TGCE3_SCHPO
ID TGCE3_SCHPO Reviewed; 460 AA.
AC O60095;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Probable lipase C14C8.15;
DE EC=3.1.1.-;
GN ORFNames=SPBC14C8.15;
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:CAA18432.1}
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).
CC -!- FUNCTION: Probable lipase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:16823372}.
CC Membrane {ECO:0000255}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA18432.1; -; Genomic_DNA.
DR PIR; T39443; T39443.
DR RefSeq; NP_595918.1; NM_001021826.2.
DR AlphaFoldDB; O60095; -.
DR SMR; O60095; -.
DR BioGRID; 276390; 13.
DR STRING; 4896.SPBC14C8.15.1; -.
DR ESTHER; schpo-SPBC14C8.15; Acidic_Lipase.
DR MaxQB; O60095; -.
DR PaxDb; O60095; -.
DR PRIDE; O60095; -.
DR EnsemblFungi; SPBC14C8.15.1; SPBC14C8.15.1:pep; SPBC14C8.15.
DR GeneID; 2539842; -.
DR KEGG; spo:SPBC14C8.15; -.
DR PomBase; SPBC14C8.15; -.
DR VEuPathDB; FungiDB:SPBC14C8.15; -.
DR eggNOG; KOG2624; Eukaryota.
DR HOGENOM; CLU_010974_5_0_1; -.
DR InParanoid; O60095; -.
DR OMA; MFGTKGF; -.
DR PhylomeDB; O60095; -.
DR PRO; PR:O60095; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; 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; IPR006693; AB_hydrolase_lipase.
DR Pfam; PF04083; Abhydro_lipase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Golgi apparatus; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..460
FT /note="Probable lipase C14C8.15"
FT /id="PRO_0000312661"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..460
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 214
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 382
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P80035"
FT ACT_SITE 408
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P80035"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 460 AA; 52670 MW; 40A431D8A7357406 CRC64;
MTLNGNIMKY CLEKGEILIS FLLIALESMF RICTVILPSP LRNWFYEQSK KVYSYFLPEL
LVDDNANKLT DARDTIDLCA LHGYDLEEHF VRTTDGYLLG LHRVYKKKKG KIEELNYLPP
VLFIHGLMMN SESWVCNLKK EDAIPFALVE QGYDVWLGNL RGNKYSIKNI KFSSQNPKFW
DFSLDSIAIF DIPSIVKYIL SVNSFDSISL VGFSQGAILA FAALSIDTEL RNSVRAFIAL
APAIAPKKYS GRTVKSIIHA NSQLLYLMFG RNSMLGSAVF WQAVLYPPVF AKIVDLFLRF
FLSWTGKNIS ETQKIVAYSH LYSFTSVKCF VHWAQITRRK VLQMYDDSPG FKPSYYTNLN
RIARYPIENI RLPITLVYGS NDNMVDIETL KTQLPPLSQC IQIPNYEHLD IIMGDTKKDI
VIQQVVEQLN HVIAGDYFES IKEEFGLDTE LVDGVMNHTI
