PDAT_SCHPO
ID PDAT_SCHPO Reviewed; 632 AA.
AC O94680;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Phospholipid:diacylglycerol acyltransferase;
DE Short=PDAT;
DE EC=2.3.1.158 {ECO:0000269|PubMed:12963726};
DE AltName: Full=Pombe LRO1 homolog 1;
DE AltName: Full=Triacylglycerol synthase;
DE Short=TAG synthase;
GN Name=plh1; ORFNames=SPBC776.14;
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=12963726; DOI=10.1074/jbc.m306998200;
RA Zhang Q., Chieu H.K., Low C.P., Zhang S., Heng C.K., Yang H.;
RT "Schizosaccharomyces pombe cells deficient in triacylglycerols synthesis
RT undergo apoptosis upon entry into the stationary phase.";
RL J. Biol. Chem. 278:47145-47155(2003).
RN [4]
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26990381; DOI=10.1111/tra.12394;
RA Meyers A., Del Rio Z.P., Beaver R.A., Morris R.M., Weiskittel T.M.,
RA Alshibli A.K., Mannik J., Morrell-Falvey J., Dalhaimer P.;
RT "Lipid droplets form from distinct regions of the cell in the fission yeast
RT Schizosaccharomyces pombe.";
RL Traffic 17:657-669(2016).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28011631; DOI=10.1242/bio.022384;
RA Yang H.J., Osakada H., Kojidani T., Haraguchi T., Hiraoka Y.;
RT "Lipid droplet dynamics during Schizosaccharomyces pombe sporulation and
RT their role in spore survival.";
RL Biol. Open 6:217-222(2017).
CC -!- FUNCTION: Catalyzes triacylglycerol (TAG) formation by an acyl-CoA
CC independent pathway. The enzyme specifically transfers acyl groups from
CC the sn-2 position of a phospholipid to diacylglycerol (DAG), thus
CC forming an sn-1-lysophospholipid. Plays a major role in triacylglycerol
CC formation at log phase (PubMed:12963726, PubMed:26990381). Involved in
CC lipid particle synthesis from the endoplasmic reticulum, promoting
CC localized TAG production at discrete ER subdomains (PubMed:26990381,
CC PubMed:28011631). {ECO:0000269|PubMed:12963726,
CC ECO:0000269|PubMed:26990381, ECO:0000269|PubMed:28011631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + a glycerophospholipid = a
CC monoacylglycerophospholipid + a triacyl-sn-glycerol;
CC Xref=Rhea:RHEA:14057, ChEBI:CHEBI:17815, ChEBI:CHEBI:64615,
CC ChEBI:CHEBI:136912, ChEBI:CHEBI:136913; EC=2.3.1.158;
CC Evidence={ECO:0000269|PubMed:12963726};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC {ECO:0000305|PubMed:12963726}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12963726, ECO:0000269|PubMed:16823372}; Single-pass
CC type II membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Has reduced whole-cell and lipid droplet (LD) TAG
CC levels. Cells lacking both TAG synthase genes (plh1 and dga1) have no
CC LDs and exhibit defects in spore germination and in spore wall
CC integrity. {ECO:0000269|PubMed:26990381, ECO:0000269|PubMed:28011631}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAA22887.2; -; Genomic_DNA.
DR PIR; T40685; T40685.
DR RefSeq; NP_596330.2; NM_001022251.2.
DR AlphaFoldDB; O94680; -.
DR SMR; O94680; -.
DR BioGRID; 277701; 29.
DR STRING; 4896.SPBC776.14.1; -.
DR ESTHER; schpo-pdat; PC-sterol_acyltransferase.
DR MaxQB; O94680; -.
DR PaxDb; O94680; -.
DR EnsemblFungi; SPBC776.14.1; SPBC776.14.1:pep; SPBC776.14.
DR GeneID; 2541187; -.
DR KEGG; spo:SPBC776.14; -.
DR PomBase; SPBC776.14; plh1.
DR VEuPathDB; FungiDB:SPBC776.14; -.
DR eggNOG; KOG2369; Eukaryota.
DR HOGENOM; CLU_016065_1_0_1; -.
DR InParanoid; O94680; -.
DR OMA; WGNSTWA; -.
DR UniPathway; UPA00282; -.
DR PRO; PR:O94680; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IC:PomBase.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0046027; F:phospholipid:diacylglycerol acyltransferase activity; IMP:PomBase.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IC:PomBase.
DR GO; GO:0140042; P:lipid droplet formation; IMP:PomBase.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0019915; P:lipid storage; EXP:PomBase.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IMP:PomBase.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR Pfam; PF02450; LCAT; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..632
FT /note="Phospholipid:diacylglycerol acyltransferase"
FT /id="PRO_0000058267"
FT TOPO_DOM 1..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..632
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 293
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT ACT_SITE 535
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT ACT_SITE 586
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3"
SQ SEQUENCE 632 AA; 70833 MW; D7F2D81FDA76EDE4 CRC64;
MASSKKSKTH KKKKEVKSPI DLPNSKKPTR ALSEQPSASE TQSVSNKSRK SKFGKRLNFI
LGAILGICGA FFFAVGDDNA VFDPATLDKF GNMLGSSDLF DDIKGYLSYN VFKDAPFTTD
KPSQSPSGNE VQVGLDMYNE GYRSDHPVIM VPGVISSGLE SWSFNNCSIP YFRKRLWGSW
SMLKAMFLDK QCWLEHLMLD KKTGLDPKGI KLRAAQGFEA ADFFITGYWI WSKVIENLAA
IGYEPNNMLS ASYDWRLSYA NLEERDKYFS KLKMFIEYSN IVHKKKVVLI SHSMGSQVTY
YFFKWVEAEG YGNGGPTWVN DHIEAFINIS GSLIGAPKTV AALLSGEMKD TAQLNQFSVY
GLEKFFSRSE RAMMVRTMGG VSSMLPKGGD VVWGNASWAP DDLNQTNFSN GAIIRYREDI
DKDHDEFDID DALQFLKNVT DDDFKVMLAK NYSHGLAWTE KEVLKNNEMP SKWINPLETS
LPYAPDMKIY CVHGVGKPTE RGYYYTNNPE GQPVIDSSVN DGTKVENGIV MDDGDGTLPI
LALGLVCNKV WQTKRFNPAN TSITNYEIKH EPAAFDLRGG PRSAEHVDIL GHSELNEIIL
KVSSGHGDSV PNRYISDIQE IINEINLDKP RN
