ID A0A0F2LU62_SPOSC Unreviewed; 804 AA.
AC A0A0F2LU62;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Sterol O-acyltransferase {ECO:0000313|EMBL:KJR80992.1};
GN ORFNames=SPSK_04973 {ECO:0000313|EMBL:KJR80992.1};
OS Sporothrix schenckii 1099-18.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1397361 {ECO:0000313|EMBL:KJR80992.1, ECO:0000313|Proteomes:UP000033710};
RN [1] {ECO:0000313|EMBL:KJR80992.1, ECO:0000313|Proteomes:UP000033710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1099-18 {ECO:0000313|EMBL:KJR80992.1,
RC ECO:0000313|Proteomes:UP000033710};
RX PubMed=25351875; DOI=10.1186/1471-2164-15-943;
RA Teixeira M.M., de Almeida L.G., Kubitschek-Barreira P., Alves F.L.,
RA Kioshima E.S., Abadio A.K., Fernandes L., Derengowski L.S., Ferreira K.S.,
RA Souza R.C., Ruiz J.C., de Andrade N.C., Paes H.C., Nicola A.M.,
RA Albuquerque P., Gerber A.L., Martins V.P., Peconick L.D., Neto A.V.,
RA Chaucanez C.B., Silva P.A., Cunha O.L., de Oliveira F.F., dos Santos T.C.,
RA Barros A.L., Soares M.A., de Oliveira L.M., Marini M.M.,
RA Villalobos-Duno H., Cunha M.M., de Hoog S., da Silveira J.F., Henrissat B.,
RA Nino-Vega G.A., Cisalpino P.S., Mora-Montes H.M., Almeida S.R.,
RA Stajich J.E., Lopes-Bezerra L.M., Vasconcelos A.T., Felipe M.S.;
RT "Comparative genomics of the major fungal agents of human and animal
RT Sporotrichosis: Sporothrix schenckii and Sporothrix brasiliensis.";
RL BMC Genomics 15:943-943(2014).
RN [2] {ECO:0000313|EMBL:KJR80992.1, ECO:0000313|Proteomes:UP000033710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1099-18 {ECO:0000313|EMBL:KJR80992.1,
RC ECO:0000313|Proteomes:UP000033710};
RX PubMed=25480940;
RA Teixeira Mde M., Rodrigues A.M., Tsui C.K., de Almeida L.G.,
RA Van Diepeningen A.D., van den Ende B.G., Fernandes G.F., Kano R.,
RA Hamelin R.C., Lopes-Bezerra L.M., Vasconcelos A.T., de Hoog S.,
RA de Camargo Z.P., Felipe M.S.;
RT "Asexual propagation of a virulent clone complex in a human and feline
RT outbreak of sporotrichosis.";
RL Eukaryot. Cell 14:158-169(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}; 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}.
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:KJR80992.1}.
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DR EMBL; AXCR01000012; KJR80992.1; -; Genomic_DNA.
DR RefSeq; XP_016583668.1; XM_016731731.1.
DR AlphaFoldDB; A0A0F2LU62; -.
DR GeneID; 27667008; -.
DR KEGG; ssck:SPSK_04973; -.
DR VEuPathDB; FungiDB:SPSK_04973; -.
DR OrthoDB; 9612at2759; -.
DR Proteomes; UP000033710; 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:SF23; STEROL O-ACYLTRANSFERASE 1-RELATED; 1.
DR Pfam; PF03062; MBOAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:KJR80992.1};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:KJR80992.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 602..624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 781..803
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 804 AA; 90908 MW; 9EF4BD413114C6D5 CRC64;
MAPNDSAFQG GSDVAAVAQN QQNQQHQQQE PRPNAMRYAA RVSSQRLDRT FSSDASVTAS
ESPSEEDYDE LTSRPAEGMV LRQRRKPQTQ LRNEVQADAS ELDDTTTEQG NSPREGLERE
AVYSPTSRLQ RGGRKLSATV IFEEKGGSGS GSGSSSAGGG RDSQGAQHSS DTTAVSSSES
VDGDANGLSS VKAYGAGRTD SHGQSYVVSI DDPKLVEILR ADLENMREDM EEKRRLLDGI
AVHDKALLDD GGQAKHRRGS VSSKPKSKKK PRGRFSDFVF TRGFSTFDRQ NAAAANSPFH
GFFTLFWISV FVFMIKIGAE NWRKTGSPLG TNEIMANMFH RDVVVMLLSD GVLCALTGVS
WLIQLVVHDG RLMEWDGAGW IVQNIWQTMY VALFIGWTQL RDWPWSHTVF FVLHGLVMLM
KQHSYAFYNG YLSSIYKRRA TLQSRLEELQ RAELHGGDVG DKIRTSSRPH ADAALASAAR
AAVSSGVKTE DGHAKKQGSH ATAEQMAAST ATPEALDKVV AALQSGQPLD YQQARVFERI
LHWEIDGLTE ELRGKSTRPD KMYPNNLTFN NHYEYIVLPT LVYELEYPRS ETINWRYAAE
KLVAVFGIIF VMIMVSQAFM YPVVMRTVAM KEAGMPLAER FKEFPWMLSD LIFPFMMEYL
LTWYLIWETI LNFLAEITFF ADRNFYSAWW NSVTWDEFAR DWNRPVHLFL LRHVYHSSIS
AMKVNKYTAT LITFFLSACV HELVMWCIFK KLRGYLLFLQ MCQLPLVRLS RTRWMRNRQT
LGNIMFWAGI FMGPTILCSL YLIL
//