TGL4_SCHPO
ID TGL4_SCHPO Reviewed; 630 AA.
AC O14115; Q9UTH6;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Triacylglycerol lipase ptl2;
DE EC=3.1.1.3 {ECO:0000250|UniProtKB:P36165};
GN Name=ptl2; ORFNames=SPAC1786.01c, SPAC31G5.20c;
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 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:P36165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000250|UniProtKB:P36165};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:P36165}.
CC -!- SIMILARITY: Belongs to the PLPL family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11704.1; -; Genomic_DNA.
DR PIR; T38637; T38637.
DR RefSeq; XP_001713076.1; XM_001713024.2.
DR AlphaFoldDB; O14115; -.
DR BioGRID; 278754; 27.
DR STRING; 4896.SPAC1786.01c.1; -.
DR iPTMnet; O14115; -.
DR MaxQB; O14115; -.
DR PaxDb; O14115; -.
DR PRIDE; O14115; -.
DR EnsemblFungi; SPAC1786.01c.1; SPAC1786.01c.1:pep; SPAC1786.01c.
DR PomBase; SPAC1786.01c; ptl2.
DR VEuPathDB; FungiDB:SPAC1786.01c; -.
DR eggNOG; KOG2214; Eukaryota.
DR HOGENOM; CLU_009031_2_2_1; -.
DR InParanoid; O14115; -.
DR OMA; DMNKWLR; -.
DR PhylomeDB; O14115; -.
DR PRO; PR:O14115; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005811; C:lipid droplet; IDA:PomBase.
DR GO; GO:0004806; F:triglyceride lipase activity; IMP:PomBase.
DR GO; GO:1990748; P:cellular detoxification; IMP:PomBase.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 Hydrolase; Lipid degradation; Lipid droplet; Lipid metabolism;
KW Reference proteome.
FT CHAIN 1..630
FT /note="Triacylglycerol lipase ptl2"
FT /id="PRO_0000116829"
FT DOMAIN 251..442
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 282..286
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 284
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 429
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ SEQUENCE 630 AA; 72522 MW; 18C93033FA80074F CRC64;
MSIPEESEIN KDYTVQEDLD EFAKYTCVYK KRHDEKIEYI TAQHDWNPVY EAVVPRKSKP
GKDEKREGFM YPILRWPLMF TAFLCLTFVA FLYLLDRLYI NCYEYFIVWR GEARRLRKLL
QEAKTYEEWK ERARALDKYF GNDEWKLDPV YDYYDYTLVQ AVYSSLVKHR EQKDWNALKS
VLDVCVRSNF GGIDSSMLYS RTYSGTKKLV EDYVNELKVC LETVIDQRLY TAQERSKMFE
YFSHNYGRTA LCLSGGASFA IYHTGVLRAL LNQDLIPNVI TGTSGGGLLA ALVCTRTNEE
LKQLLVPELA SKYQSDIGNW LDATKRYFRT GARFDEILWA KTCMYFTRGS LTFAEAYKRT
GRILNISVIP SDVHSPPKLI NYLTSPDTVI WSAVIASCAV PGILNPIPLM TRSQSHRLIP
HNFGNRFKDG SLRTDIPLSE LRTQFNVHFS IVSQTNPHVQ VFFFSPRGTV GRPVSHRKGR
GWRGGYVGSA IEQFLKYDMI KWLHVIRSLE LLPRPLGTDW SSVFLQKFDG TITIWPKTKF
QDFYYILSPP SVERLGYMID AGQAATFPKL DFIAARMTIE KLIEKGRMMD KPSKLGRSID
GTIGTSMSRG DIEISQESAS ISPEDIDIVN
