MU180_SCHPO
ID MU180_SCHPO Reviewed; 381 AA.
AC Q9HDV1;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Putative steryl acetyl hydrolase mug81;
DE EC=3.1.1.-;
DE AltName: Full=Meiotically up-regulated gene 180 protein;
GN Name=mug180; ORFNames=SPBPB2B2.02;
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 FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [3]
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: Required for the deacetylation of acetylated sterols (By
CC similarity). Has a role in meiosis. {ECO:0000250,
CC ECO:0000269|PubMed:16303567}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-
CC pass type II membrane protein {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAC21404.1; -; Genomic_DNA.
DR RefSeq; NP_596850.1; NM_001023873.2.
DR AlphaFoldDB; Q9HDV1; -.
DR SMR; Q9HDV1; -.
DR BioGRID; 277903; 1.
DR ESTHER; schpo-SPBPB2B2.02; Steryl_acetyl_hydrolase.
DR PaxDb; Q9HDV1; -.
DR EnsemblFungi; SPBPB2B2.02.1; SPBPB2B2.02.1:pep; SPBPB2B2.02.
DR GeneID; 2541394; -.
DR KEGG; spo:SPBPB2B2.02; -.
DR PomBase; SPBPB2B2.02; mug180.
DR VEuPathDB; FungiDB:SPBPB2B2.02; -.
DR eggNOG; ENOG502RDZA; Eukaryota.
DR HOGENOM; CLU_717977_0_0_1; -.
DR InParanoid; Q9HDV1; -.
DR OMA; YNYSAND; -.
DR PhylomeDB; Q9HDV1; -.
DR PRO; PR:Q9HDV1; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR GO; GO:0034084; F:steryl deacetylase activity; ISO:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0034210; P:sterol deacetylation; ISO:PomBase.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR019436; Say1-like.
DR Pfam; PF10340; Say1_Mug180; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Glycoprotein; Hydrolase; Meiosis;
KW Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..381
FT /note="Putative steryl acetyl hydrolase mug81"
FT /id="PRO_0000278630"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..381
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOTIF 125..127
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 200
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 381 AA; 43152 MW; AEB2C5FF983E24EA CRC64;
MISLSLLYRI LTLPIILVGT TILYFTIGTN FPHDELRHNL LSTLFCSSML HLSKGLTVKD
VRIFFHDSIG STLLKNRKKL NSENELPNYG EKFTHKYDNQ DMPDSVWLAK VNGMTKSDPI
ILHLHGGMMA LPYDKVILVG LSNLYKLFST TMNRPPSILL VDYSLVSQGY TYPKQVRECL
NVYQVLISKG FRNITVLGES AGGTLILSFL YQISELSKLN KVVWPKGVAL ISPWLDLTNA
KKIGSYRAND GLDVICYETL NRFGKAYVNN EESLFTSSVV NINMNCDISI WSKIPPIQDG
KVLVLFGENE VFRDEILSWT SKIGLLKAYP NRVLMDKQGI HIGLFLEESP SIGPGMTNLD
IWKKKFSVNS LYTFLRETFE E