ID   TGCE1_SCHPO             Reviewed;         467 AA.
AC   O74430;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Probable lipase C1672.09;
DE            EC=3.1.1.-;
GN   ORFNames=SPCC1672.09;
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] {ECO:0000312|EMBL:CAA20447.1}
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] {ECO:0000305}
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).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, 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: Probable lipase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Membrane
CC       {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; CU329672; CAA20447.1; -; Genomic_DNA.
DR   PIR; T41053; T41053.
DR   RefSeq; NP_587880.1; NM_001022872.2.
DR   AlphaFoldDB; O74430; -.
DR   SMR; O74430; -.
DR   BioGRID; 275910; 10.
DR   STRING; 4896.SPCC1672.09.1; -.
DR   ESTHER; schpo-SPCC1672.09; Acidic_Lipase.
DR   iPTMnet; O74430; -.
DR   MaxQB; O74430; -.
DR   PaxDb; O74430; -.
DR   EnsemblFungi; SPCC1672.09.1; SPCC1672.09.1:pep; SPCC1672.09.
DR   GeneID; 2539344; -.
DR   KEGG; spo:SPCC1672.09; -.
DR   PomBase; SPCC1672.09; -.
DR   VEuPathDB; FungiDB:SPCC1672.09; -.
DR   eggNOG; KOG2624; Eukaryota.
DR   HOGENOM; CLU_010974_5_0_1; -.
DR   InParanoid; O74430; -.
DR   OMA; DGEHVDC; -.
DR   PhylomeDB; O74430; -.
DR   PRO; PR:O74430; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004771; F:sterol esterase activity; ISO:PomBase.
DR   GO; GO:0006696; P:ergosterol biosynthetic process; ISO:PomBase.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Membrane; Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..467
FT                   /note="Probable lipase C1672.09"
FT                   /id="PRO_0000312659"
FT   TOPO_DOM        1..17
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        18..38
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        39..467
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          127..421
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   REGION          440..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..460
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        222
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        389
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P80035"
FT   ACT_SITE        415
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P80035"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   467 AA;  54381 MW;  2ED7D0A3F5D86FEB CRC64;
     MIQLPFIQRL KWEEYMALFL GFFFVIFEKL LSCLAFMIHN TLGLFYRSVV RNEIKKRSKK
     RSRSRSVSLQ RAKAIHDAAD IREMCKISGY YVEDHLVRTE DDYILCIHRI SKDSPGRIGS
     PHPKKLPVVY CHHGLLMNSE VWVCNVDPRN CLVFDLVNKG YDVWLGNNRG NKYSRQHLRF
     DSTDKEFWDF SIDDFAQYDI PDTIDYILKT SGQTKLTYIG FSQGTAQAFA SLSIHPLLND
     KINSLIALAP AISPKGLHNR VVDAFVKARP SILFFLFGRK SILPSAGFWQ SFLAPKFFDA
     VLAYCLSQLF NWSCQNISSY QRLVSFAHLY SYTSVKCLVH WFQIMRSAEF RMYDNDQLGH
     DYFLKYYKAA KFPTNNIRTP IYLIWGGSDS LVDIQAMLNA LPAEVEHVKV DSYEHLDMIW
     ADTVKDYVIP PVLRRLRDIH HPPEHEENDK ENREIQKNHI APRNKPI