ID A0A137QJJ7_9AGAR Unreviewed; 500 AA.
AC A0A137QJJ7;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
GN ORFNames=AN958_08852 {ECO:0000313|EMBL:KXN87421.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN87421.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN87421.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN87421.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KQ962247; KXN87421.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137QJJ7; -.
DR STRING; 1714833.A0A137QJJ7; -.
DR OrthoDB; 9612at2759; -.
DR Proteomes; UP000070249; 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 2-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 ECO:0000313|EMBL:KXN87421.1};
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:UP000070249};
KW Transferase {ECO:0000256|PIRNR:PIRNR000439, ECO:0000313|EMBL:KXN87421.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 73..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 477..499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 437
FT /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ SEQUENCE 500 AA; 57864 MW; 30DEA1EC6AE0D8AE CRC64;
MATVISSSPP KETGFLERKR IDKFNSTEGT LFVSKPYRSK DSRKLRALIT FTPRKSVFDT
TNETSGVNEF RGFYTLFWVS IFIWTVRTYI NSIEAYGVPL NLDFAMTFSQ DAVTLAISDF
FLVMSTGFCV PFAKALSRGW IPYYWVGLTL QHILQTTILF TTITWTFNRK WPWVQSGFLT
LHSLVMVMKM HSYLTFNGHL QYTSQQSRLN SRDTTYSATI SSSITEVKET IQPPQHPLVS
HPDPSISALA KEYSDLQAEL VSLGPERVSW PNNITWKNFA VYQLIPTLIY ELEYPRTKQI
RPLYIVEKTI ATFGTFVLLY TVTETFILPL TPTSEQSFFR SLLDLALPFM MAYVLLFYII
FECICNGFAE LSYFADRQFY EDWSRWNSTS WDEFSRKWNK PVHGFLLRHV YAPLIYSCGF
SKTVAMLFTF FLSASAHELV MVVVTQKIRL YLLVMQLVQI PLILLSRHPI IKRNKLMGNV
VFWLGLYAGF PLLCVAYVAY
//