Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P40857 (PHS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 102. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase PHS1

EC=4.2.1.134
Alternative name(s):
3-hydroxyacyl-CoA dehydratase PHS1
Short name=HACD
PTPLA homolog involved in sphingolipid biosynthesis protein 1
Gene names
Name:PHS1
Ordered Locus Names:YJL097W
ORF Names:J0902
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the dehydration step in very long-chain fatty acid (VLCFA) synthesis. Ref.7 Ref.8

Catalytic activity

A very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] = a very-long-chain trans-2,3-dehydroacyl-[acyl-carrier protein] + H2O. Ref.7 Ref.8

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Vacuole membrane; Multi-pass membrane protein Ref.5 Ref.8.

Sequence similarities

Belongs to the very long-chain fatty acids dehydratase HACD family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 217217Very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase PHS1
PRO_0000203047

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 2918Helical; Potential
Topological domain30 – 4718Lumenal Potential
Transmembrane48 – 6619Helical; Potential
Topological domain67 – 7610Cytoplasmic Potential
Transmembrane77 – 9418Helical; Potential
Topological domain95 – 995Lumenal Potential
Transmembrane100 – 11718Helical; Potential
Topological domain118 – 14225Cytoplasmic Potential
Transmembrane143 – 16018Helical; Potential
Topological domain161 – 17818Lumenal Potential
Transmembrane179 – 19618Helical; Potential
Topological domain197 – 21721Cytoplasmic Potential
Motif214 – 2174Endoplasmic reticulum retention signal

Sites

Active site1491 Probable
Active site1561 Probable

Experimental info

Mutagenesis1491Y → A: No catalytic activity. Ref.8
Mutagenesis1561E → A: No catalytic activity. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P40857 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 5C87BC9563FB83AA

FASTA21724,511
        10         20         30         40         50         60 
MSKKLASPLS FLPLYNLLSA VGWSYLLYLV ISLYPKVGQP AFFYQTKNVA TLVQCGAIIE 

        70         80         90        100        110        120 
IINSFLGVVR SPLLTTVAQV SSRLLVVLGI FQLLPNTSGV QSVVYISLLL AWSITEIVRY 

       130        140        150        160        170        180 
LYYFFMLVFK NGAPKILILL RYNLFWILYP TGVASELRII YCALNAAESQ YSLLYKRILI 

       190        200        210 
AAMLAYIPGF PMLFLHMVAQ RKKVMKSLRS SFGKKLI 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and function analysis of a 9.74 kb fragment of Saccharomyces cerevisiae chromosome X including the BCK1 gene."
Miosga T., Boles E., Schaaff-Gerstenschlaeger I., Schmitt S., Zimmermann F.K.
Yeast 10:1481-1488(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[7]"A molecular caliper mechanism for determining very long-chain fatty acid length."
Denic V., Weissman J.S.
Cell 130:663-677(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[8]"Membrane topology and essential amino acid residues of Phs1, a 3-hydroxyacyl-CoA dehydratase involved in very long-chain fatty acid elongation."
Kihara A., Sakuraba H., Ikeda M., Denpoh A., Igarashi Y.
J. Biol. Chem. 283:11199-11209(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF TYR-149 AND GLU-156, ACTIVE SITE, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X77923 Genomic DNA. Translation: CAA54893.1.
Z49372 Genomic DNA. Translation: CAA89391.1.
AY557855 Genomic DNA. Translation: AAS56181.1.
BK006943 Genomic DNA. Translation: DAA08703.1.
PIRS50296.
RefSeqNP_012438.1. NM_001181530.1.

3D structure databases

ProteinModelPortalP40857.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33660. 27 interactions.
DIPDIP-2104N.
IntActP40857. 31 interactions.
MINTMINT-534987.
STRING4932.YJL097W.

Proteomic databases

PaxDbP40857.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJL097W; YJL097W; YJL097W.
GeneID853348.
KEGGsce:YJL097W.

Organism-specific databases

CYGDYJL097w.
SGDS000003633. PHS1.

Phylogenomic databases

eggNOGCOG5198.
GeneTreeENSGT00530000062962.
HOGENOMHOG000190538.
KOK10703.
OMAGEFTKWT.
OrthoDBEOG7NKKXC.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17327.
YEAST:G3O-31552-MONOMER.
YEAST:MONOMER3O-85.

Gene expression databases

GenevestigatorP40857.

Family and domain databases

InterProIPR007482. Tyr_Pase-like_PTPLA.
[Graphical view]
PANTHERPTHR11035. PTHR11035. 1 hit.
PfamPF04387. PTPLA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio973747.

Entry information

Entry namePHS1_YEAST
AccessionPrimary (citable) accession number: P40857
Secondary accession number(s): D6VW87
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 19, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Yeast

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

SIMILARITY comments

Index of protein domains and families