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Database: UniProt
Entry: A0A0F2LU62_SPOSC
LinkDB: A0A0F2LU62_SPOSC
Original site: A0A0F2LU62_SPOSC 
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
//
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