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O42916 (ALE1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysophospholipid acyltransferase
Short name=LPLAT
EC=2.3.1.23
EC=2.3.1.51
Alternative name(s):
1-acyl-sn-glycerol-3-phosphate acyltransferase
Short name=AGPAT
Lysophosphatidic acid acyltransferase
Short name=LPAAT
Lysophosphatidylcholine acyltransferase
Short name=LPCAT
Lysophosphatidylethanolamine acyltransferase
Short name=LPEAT
Gene names
Name:ale1
Synonyms:lpt1
ORF Names:SPBC16A3.10
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Protein existenceEvidence 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 protein By similarity Ref.1 Ref.3.

Sequence similarities

Belongs to the membrane-bound acyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 509509Lysophospholipid acyltransferase
PRO_0000315633

Regions

Topological domain1 – 1414Lumenal By similarity
Transmembrane15 – 3521Helical; Potential
Topological domain36 – 5520Cytoplasmic By similarity
Transmembrane56 – 7621Helical; Potential
Topological domain77 – 9418Lumenal By similarity
Transmembrane95 – 11521Helical; Potential
Topological domain116 – 223108Cytoplasmic By similarity
Transmembrane224 – 24421Helical; Potential
Topological domain245 – 2462Lumenal By similarity
Transmembrane247 – 26721Helical; Potential
Topological domain268 – 410143Cytoplasmic By similarity
Transmembrane411 – 43121Helical; Potential
Topological domain432 – 44110Lumenal By similarity
Transmembrane442 – 46221Helical; Potential
Topological domain463 – 50947Cytoplasmic By similarity

Sites

Active site3631 By similarity

Amino acid modifications

Modified residue4901Phosphoserine Ref.4

Sequences

Sequence LengthMass (Da)Tools
O42916 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 74B4E3E3D9DE65D9

FASTA50958,822
        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

« Hide

References

« Hide '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. expand/collapse author list , 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: 972 / ATCC 24843.
[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

EMBL
GenBank
DDBJ		AB305042 mRNA. Translation: BAF93898.1.
CU329671 Genomic DNA. Translation: CAA16861.1.
PIRT39542.
RefSeqNP_596779.1. NM_001023800.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO42916.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC16A3.10.1; SPBC16A3.10.1:pep; SPBC16A3.10.
GeneID2539940.
GenomeReviewsGene locus ale1 in contig CU329671_GR.
KEGGspo:SPBC16A3.10.
NMPDRfig|4896.1.peg.2645.

Organism-specific databases

GeneDB_SpombeSPBC16A3.10.

Phylogenomic databases

eggNOGfuNOG05319.
GeneTreeEFGT00050000006723.
HOGENOMHBG737510.
OMATCNFMGI.
OrthoDBEOG4RNFHS.

Gene expression databases

ArrayExpressO42916.

Family and domain databases

InterProIPR004299. MBOAT_fam.
[Graphical view]
KOK13519.
PfamPF03062. MBOAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALE1_SCHPO
AccessionPrimary (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: December 14, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents