ID A0A163JBS4_ABSGL Unreviewed; 512 AA.
AC A0A163JBS4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
GN Name=ABSGL_03801.1 scaffold 4673 {ECO:0000313|EMBL:SAL98272.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAL98272.1};
RN [1] {ECO:0000313|EMBL:SAL98272.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL98272.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-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 -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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; LT552062; SAL98272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163JBS4; -.
DR STRING; 4829.A0A163JBS4; -.
DR InParanoid; A0A163JBS4; -.
DR OMA; SCLSHDS; -.
DR OrthoDB; 9612at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProt.
DR InterPro; IPR004299; MBOAT_fam.
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; 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:UP000078561};
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 102..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 418..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 476..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 23..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 435
FT /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ SEQUENCE 512 AA; 58759 MW; 981987E1987B05AF CRC64;
MLDPETKHAE AIEQVITMST AYRRSAKVVT DSEDDQSDSR QRRDLRFTSR RVSTINEEKP
DDKKKKTAPA ATPFGPHHTI PIHTLSKASV LSKEAPPENY SGFIRLGMLV LGASNIRLMI
ENYMKYGLMI RLPHSYIPSQ DYGLFALAWL SVPLSLVVSF VVEYGMRKLA SQARNAKPDF
LKKLAVVEKV AALTHVGHLI FLLSFSSYIV YNHIYHPLVG SAVLIICLIT FLKLTSYCLV
NGELRERYVN GHNDEFYDED VAYPNNIKPS NLLYFFFAPT LCYQPSYPRT PTFRPTFFMK
RVAELVVCLV MMHVLMEQYA KPTLANSLKA LEEKNYVVIV ERVLKLSTTA VVIWLLMFYA
LFHAYLNALS ELLRFGDRTF YLAWWNSGNL ATYWRLWNRP VYLFFKRHVY LPSVQRGLPP
YVGQLLVFFV SAVLHEYMVG IPTHSVNGGA FFGMLGQIPL IAITKPLEKW RGKESALGNT
IFWIVFCVVG QPTIALMYYY QWTITHKHIE MP
//