TGCE2_SCHPO
ID TGCE2_SCHPO Reviewed; 443 AA.
AC P78898;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Probable lipase C16A3.12c;
DE EC=3.1.1.-;
GN ORFNames=SPBC16A3.12c;
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:CAA16863.1}
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: Cytoplasm {ECO:0000269|PubMed:16823372}. Vacuole
CC {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Single-pass type
CC II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA16863.1; -; Genomic_DNA.
DR PIR; T39540; T39540.
DR PIR; T43170; T43170.
DR RefSeq; NP_596777.1; NM_001023798.2.
DR AlphaFoldDB; P78898; -.
DR SMR; P78898; -.
DR BioGRID; 276421; 6.
DR STRING; 4896.SPBC16A3.12c.1; -.
DR ESTHER; schpo-SPBC16A3.12C; Acidic_Lipase.
DR MaxQB; P78898; -.
DR PaxDb; P78898; -.
DR EnsemblFungi; SPBC16A3.12c.1; SPBC16A3.12c.1:pep; SPBC16A3.12c.
DR GeneID; 2539875; -.
DR KEGG; spo:SPBC16A3.12c; -.
DR PomBase; SPBC16A3.12c; -.
DR VEuPathDB; FungiDB:SPBC16A3.12c; -.
DR eggNOG; KOG2624; Eukaryota.
DR HOGENOM; CLU_010974_5_0_1; -.
DR InParanoid; P78898; -.
DR OMA; GHMPTKA; -.
DR PhylomeDB; P78898; -.
DR PRO; PR:P78898; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0000324; C:fungal-type vacuole; 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 InterPro; IPR025483; Lipase_euk.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Vacuole.
FT CHAIN 1..443
FT /note="Probable lipase C16A3.12c"
FT /id="PRO_0000312660"
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..443
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 116..410
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 210
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 378
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P80035"
FT ACT_SITE 404
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P80035"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 443 AA; 51548 MW; 92ED3CBACFC42D0B CRC64;
MSGFNKNQIY WGDYVGVIAA FVGVYTELVA RIFIYMIPER VREWFRVRII VLYHYYISSK
TTDGMTDAVQ KCRNIYEICE AFGYRVEEHL VRTQDNFILC LHRITHPKQS QHKREVVYCH
HGLMTNSELW VAVNESERSL PFVLIESGYD VWLGNNRGNK YSRKHITYKP KDEEFWNFSL
DDMAMFDIPD TVDYILRETG REKLNYIGFS QGTAQAMAAL SINPDLNDKV NIFIGLAPAY
APKGFSNYFV DYIVKVNPKI MYHLFGRRCL LPSVTFWQNI CYPPIFVKIV DVSLKILFNW
DLSNISLNQK LCGYAHLYSF SSVKSVVHWL QIIKNCTFQL YDDDMALLAG YGSRHYQVPL
FPTNNIKCPM LILWGGKDTL INMEVMRTAL PPHAKEVSIA HYEHLDFLWG QDVKEEVFPV
VIDALKHHSL GKAKHFVKQN GFH
