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Protein

Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PHS1

Gene

PHS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.2 Publications

Catalytic activityi

A very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain trans-2,3-dehydroacyl-CoA + H2O.2 Publications

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.2 Publications
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1491 Publication1
Active sitei1561 Publication1

GO - Molecular functioni

GO - Biological processi

  • cell differentiation Source: EnsemblPlants
  • fatty acid elongation Source: SGD
  • negative regulation of developmental growth Source: EnsemblPlants
  • negative regulation of peptidyl-tyrosine phosphorylation Source: EnsemblPlants
  • regulation of cell division Source: EnsemblPlants
  • sphingolipid biosynthetic process Source: SGD
  • vacuolar transport Source: SGD
  • very long-chain fatty acid biosynthetic process Source: GO_Central

Keywordsi

Molecular functionLyase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-85
YEAST:MONOMER3O-85
ReactomeiR-SCE-75876 Synthesis of very long-chain fatty acyl-CoAs
UniPathwayiUPA00094

Chemistry databases

SwissLipidsiSLP:000000492

Names & Taxonomyi

Protein namesi
Recommended name:
Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PHS1Curated (EC:4.2.1.1342 Publications)
Alternative name(s):
3-hydroxyacyl-CoA dehydratase PHS1
Short name:
HACD
PTPLA homolog involved in sphingolipid biosynthesis protein 1
Gene namesi
Name:PHS1
Ordered Locus Names:YJL097W
ORF Names:J0902
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL097W
SGDiS000003633 PHS1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 11CytoplasmicSequence analysisAdd BLAST11
Transmembranei12 – 29HelicalSequence analysisAdd BLAST18
Topological domaini30 – 47LumenalSequence analysisAdd BLAST18
Transmembranei48 – 66HelicalSequence analysisAdd BLAST19
Topological domaini67 – 76CytoplasmicSequence analysis10
Transmembranei77 – 94HelicalSequence analysisAdd BLAST18
Topological domaini95 – 99LumenalSequence analysis5
Transmembranei100 – 117HelicalSequence analysisAdd BLAST18
Topological domaini118 – 142CytoplasmicSequence analysisAdd BLAST25
Transmembranei143 – 160HelicalSequence analysisAdd BLAST18
Topological domaini161 – 178LumenalSequence analysisAdd BLAST18
Transmembranei179 – 196HelicalSequence analysisAdd BLAST18
Topological domaini197 – 217CytoplasmicSequence analysisAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi149Y → A: No catalytic activity. 1 Publication1
Mutagenesisi156E → A: No catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002030471 – 217Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PHS1Add BLAST217

Proteomic databases

PaxDbiP40857
PRIDEiP40857
TopDownProteomicsiP40857

PTM databases

CarbonylDBiP40857

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CREB3L1Q96BA83EBI-26003,EBI-6942903From Homo sapiens.

Protein-protein interaction databases

BioGridi33660266 interactors.
DIPiDIP-2104N
IntActiP40857 34 interactors.
STRINGi4932.YJL097W

Structurei

3D structure databases

ProteinModelPortaliP40857
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi214 – 217Endoplasmic reticulum retention signal4

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000062962
HOGENOMiHOG000190538
InParanoidiP40857
KOiK10703
OMAiSYILWQL
OrthoDBiEOG092C4NVA

Family and domain databases

InterProiView protein in InterPro
IPR007482 Tyr_Pase-like_PTPLA
PANTHERiPTHR11035 PTHR11035, 1 hit
PfamiView protein in Pfam
PF04387 PTPLA, 1 hit

Sequencei

Sequence statusi: Complete.

P40857-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKKLASPLS FLPLYNLLSA VGWSYLLYLV ISLYPKVGQP AFFYQTKNVA
60 70 80 90 100
TLVQCGAIIE IINSFLGVVR SPLLTTVAQV SSRLLVVLGI FQLLPNTSGV
110 120 130 140 150
QSVVYISLLL AWSITEIVRY LYYFFMLVFK NGAPKILILL RYNLFWILYP
160 170 180 190 200
TGVASELRII YCALNAAESQ YSLLYKRILI AAMLAYIPGF PMLFLHMVAQ
210
RKKVMKSLRS SFGKKLI
Length:217
Mass (Da):24,511
Last modified:February 1, 1995 - v1
Checksum:i5C87BC9563FB83AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77923 Genomic DNA Translation: CAA54893.1
Z49372 Genomic DNA Translation: CAA89391.1
AY557855 Genomic DNA Translation: AAS56181.1
BK006943 Genomic DNA Translation: DAA08703.1
PIRiS50296
RefSeqiNP_012438.1, NM_001181530.1

Genome annotation databases

EnsemblFungiiYJL097W; YJL097W; YJL097W
GeneIDi853348
KEGGisce:YJL097W

Similar proteinsi

Entry informationi

Entry nameiHACD_YEAST
AccessioniPrimary (citable) accession number: P40857
Secondary accession number(s): D6VW87
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: March 28, 2018
This is version 135 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome