Reviewed, UniProtKB/Swiss-Prot O42916 (ALE1_SCHPO)

Names and origin

Protein names

Recommended name:
    Lysophospholipid acyltransferase
      Short name=LPLAT
    EC=2.3.1.51
    EC=2.3.1.23
Alternative name(s):
    1-acyl-sn-glycerol-3-phosphate acyltransferase
      Short name=AGPAT
    Lysophosphatidic acid acyltransferase
      Short name=LPAAT
    Lysophosphatidylethanolamine acyltransferase
      Short name=LPEAT
    Lysophosphatidylcholine acyltransferase
      Short name=LPCAT

Gene names

Name:	ale1
Synonyms:	lpt1
ORF Names:	SPBC16A3.10

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	509 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Membrane-bound O-acyltransferase that mediates the incorporation of unsaturated acyl chains into the sn-2 position of phopholipids. Ref.1
Catalytic activity	Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate. Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine. Acyl-CoA + 1-acyl-sn-glycero-3-phosphoethanolamine = CoA + 1,2-diacyl-sn-glycero-3-phosphoethanolamine.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Microsome membrane; Multi-pass membrane proteinBy similarity.
Sequence similarities	Belongs to the membrane-bound acyltransferase family.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred by curator. Source: GeneDB_SPombe integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-acylglycerol-3-phosphate O-acyltransferase activity Inferred from electronic annotation. Source: EC 1-acylglycerophosphocholine O-acyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 509	509	Lysophospholipid acyltransferase		PRO_0000315633
Regions
	Topological domain	1 – 14	14	Lumenal By similarity
	Transmembrane	15 – 35	21	Potential
	Topological domain	36 – 55	20	Cytoplasmic By similarity
	Transmembrane	56 – 76	21	Potential
	Topological domain	77 – 94	18	Lumenal By similarity
	Transmembrane	95 – 115	21	Potential
	Topological domain	116 – 223	108	Cytoplasmic By similarity
	Transmembrane	224 – 244	21	Potential
	Topological domain	245 – 246	2	Lumenal By similarity
	Transmembrane	247 – 267	21	Potential
	Topological domain	268 – 410	143	Cytoplasmic By similarity
	Transmembrane	411 – 431	21	Potential
	Topological domain	432 – 441	10	Lumenal By similarity
	Transmembrane	442 – 462	21	Potential
	Topological domain	463 – 509	47	Cytoplasmic By similarity
Sites
	Active site	363	1	By similarity
Amino acid modifications
	Modified residue	490	1	Phosphoserine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O42916-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 74B4E3E3D9DE65D9	FASTA	509	58,822
	10 20 30 40 50 60 MAYLIDIPFE YFSSFLGVHP DQLKLLFCFL SAYPFAGILK RLPSAPWIRN LFSISIGLFY 70 80 90 100 110 120 LIGVHHLYDG VLVLLFDALF TYFVAAFYRS SRMPWIIFIV ILGHTFSSHV IRYIYPSENT 130 140 150 160 170 180 DITASQMVLC MKLTAFAWSV YDGRLPSSEL SSYQKDRALR KIPNILYFLG YVFFFPSLLV 190 200 210 220 230 240 GPAFDYVDYE RFITLSMFKP LADPYEKQIT PHSLEPALGR CWRGLLWLIL FITGSSIYPL 250 260 270 280 290 300 KFLLTPKFAS SPILLKYGYV CITAFVARMK YYGAWELSDG ACILSGIGYN GLDSSKHPRW 310 320 330 340 350 360 DRVKNIDPIK FEFADNIKCA LEAWNMNTNK WLRNYVYLRV AKKGKRPGFK STLSTFTVSA 370 380 390 400 410 420 MWHGVSAGYY LTFVSAAFIQ TVAKYTRRHV RPFFLKPDME TPGPFKRVYD VIGMVATNLS 430 440 450 460 470 480 LSYLIISFLL LNLKESIHVW KELYFIVHIY ILIALAVFNS PIRSKLDNKI RSRVNSYKLK 490 500 SYEQSMKSTS DTDMLNMSVP KREDFENDE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"LPT1 encodes a membrane-bound O-acyltransferase involved in the acylation of lysophospholipids in the yeast Saccharomyces cerevisiae." Tamaki H., Shimada A., Itoh Y., Ohya M., Takase J., Miyashita M., Miyagawa H., Nozaki H., Nakayama R., Kumagai H. J. Biol. Chem. 282:34288-34298(2007) [PubMed: 17890783] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, FUNCTION.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB305042 mRNA. Translation: BAF93898.1. CU329671 Genomic DNA. Translation: CAA16861.1.
PIR	T39542.
RefSeq	NP_596779.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2539940.
KEGG	spo:SPBC16A3.10.
NMPDR	fig|4896.1.peg.2645.
Organism-specific databases
GeneDB_Spombe	SPBC16A3.10.
Gene expression databases
ArrayExpress	O42916.
Family and domain databases
InterPro	IPR004299. MBOAT_fam. [Graphical view]
Pfam	PF03062. MBOAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALE1_SCHPO

Accession

Primary (citable) accession number: O42916
Secondary accession number(s): A9EDQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	June 1, 1998
Last modified:	November 25, 2008
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)