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A6ZSP9 (LAG1_YEAS7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sphingosine N-acyltransferase LAG1

EC=2.3.1.24
Alternative name(s):
Longevity assurance factor 1
Longevity assurance protein 1
Gene names
Name:LAG1
ORF Names:SCY_2383
OrganismSaccharomyces cerevisiae (strain YJM789) (Baker's yeast) [Complete proteome]
Taxonomic identifier307796 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length411 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Component of the ceramide synthase complex required for C26-CoA-dependent ceramide synthesis. Redundant to LAC1. Facilites ER-to-Golgi transport of GPI-anchored proteins. Involved in the aging process By similarity.

Catalytic activity

Acyl-CoA + sphingosine = CoA + N-acylsphingosine.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the sphingosine N-acyltransferase family.

Contains 1 TLC (TRAM/LAG1/CLN8) domain.

Ontologies

Keywords
   Biological processLipid metabolism
Lipid synthesis
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionTransferase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processlipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionsphingosine N-acyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 411411Sphingosine N-acyltransferase LAG1
PRO_0000308913

Regions

Topological domain1 – 8181Cytoplasmic By similarity
Transmembrane82 – 10221Helical; Potential
Topological domain103 – 13432Lumenal By similarity
Transmembrane135 – 15521Helical; Potential
Topological domain156 – 17621Cytoplasmic By similarity
Transmembrane177 – 19721Helical; Potential
Topological domain198 – 21114Lumenal By similarity
Transmembrane212 – 23221Helical; Potential
Topological domain233 – 25119Cytoplasmic By similarity
Transmembrane252 – 27221Helical; Potential
Topological domain273 – 29624Lumenal By similarity
Transmembrane297 – 31721Helical; Potential
Topological domain318 – 35538Cytoplasmic By similarity
Transmembrane356 – 37621Helical; Potential
Topological domain377 – 41135Lumenal By similarity
Domain168 – 384217TLC

Amino acid modifications

Modified residue81Phosphoserine By similarity
Modified residue231Phosphoserine By similarity
Modified residue241Phosphoserine By similarity
Glycosylation1031N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
A6ZSP9 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: C3A2847B9613EB9E

FASTA41148,470
        10         20         30         40         50         60 
MTSATDKSID RLVVNAKTRR RNSSVGKIDL GDTVPGFAAM PESAASKNEA KKRMKALTGD 

        70         80         90        100        110        120 
SKKDSDLLWK VWFSYREMNY RHSWLTPFFI LVCVYSAYFL SGNRTESNPL HMFVAISYQV 

       130        140        150        160        170        180 
DGTDSYAKGI KDLSFVFFYM IFFTFLREFL MDVVIRPFTV YLNVTSEHRQ KRMLEQMYAI 

       190        200        210        220        230        240 
FYCGVSGPFG LYIMYHSDLW LFKTKPMYRT YPDITNPFLF KIFYLGQAAF WAQQACVLVL 

       250        260        270        280        290        300 
QLEKPRKDYK ELVFHHIVTL LLIWSSYVFH FTKMGLAIYI TMDVSDFFLS LSKTLNYLNS 

       310        320        330        340        350        360 
VFTPFVFGLF VFFWIYLRHV VNIRILWSVL TEFRHEGNYV LNFATQQYKC WISLPIVFVL 

       370        380        390        400        410 
IAALQLVNLY WLFLILRILY RLIWQGIQKD ERSDSDSDES AENEESKEKC E 

« Hide

References

[1]"Genome sequencing and comparative analysis of Saccharomyces cerevisiae strain YJM789."
Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z., Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X., Jia P., Luedi P., Oefner P.J., David L. expand/collapse author list , Dietrich F.S., Li Y., Davis R.W., Steinmetz L.M.
Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007) [PubMed: 17652520] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YJM789.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFW02000082 Genomic DNA. Translation: EDN62230.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.3.1.24. 984.

Family and domain databases

InterProIPR016439. Longevity_assurance_LAG1_LAC1.
IPR006634. TLC-dom.
IPR013599. TRAM1.
[Graphical view]
PfamPF08390. TRAM1. 1 hit.
PF03798. TRAM_LAG1_CLN8. 1 hit.
[Graphical view]
PIRSFPIRSF005225. LAG1_LAC1. 1 hit.
SMARTSM00724. TLC. 1 hit.
[Graphical view]
PROSITEPS50922. TLC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLAG1_YEAS7
AccessionPrimary (citable) accession number: A6ZSP9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: September 11, 2007
Last modified: May 31, 2011
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families