADAKAHRAE IDFNATATNS
SNTSDREETP LSMTPLAPEG MQSSYMDASA ASVLRKRLIA AEKQGNGNGT TLSSSSETGN
ATVTTGGGEG AGAQTGEALH VHPLVDHPDQ EVSAMAADLT ELRTELSTRG PYPVKWPENI
TLKNFAVYQL VPTLVYELEY PRTERIRPLY VFEKTVATFG TFALLYTVTE TFILPHVPTL
KEQSFFRSLL DLSIPFMMAY LLLFFIIFEC ICNGFAELSY FADRGFYEDW WNSTSWDEFS
RKWNKPVHTF LLRHVYASTI TSYKLSRRNA MIVTFLLSAC AHELVMVVVT QKIRMYLFLL
QLAQIPLIAI SRIPVIKKNK LLGNVVFWIG LYAGFPLLCV AYCAY
//