ID F7VK81_SORMK Unreviewed; 520 AA.
AC F7VK81;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
GN ORFNames=SMAC_00123 {ECO:0000313|EMBL:CCC05908.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC05908.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC05908.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC05908.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCC05908.1}.
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; CABT02000001; CCC05908.1; -; Genomic_DNA.
DR RefSeq; XP_003351582.1; XM_003351534.1.
DR AlphaFoldDB; F7VK81; -.
DR STRING; 771870.F7VK81; -.
DR GeneID; 10809175; -.
DR KEGG; smp:SMAC_00123; -.
DR VEuPathDB; FungiDB:SMAC_00123; -.
DR eggNOG; KOG0380; Eukaryota.
DR HOGENOM; CLU_018190_3_0_1; -.
DR InParanoid; F7VK81; -.
DR OMA; SCLSHDS; -.
DR OrthoDB; 9612at2759; -.
DR Proteomes; UP000001881; 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; 2.
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:UP000001881};
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 112..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 424
FT /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ SEQUENCE 520 AA; 59002 MW; B4E3C02ACD187DFC CRC64;
MSSPTTTATG LDPAVQNDNV IRRTHGPENS KISNGEANGS VDSDNDTRKQ MKKAIRSKYR
HVEAVHSQSR PSCLSHDTTE SPSFLGFRNL MYGVLICIGC HDFRKSDINM GLLLYFLIPC
HLFIAYIIEY YAAVQARAER NAASEAKKGE GNHQDGTSSP TEEQHRKFQS TWKLVRLLHA
INVTTALALT SYVVYYHIHH PLIGTLTEVH AIVVWLKTAS YAFTNRDLRH AYLHPARGEL
DALPELYAQC PYPENITMGN LCYFWWAPTL VYQPVYPRTN KIRWSFVAKR CGEVVCLSVF
IWFTSAQYAT PVLRNSLDKI ASLDIPSIVE RLLKLSTISL IIWLAGFFAL FQSFLNALAE
VMRFADRSFY DEWWNSESLG VYWRTWNKPV YQYFKRHVYS PMRSRGWSNG TASLAVFFLS
AVLHELLVGV PTHNIIGVAF LGMFLQLPLI QLTKPLEKKT SPNGKLLGNT IFWVSFTIFG
QPFAALMYFY AWQAKYGSVS KMATMQQLVE QGQGTCPPLG
//