ID D8Q1E9_SCHCM Unreviewed; 588 AA.
AC D8Q1E9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
GN ORFNames=SCHCODRAFT_53724 {ECO:0000313|EMBL:EFI98495.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFI98495.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
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}.
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DR EMBL; GL377305; EFI98495.1; -; Genomic_DNA.
DR RefSeq; XP_003033398.1; XM_003033352.1.
DR AlphaFoldDB; D8Q1E9; -.
DR STRING; 578458.D8Q1E9; -.
DR GeneID; 9590872; -.
DR KEGG; scm:SCHCO_02619284; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02619284; -.
DR eggNOG; KOG0380; Eukaryota.
DR HOGENOM; CLU_018190_2_0_1; -.
DR InParanoid; D8Q1E9; -.
DR OMA; FNRQWPW; -.
DR OrthoDB; 9612at2759; -.
DR Proteomes; UP000007431; 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; 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:UP000007431};
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 71..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 568..587
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 525
FT /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ SEQUENCE 588 AA; 65998 MW; 4C61040CDBFF767C CRC64;
MPVDAAATTT EALAARTGGE GLETPAGTLY VSKPFRSKSS KKLRALITFT PRKSAFDTTN
ELSGANEFRG FFTLFWISMF IFTIRTYISS IETQGAPLNL AFATMFSQDA VTLFWSDMLL
IASSVLCVPF AKAIATNTIQ YYWTGVILQH IFQTSILFIA VSWTYHRQWP WVQSGFLTLH
TLVMIMKMHS YINVNGYMQY ITAQSQQVLD QMRKATETIG GGWDHAIEVA KARRAELDNA
AGMSSGTDSP PSMDTTPPVM ATPPIATGAS ASYVDADTAT ALRKRLASVA PGVANDMRKA
EKAQEAAAAD EKSGVRSHVV SALEPHPLVD HPNEEIAQMA KDYSEMQGEL TSTGPERITW
PNNVTYKNFG LYLLIPSLVY ELEYPRTDKI RPIYVFEKVT AFFGSFALLY TITETFILPK
IPTADQSFLL SLLDLAMPFM FGYLMIFYII FECICNAFAE ISYFADRQFY EDWWNSTSWD
EFSRKWNRPV HSFLLRHVYA STITGYGLSR TQAMFATFLL SACAHELVMI VVTHKIRMYL
FSLQLIQIPL IAIGRHPVIK RNKLAGNINF WLGLYAGFPL LCVAYCAY
//
