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Database: UniProt
Entry: A0A163JBS4_ABSGL
LinkDB: A0A163JBS4_ABSGL
Original site: A0A163JBS4_ABSGL 
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
//
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