Q9VPD3 · PTSS_DROME

Function

function

Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) is replaced by L-serine.

Catalytic activity

Pathway

Phospholipid metabolism; phosphatidylserine biosynthesis.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentendomembrane system
Cellular Componentendoplasmic reticulum membrane
Molecular FunctionL-serine-phosphatidylcholine phosphatidyltransferase activity
Molecular FunctionL-serine-phosphatidylethanolamine phosphatidyltransferase activity
Molecular Functionphosphotransferase activity, for other substituted phosphate groups
Biological Processphosphatidylserine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphatidylserine synthase
  • EC number

Gene names

    • Name
      Pss
    • Synonyms
      l(3)77CDf
      , ptdss1
    • ORF names
      CG4825

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    Q9VPD3
  • Secondary accessions
    • M9PIC3

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-92Cytoplasmic
Transmembrane93-113Helical
Topological domain114-122Lumenal
Transmembrane123-143Helical
Topological domain144-153Cytoplasmic
Transmembrane154-174Helical
Topological domain175-239Lumenal
Transmembrane240-260Helical
Topological domain261-266Cytoplasmic
Transmembrane267-287Helical
Topological domain288-339Lumenal
Transmembrane340-360Helical
Topological domain361-367Cytoplasmic
Transmembrane368-388Helical
Topological domain389-402Lumenal
Transmembrane403-423Helical
Topological domain424-436Cytoplasmic
Transmembrane437-457Helical
Topological domain458-498Lumenal

Keywords

Phenotypes & Variants

Disruption phenotype

Lethal at the first instar larval stage (PubMed:31869331).
RNAi-mediated knockdown in salivary glands reduces phosphatidylserine (PS) levels and depletes Akt1 from the plasma membrane contributing to cell growth defects probably by affecting the insulin pathway; causes a shift from phospholipid synthesis to neutral lipid synthesis, which results in ectopic lipid accumulation in third instar larval salivary glands; reduces mitochondrial PS levels thereby impairing mitochondrial protein import and mitochondrial integrity (PubMed:31869331).

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00004508221-498Phosphatidylserine synthase
Glycosylation205N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-65Disordered
Compositional bias7-21Polar residues
Compositional bias465-488Polar residues
Region465-498Disordered

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q9VPD3-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    498
  • Mass (Da)
    56,835
  • Last updated
    2000-05-01 v1
  • Checksum
    617134A5D78F028E
MKKRTNSRGTPTSSGDALLDTSFSSAGDAERDHPAYKSGAASAPATPTKRRDGSDGSVSSAGARRKRKDEIAQTFVIVNERPVDDISLDFFYKPHTITLLAVSVLAVMYFAFVRNEANVDENLWAGLLCIVFFFLIVSVIAFPNGPFTRPHPAVWRILFGCSVLYLLTLQFLMFQNYPTIRSIFYWIDPKLKNFHIDMEKEYGVNCSDISWDRVKGHLDVFAWGHFLGWAFKAILIRHMGILWAISVMWEITEITFAHLLPNFIECWWDALILDVIICNGLGIWMGLKICQILEMREYKWASIKDISTTTGKIKRAMLQFTPESWSAIRWLDPKSTAMRFAAVIQLVIFWQVTELNTFFLKHIFEMPPDHFIVIGRLIFIGLFVAPSVRQYYVYVTDTRCKRVGTQCWVYGAIMVSEAILCIKNGKELFERTQAINIVLWLTVQVIISVAFVYLAVYWQQRQLKKVSSTPAKTKETIPASSSSPSKGKLSPQKEKKLK

Q9VPD3-2

  • Name
    B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for compositional bias, alternative sequence.

TypeIDPosition(s)Description
Compositional bias7-21Polar residues
Alternative sequenceVSP_060726459in isoform B
Compositional bias465-488Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE014296
EMBL· GenBank· DDBJ
AAF51622.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014296
EMBL· GenBank· DDBJ
AGB94811.1
EMBL· GenBank· DDBJ
Genomic DNA
AY069402
EMBL· GenBank· DDBJ
AAL39547.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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