ID   TGL5_SCHPO              Reviewed;         483 AA.
AC   Q9Y827;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 112.
DE   RecName: Full=Triacylglycerol lipase ptl3;
DE            EC=3.1.1.3 {ECO:0000250|UniProtKB:Q12043};
GN   Name=ptl3; ORFNames=SPAC1A6.05c;
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   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   FUNCTION.
RX   PubMed=22592553; DOI=10.1007/s00253-012-4151-8;
RA   Yazawa H., Kumagai H., Uemura H.;
RT   "Characterization of triglyceride lipase genes of fission yeast
RT   Schizosaccharomyces pombe.";
RL   Appl. Microbiol. Biotechnol. 96:981-991(2012).
CC   -!- FUNCTION: Lipid particle-localized triacylglycerol (TAG) lipase. The
CC       lipid droplet/particle is a lipid storage compartment which serves as a
CC       depot of energy and building blocks for membrane lipid biosynthesis.
CC       Involved in the mobilization of the non-polar storage lipids
CC       triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs,
CC       releasing and supplying specific fatty acids to the appropriate
CC       metabolic pathways. {ECO:0000269|PubMed:22592553}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC         H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC         Evidence={ECO:0000250|UniProtKB:Q12043};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Lipid
CC       droplet {ECO:0000250|UniProtKB:Q12043}.
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DR   EMBL; CU329670; CAB16355.2; -; Genomic_DNA.
DR   PIR; T38008; T38008.
DR   RefSeq; NP_593197.1; NM_001018593.2.
DR   AlphaFoldDB; Q9Y827; -.
DR   BioGRID; 278680; 3.
DR   STRING; 284812.Q9Y827; -.
DR   MaxQB; Q9Y827; -.
DR   PaxDb; 4896-SPAC1A6-05c-1; -.
DR   EnsemblFungi; SPAC1A6.05c.1; SPAC1A6.05c.1:pep; SPAC1A6.05c.
DR   GeneID; 2542205; -.
DR   KEGG; spo:SPAC1A6.05c; -.
DR   PomBase; SPAC1A6.05c; ptl3.
DR   VEuPathDB; FungiDB:SPAC1A6.05c; -.
DR   eggNOG; KOG2214; Eukaryota.
DR   HOGENOM; CLU_009031_5_1_1; -.
DR   InParanoid; Q9Y827; -.
DR   OMA; WILNITV; -.
DR   PhylomeDB; Q9Y827; -.
DR   PRO; PR:Q9Y827; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005811; C:lipid droplet; ISO:PomBase.
DR   GO; GO:0004806; F:triglyceride lipase activity; IMP:PomBase.
DR   GO; GO:0019433; P:triglyceride catabolic process; ISO:PomBase.
DR   GO; GO:0006642; P:triglyceride mobilization; IMP:PomBase.
DR   CDD; cd07230; Pat_TGL4-5_like; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR021771; Triacylglycerol_lipase_N.
DR   PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR   PANTHER; PTHR14226:SF10; TRIACYLGLYCEROL LIPASE 4-RELATED; 1.
DR   Pfam; PF11815; DUF3336; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Lipid degradation; Lipid droplet; Lipid metabolism;
KW   Reference proteome.
FT   CHAIN           1..483
FT                   /note="Triacylglycerol lipase ptl3"
FT                   /id="PRO_0000317235"
FT   DOMAIN          141..340
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           145..150
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           172..176
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        174
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        327
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   483 AA;  54684 MW;  B47CD9E513EBAACF CRC64;
     MSKNEIKLQM EYASSYETWL EAAEKLDVIE GKYQWREQKE SDEYDYVLVE SRLHELRRHR
     LSKNTRLLLG LLRNSVARDF ANMDNSRLYN YAHSGTKKLI DEFIQEVLMC LTYLEETPDL
     SLDEKITEFS RLKLTTGNTA LILSGGGTFG MTHIGVLQSL HEQGLVPKII CGSSAGAIVA
     CAAAVRNKEE QEILLRQFHT GDLSVFTDPN AAPPSVIQSV KQYFTRGCVL DISHLERVMK
     LLIGDFTFQE AYDRSGYILN VTVSCGSLFE MPSLLNYITA PNVLVWSAVV ATCSVPFLFK
     RATLWERDPL TREVSAFCVT DAPLWMDGSV DNDIPHAKLT ELFHVNHFIV SQVNFHIVPF
     IMDPTSHNWV ERCCKKAIDL AAQEVSLTFR LFAELGIFSV LFTKLQSVIT QKYSGDITII
     PRLNYREVNK VIKNPTPSFL LDAATRGKRG TWTKVPVTRN HCAIEILIAA AYTRLIKRSK
     SLK
//