AREH1_SCHPO
ID AREH1_SCHPO Reviewed; 537 AA.
AC Q10269;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable sterol O-acyltransferase 1;
DE EC=2.3.1.-;
DE AltName: Full=Sterol-ester synthase 1;
GN Name=are1; ORFNames=SPAC13G7.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Sterol O-acyltransferase that catalyzes the formation of
CC stery esters. {ECO:0000250|UniProtKB:P25628}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Sterol o-acyltransferase subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAA93593.1; -; Genomic_DNA.
DR PIR; S67434; S67434.
DR RefSeq; NP_593707.1; NM_001019138.2.
DR AlphaFoldDB; Q10269; -.
DR BioGRID; 279297; 4.
DR STRING; 4896.SPAC13G7.05.1; -.
DR iPTMnet; Q10269; -.
DR MaxQB; Q10269; -.
DR PaxDb; Q10269; -.
DR PRIDE; Q10269; -.
DR EnsemblFungi; SPAC13G7.05.1; SPAC13G7.05.1:pep; SPAC13G7.05.
DR GeneID; 2542851; -.
DR KEGG; spo:SPAC13G7.05; -.
DR PomBase; SPAC13G7.05; are1.
DR VEuPathDB; FungiDB:SPAC13G7.05; -.
DR eggNOG; KOG0380; Eukaryota.
DR HOGENOM; CLU_018190_2_1_1; -.
DR InParanoid; Q10269; -.
DR OMA; FYLIFEC; -.
DR PhylomeDB; Q10269; -.
DR PRO; PR:Q10269; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IC:PomBase.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0034737; F:ergosterol O-acyltransferase activity; ISO:PomBase.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006696; P:ergosterol biosynthetic process; ISO:PomBase.
DR GO; GO:0008204; P:ergosterol metabolic process; IBA:GO_Central.
DR GO; GO:0140042; P:lipid droplet formation; IMP:PomBase.
DR InterPro; IPR004299; MBOAT_fam.
DR InterPro; IPR014371; Oat_ACAT_DAG_ARE.
DR PANTHER; PTHR10408; PTHR10408; 1.
DR Pfam; PF03062; MBOAT; 1.
DR PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..537
FT /note="Probable sterol O-acyltransferase 1"
FT /id="PRO_0000207652"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 418..424
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT ACT_SITE 474
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 537 AA; 63098 MW; 41DBA79402B67A28 CRC64;
MTDTPRILIT PSPLSDISTT INKPNVHPSM SLLKALPECR LVVKSKGDKN NANVVEFPLD
RHKQLLIAGK VYHDYKFKPR KSIFDRVTDP NYFAKSEFRG FYVLFWLSMA AWVLQLYARS
YWQRDTLLGL PLARQVFRQF FVLFSSDFLM ICLSFFSYGL QVCIEKNMIR WANLGYTIQT
LWQGFYMVLA VYWVKHRDFP IVQCVFFTLH CAVLIMKQFS YSHHMGYISE IRILHNEYEK
LLKFVRECLN STEKDEKYTF ELTFPNKPAE TISTLQAEEI VALTAKYLSR QMRSEVGNVV
YPDNINFFNY VDYLLVPSLV YSMEFPRVAH FRWHYMAFKA GSTFGLLALT LALVDWYFVP
SAVAVKDLDF IGKLRIAPLL MNKIMFPAII LYLIMFYLIF DCILNAFAEI TKFADRGFYG
AWWNTVTWDE FSREWNKPVH VFLMRHVYHS SISGFKLKKS HAVLLTFLIS ALVHEFVMLL
ATGKFRCYIL TFQLLQIPLY DLQQMFAFKK RDILGNVFFW IGMFTGPSFL CILYIVF
