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P33333 (PLSC_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase
Short name=1-AGP acyltransferase
Short name=1-AGPAT
EC=2.3.1.51
Alternative name(s):
Lysophosphatidic acid acyltransferase
Short name=LPAAT
Gene names
Name:SLC1
Ordered Locus Names:YDL052C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be an acyltransferase with an altered substrate specificity that enables it to use a C-26-CoA in place of the C-16 or C-18-CoAs used by the wild-type protein.

Catalytic activity

Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.

Subcellular location

Membrane; Single-pass membrane protein Potential.

Domain

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity.

Sequence similarities

Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglycerophospholipid biosynthetic process

Inferred from genetic interaction. Source: SGD

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lipid particle

Inferred from direct assay. Source: SGD

   Molecular function1-acylglycerol-3-phosphate O-acyltransferase activity

Inferred from direct assay. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase
PRO_0000208189

Regions

Transmembrane16 – 3015Helical; Potential
Motif82 – 876HXXXXD motif

Natural variations

Natural variant441Q → L in allele suppressor SLC1-1.

Experimental info

Sequence conflict1151W → R in AAT92911. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P33333 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 36ECBBC2659655EB

FASTA30333,887
        10         20         30         40         50         60 
MSVIGRFLYY LRSVLVVLAL AGCGFYGVIA SILCTLIGKQ HLAQWITARC FYHVMKLMLG 

        70         80         90        100        110        120 
LDVKVVGEEN LAKKPYIMIA NHQSTLDIFM LGRIFPPGCT VTAKKSLKYV PFLGWFMALS 

       130        140        150        160        170        180 
GTYFLDRSKR QEAIDTLNKG LENVKKNKRA LWVFPEGTRS YTSELTMLPF KKGAFHLAQQ 

       190        200        210        220        230        240 
GKIPIVPVVV SNTSTLVSPK YGVFNRGCMI VRILKPISTE NLTKDKIGEF AEKVRDQMVD 

       250        260        270        280        290        300 
TLKEIGYSPA INDTTLPPQA IEYAALQHDK KVNKKIKNEP VPSVSISNDV NTHNEGSSVK 


KMH

« Hide

References

« Hide 'large scale' references
[1]"A suppressor gene that enables Saccharomyces cerevisiae to grow without making sphingolipids encodes a protein that resembles an Escherichia coli fatty acyltransferase."
Nagiec M.M., Wells G.B., Lester R.L., Dickson R.C.
J. Biol. Chem. 268:22156-22163(1993) [PubMed: 8408076] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L13282 Unassigned DNA. Translation: AAA16514.1.
Z74100 Genomic DNA. Translation: CAA98614.1.
AY692892 Genomic DNA. Translation: AAT92911.1.
BK006938 Genomic DNA. Translation: DAA11804.1.
PIRA48600.
RefSeqNP_010231.1. NM_001180111.1.

3D structure databases

ProteinModelPortalP33333.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5136N.
IntActP33333. 58 interactions.
MINTMINT-519109.
STRINGP33333.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL052C; YDL052C; YDL052C.
GeneID851508.
KEGGsce:YDL052C.
NMPDRfig|4932.3.peg.971.

Organism-specific databases

CYGDYDL052c.
SGDS000002210. SLC1.

Phylogenomic databases

eggNOGfuNOG07013.
HOGENOMHBG736534.
OMAGCTVTAK.
OrthoDBEOG4K9FNN.

Gene expression databases

ArrayExpressP33333.
GenevestigatorP33333.
GermOnlineYDL052C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR002123. Acyltransferase.
IPR004552. AGP_acyltrans.
[Graphical view]
KOK13509.
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsTIGR00530. AGP_acyltrn. 1 hit.
ProtoNetSearch...

Other

NextBio968866.

Entry information

Entry namePLSC_YEAST
AccessionPrimary (citable) accession number: P33333
Secondary accession number(s): D6VRU4, E9P8Y5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: December 14, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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