LOA1_SCHPO
ID LOA1_SCHPO Reviewed; 300 AA.
AC Q9US27;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Putative lysophosphatidic acid:oleoyl-CoA acyltransferase;
DE Short=LPAAT;
DE Short=Lysophosphatidic acid acyltransferase;
DE EC=2.3.1.51;
DE AltName: Full=Vacuolar protein sorting-associated protein 66;
GN Name=vps66; ORFNames=SPAC1783.02c;
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 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: Acyl-CoA-dependent lysophosphatidic acid acyltransferase with
CC preference for oleoyl-CoA. Involved in triacylglyceride homeostasis and
CC lipid droplet formation. Involved in vacuolar protein sorting (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane
CC protein {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:16823372}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16823372}. Note=Lipid droplets consist of a surface
CC phospholipid monolayer and a hydrophobic interior. The latter makes
CC embedding of proteins containing transmembrane segments difficult, and
CC these may instead adopt a hairpin or monotonic conformation when
CC associated with lipid droplet membranes (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB66165.2; -; Genomic_DNA.
DR PIR; T50104; T50104.
DR RefSeq; NP_593657.2; NM_001019089.2.
DR AlphaFoldDB; Q9US27; -.
DR BioGRID; 278826; 3.
DR STRING; 4896.SPAC1783.02c.1; -.
DR MaxQB; Q9US27; -.
DR PaxDb; Q9US27; -.
DR EnsemblFungi; SPAC1783.02c.1; SPAC1783.02c.1:pep; SPAC1783.02c.
DR GeneID; 2542362; -.
DR KEGG; spo:SPAC1783.02c; -.
DR PomBase; SPAC1783.02c; vps66.
DR VEuPathDB; FungiDB:SPAC1783.02c; -.
DR eggNOG; KOG2898; Eukaryota.
DR HOGENOM; CLU_048121_1_0_1; -.
DR InParanoid; Q9US27; -.
DR OMA; KFTRWRD; -.
DR PRO; PR:Q9US27; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; ISO:PomBase.
DR GO; GO:0019915; P:lipid storage; IC:PomBase.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISO:PomBase.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Endoplasmic reticulum; Golgi apparatus; Lipid droplet;
KW Lipid metabolism; Membrane; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..300
FT /note="Putative lysophosphatidic acid:oleoyl-CoA
FT acyltransferase"
FT /id="PRO_0000356186"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 115..120
FT /note="HXXXXD motif"
SQ SEQUENCE 300 AA; 33247 MW; 51FD291755328F20 CRC64;
MEKFTRWRDP GTGIAPFHPI NTETPSGFNF KWILIVVVMI LRVPLCIISV TLWFLWSCFL
KPILSIQPKL SFFIDSSLSR LLLLCFGCLK LSKSTSGSFV QGDSLQPGDI LAVNHSSPLD
VLVLSCLYNC TFAVCDSKTS NVSIISAQAY FWSCFFSPSK LKITDAKPLA KVAAKASKIG
TVVILFPEGV CTNGRALCQF TPCFDSAKET DRIFPLYIKY LPPCVTLPVP SLLSFARSVL
LTVSFEIRIR FSAEPLIPRN CTDVTESAQE VLSKLGRSRV VKLGKSDKLS YLDARSKKHV
