ALE1_SCHPO
ID ALE1_SCHPO Reviewed; 509 AA.
AC O42916; A9EDQ0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Lysophospholipid acyltransferase;
DE Short=LPLAT;
DE EC=2.3.1.23;
DE EC=2.3.1.51;
DE AltName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase;
DE Short=AGPAT;
DE AltName: Full=Lysophosphatidic acid acyltransferase;
DE Short=LPAAT;
DE AltName: Full=Lysophosphatidylcholine acyltransferase;
DE Short=LPCAT;
DE AltName: Full=Lysophosphatidylethanolamine acyltransferase;
DE Short=LPEAT;
GN Name=ale1; Synonyms=lpt1; ORFNames=SPBC16A3.10;
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 [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17890783; DOI=10.1074/jbc.m704509200;
RA Tamaki H., Shimada A., Itoh Y., Ohya M., Takase J., Miyashita M.,
RA Miyagawa H., Nozaki H., Nakayama R., Kumagai H.;
RT "LPT1 encodes a membrane-bound O-acyltransferase involved in the acylation
RT of lysophospholipids in the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 282:34288-34298(2007).
RN [2]
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 [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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Membrane-bound O-acyltransferase that mediates the
CC incorporation of unsaturated acyl chains into the sn-2 position of
CC phospholipids. {ECO:0000269|PubMed:17890783}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a
CC 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:64612;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Microsome membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB305042; BAF93898.1; -; mRNA.
DR EMBL; CU329671; CAA16861.1; -; Genomic_DNA.
DR PIR; T39542; T39542.
DR RefSeq; NP_596779.1; NM_001023800.2.
DR AlphaFoldDB; O42916; -.
DR SMR; O42916; -.
DR BioGRID; 276484; 14.
DR STRING; 4896.SPBC16A3.10.1; -.
DR iPTMnet; O42916; -.
DR MaxQB; O42916; -.
DR PaxDb; O42916; -.
DR PRIDE; O42916; -.
DR EnsemblFungi; SPBC16A3.10.1; SPBC16A3.10.1:pep; SPBC16A3.10.
DR GeneID; 2539940; -.
DR KEGG; spo:SPBC16A3.10; -.
DR PomBase; SPBC16A3.10; ale1.
DR VEuPathDB; FungiDB:SPBC16A3.10; -.
DR eggNOG; KOG2704; Eukaryota.
DR HOGENOM; CLU_011340_5_0_1; -.
DR InParanoid; O42916; -.
DR OMA; WHGTRPG; -.
DR PhylomeDB; O42916; -.
DR Reactome; R-SPO-1482788; Acyl chain remodelling of PC.
DR Reactome; R-SPO-1482801; Acyl chain remodelling of PS.
DR Reactome; R-SPO-1482839; Acyl chain remodelling of PE.
DR Reactome; R-SPO-1482922; Acyl chain remodelling of PI.
DR PRO; PR:O42916; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; ISO:PomBase.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; ISO:PomBase.
DR GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IC:PomBase.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Microsome; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..509
FT /note="Lysophospholipid acyltransferase"
FT /id="PRO_0000315633"
FT TOPO_DOM 1..14
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..94
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..246
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..441
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 488..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 363
FT /evidence="ECO:0000250"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 509 AA; 58822 MW; 74B4E3E3D9DE65D9 CRC64;
MAYLIDIPFE YFSSFLGVHP DQLKLLFCFL SAYPFAGILK RLPSAPWIRN LFSISIGLFY
LIGVHHLYDG VLVLLFDALF TYFVAAFYRS SRMPWIIFIV ILGHTFSSHV IRYIYPSENT
DITASQMVLC MKLTAFAWSV YDGRLPSSEL SSYQKDRALR KIPNILYFLG YVFFFPSLLV
GPAFDYVDYE RFITLSMFKP LADPYEKQIT PHSLEPALGR CWRGLLWLIL FITGSSIYPL
KFLLTPKFAS SPILLKYGYV CITAFVARMK YYGAWELSDG ACILSGIGYN GLDSSKHPRW
DRVKNIDPIK FEFADNIKCA LEAWNMNTNK WLRNYVYLRV AKKGKRPGFK STLSTFTVSA
MWHGVSAGYY LTFVSAAFIQ TVAKYTRRHV RPFFLKPDME TPGPFKRVYD VIGMVATNLS
LSYLIISFLL LNLKESIHVW KELYFIVHIY ILIALAVFNS PIRSKLDNKI RSRVNSYKLK
SYEQSMKSTS DTDMLNMSVP KREDFENDE
