ID A0A081CKQ6_PSEA2 Unreviewed; 742 AA.
AC A0A081CKQ6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Related to acyl-CoA sterol acyltransferase {ECO:0000313|EMBL:SPO48137.1};
DE SubName: Full=Sterol o-acyltransferase {ECO:0000313|EMBL:GAK67252.1};
GN ORFNames=PAN0_017d5479 {ECO:0000313|EMBL:GAK67252.1}, PSANT_05825
GN {ECO:0000313|EMBL:SPO48137.1};
OS Pseudozyma antarctica (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK67252.1, ECO:0000313|Proteomes:UP000053758};
RN [1] {ECO:0000313|Proteomes:UP000053758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10317 {ECO:0000313|Proteomes:UP000053758};
RA Saika A., Koike H., Hori T., Fukuoka T., Sato S., Habe H., Kitamoto D.,
RA Morita T.;
RT "Draft Genome Sequence of the Yeast Pseudozyma antarctica Type Strain
RT JCM10317, a Producer of the Glycolipid Biosurfactants, Mannosylerythritol
RT Lipids.";
RL Genome Announc. 2:e00878-e00814(2014).
RN [2] {ECO:0000313|EMBL:GAK67252.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK67252.1};
RA Morita T., Saika A., Koike H.;
RT "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT as a producer of lipase B which used in a wide range of industrial
RT applications.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SPO48137.1, ECO:0000313|Proteomes:UP000325008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34888 {ECO:0000313|Proteomes:UP000325008}, and ATCC34888
RC {ECO:0000313|EMBL:SPO48137.1};
RA Guldener U.;
RL Submitted (MAR-2018) 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}; 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; DF830084; GAK67252.1; -; Genomic_DNA.
DR EMBL; OOIQ01000017; SPO48137.1; -; Genomic_DNA.
DR RefSeq; XP_014654539.1; XM_014799053.1.
DR AlphaFoldDB; A0A081CKQ6; -.
DR GeneID; 26306339; -.
DR HOGENOM; CLU_018190_2_0_1; -.
DR OrthoDB; 9612at2759; -.
DR Proteomes; UP000053758; Unassembled WGS sequence.
DR Proteomes; UP000325008; 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; 3.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:GAK67252.1};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053758};
KW Transferase {ECO:0000313|EMBL:GAK67252.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 547..566
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 586..605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 692..710
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 722..741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 24..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 679
FT /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ SEQUENCE 742 AA; 83417 MW; 799E356AD2DA5941 CRC64;
MATNETSSGA RALPVEEDFV AKHPKIAQLM TDTPEDAISS AVSTPASEMV PSSELPSTPT
NGRATPSDSE PEPSVATSTL TTTISNSHGT GSSTFEFKHI GAKALSPRVG KDGAIHLKPV
AASTRSRKKM RAVVSFKPRN SHFDRFNETS SRDQFRGFFT LFWVCLALFV LNTSYTSFAS
TGQVLSLTFA TLFSRDAWIL AISDGVLIAS LFICVPFAKV CRRGWVRYWP TAVTFQHLWQ
ATLLGLVIKW ARYREWPWVQ SGFFVLHTLA MMMKIHSYMN VNGNMADTYH RMRRIEGMLE
ERVAEVEGAE AGRGDEQLHA AWGKAVRLAR NAAGFGDKDA DKATAHSLAE WSALHKQRGS
SSSRLHLGQA LNAAPQGEEP SPKLTVKDES SQARDQADSL PDPPGRKDKQ LSREEHIQLH
KNMTDKTNAE RKAGTDKDNE AKADSSLNRR RSTSRAASGA EPHQIRDPHP LSSHPDGLIS
DLAREIEVLR EDLLSSRPSS EPSPELIRQD PVMWPANLTY ANFWDYLLVP TLVYELSYPR
LKTIRPLYVL EKTLATFGTF LVIYVITEHW IMPFTPTPET PFLRTFLQLA VPMMINYLLI
FYIMFECICN AFAELTRFAD REFYLDWWNA TSMDVFSRKW NKPVHSFLLR HVYASTIAAW
GLSKSMAMFL TFLLSSLVHE LVMAIVSGKI RFYLFAAQMV QLPLIIISQI PFIKRNETLG
NMIFWIGLMA GFPLLNIGYL VY
//
