GenomeNet

Database: UniProt
Entry: B8M842_TALSN
LinkDB: B8M842_TALSN
Original site: B8M842_TALSN 
ID   B8M842_TALSN            Unreviewed;       534 AA.
AC   B8M842;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
GN   ORFNames=TSTA_032590 {ECO:0000313|EMBL:EED20004.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED20004.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962654; EED20004.1; -; Genomic_DNA.
DR   RefSeq; XP_002480438.1; XM_002480393.1.
DR   AlphaFoldDB; B8M842; -.
DR   STRING; 441959.B8M842; -.
DR   GeneID; 8099872; -.
DR   VEuPathDB; FungiDB:TSTA_032590; -.
DR   eggNOG; KOG0380; Eukaryota.
DR   InParanoid; B8M842; -.
DR   OMA; FICQMLQ; -.
DR   OrthoDB; 9612at2759; -.
DR   PhylomeDB; B8M842; -.
DR   Proteomes; UP000001745; 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:SF26; O-ACYLTRANSFERASE; 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   ECO:0000313|EMBL:EED20004.1};
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:UP000001745};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000439, ECO:0000313|EMBL:EED20004.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        204..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        330..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        383..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        452..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        482..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        511..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          28..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        471
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ   SEQUENCE   534 AA;  61145 MW;  748DCF44FF20AAD3 CRC64;
     MSTATSNGSM TSQVLRARAI KSLQAADERL GTSNSIPDKE NADSSGASTP VPEDAPPSVK
     SISTARKQVR ARRRLFHTID YIPRVSHFDP QSDYHNFRGF FTLFWIGLFI MVVTTVLRNI
     KDTGHPLRVK MWSLLTANVW QLAISDLAMV VSSGLALPIQ KLTRKGGNIL RWYRAGILIQ
     SLYQIAWLTL WIKWPFMLHW TWTAQVFFTL HTLTILMKVH SYAFYNGHLS ETERRLSELD
     KPGQGSMAAA VRYPSSPARA ETMNGSFEIK GEEPLSRLRD DLATELTSPL GQVTYPQNLT
     LGNFVDFLFC PTLCYEIEYP RTPSIRWTEV FFKALAVFGC IFLLTLTSEE FIVPVLHEAS
     ISLSSVNTWS DQALILAETT SMLLFPFMIT FLLVFLVIFE YLLGAFAEIT RFADRRFYSD
     WWNSCDWLEF SREWNIPVHH FLRRHVYFSS KAYFSAPVAM FITFLVSALA HELVMSCITK
     KLRGYGFLLM MLQLPIIAIQ RTPLIRQAKT WNNIVFWFSM ILGLSMMCAL YVLV
//
DBGET integrated database retrieval system