TGL5_SCHPO
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 03-AUG-2022, entry version 107.
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; 4896.SPAC1A6.05c.1; -.
DR MaxQB; Q9Y827; -.
DR PaxDb; Q9Y827; -.
DR PRIDE; Q9Y827; -.
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; VTEWHDA; -.
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 InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR021771; Triacylglycerol_lipase_N.
DR Pfam; PF11815; DUF3336; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 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
