AREH2_SCHPO
ID AREH2_SCHPO Reviewed; 472 AA.
AC Q9UU82;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable sterol O-acyltransferase 2;
DE EC=2.3.1.-;
DE AltName: Full=Sterol-ester synthase 2;
GN Name=are2; ORFNames=SPCP1E11.05c;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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:0000250|UniProtKB:P25628}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Sterol o-acyltransferase subfamily. {ECO:0000305}.
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DR EMBL; CU329672; CAB54864.1; -; Genomic_DNA.
DR PIR; T41684; T41684.
DR RefSeq; NP_588558.1; NM_001023545.2.
DR AlphaFoldDB; Q9UU82; -.
DR SMR; Q9UU82; -.
DR BioGRID; 275435; 53.
DR STRING; 4896.SPCP1E11.05c.1; -.
DR iPTMnet; Q9UU82; -.
DR MaxQB; Q9UU82; -.
DR PaxDb; Q9UU82; -.
DR PRIDE; Q9UU82; -.
DR EnsemblFungi; SPCP1E11.05c.1; SPCP1E11.05c.1:pep; SPCP1E11.05c.
DR GeneID; 2538854; -.
DR KEGG; spo:SPCP1E11.05c; -.
DR PomBase; SPCP1E11.05c; are2.
DR VEuPathDB; FungiDB:SPCP1E11.05c; -.
DR eggNOG; KOG0380; Eukaryota.
DR HOGENOM; CLU_018190_2_0_1; -.
DR InParanoid; Q9UU82; -.
DR OMA; FWCSMIL; -.
DR PhylomeDB; Q9UU82; -.
DR PRO; PR:Q9UU82; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA: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 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..472
FT /note="Probable sterol O-acyltransferase 2"
FT /id="PRO_0000315968"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 355..361
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT ACT_SITE 409
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 472 AA; 55157 MW; C0325046AE97FAF8 CRC64;
MIAATPAKSK PSDVNLEQTF KGVSETSKID LRRSRAAYRP LELSPTPSIF ARNYQRNAVD
FTGFFVLFWV AVSIMIFMSF LENFELTGRP VVGTIFKYFQ SNLLDLAKAD LAMSSMFLLA
FPFQKIFALG YLRWYGLGVY LYSILILLFL SHCVLRCCLS NWSWTHRAMF ILHSMVILMK
LHSYNVVNGW YSYCYHSLNK LQSKKTDLDD DERSSVEFYE HCLNHHGNTY PENLTIPNAL
DFLFMPSLCY QLYYPRTAHV RIHYLIECAL GTFGCIFLLV IISDHFMVPV LAKAIRTIIE
APEDASATYF AIRLGHTVAF LMFPFMLSFL LVFWVIFEGV CNFSAEITRF ADRNFYDDWW
NCWTWDQFAR TWNKPVHYFL LRHVYVPLNS FMSKSLSTFF TFFVSSVLHE LVMGCITLKI
RGYGLFFQMT QIPYIIIQRQ KFVRRHRLLG NIAFWFSIII GIALIAALYI LF
