Q9QZU4 · PLAT1_MOUSE

  • Protein
    Phospholipase A and acyltransferase 1
  • Gene
    Plaat1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Exhibits both phospholipase A1/2 and acyltransferase activities (By similarity).
Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:21880860).
Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (By similarity).
Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (By similarity).

Catalytic activity

  • a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+
    This reaction proceeds in the forward direction.
    EC:3.1.1.4 (UniProtKB | ENZYME | Rhea)
  • a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+
    This reaction proceeds in the forward direction.
    EC:3.1.1.32 (UniProtKB | ENZYME | Rhea)
  • 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + hexadecanoate
    This reaction proceeds in the forward direction.
  • 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + hexadecanoate
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + H+ + hexadecanoate
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H+
    This reaction proceeds in the forward direction.
  • 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine = H+ + hexadecanoyl-sn-glycero-3-phosphocholine + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine
    This reaction proceeds in the forward direction.
  • 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + a 2-acyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + 2-hexadecanoyl-sn-glycero-3-phosphocholine
    This reaction proceeds in the forward direction.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site30
Active site119Acyl-thioester intermediate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentendoplasmic reticulum
Cellular Componentlysosome
Cellular Componentmembrane
Cellular Componentmitochondrion
Cellular Componentnuclear envelope lumen
Cellular Componentnucleus
Cellular Componentperoxisome
Molecular Function1-acyl-2-lysophosphatidylserine acylhydrolase activity
Molecular FunctionN-acyltransferase activity
Molecular FunctionO-acyltransferase activity
Molecular Functionphosphatidylserine 1-acylhydrolase activity
Molecular Functionphospholipase A1 activity
Molecular Functionphospholipase A2 activity
Molecular Functionphospholipase activity
Biological Processether lipid metabolic process
Biological Processlens fiber cell differentiation
Biological Processlipid catabolic process
Biological ProcessN-acylphosphatidylethanolamine metabolic process
Biological Processorganelle disassembly
Biological Processperoxisome organization
Biological Processphosphatidylcholine metabolic process
Biological ProcessRas protein signal transduction
Biological Processregulation of cell growth

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phospholipase A and acyltransferase 1
  • EC number
  • Alternative names
    • HRAS-like suppressor 1
      (HRSL1)
    • Phospholipid-metabolizing enzyme A-C1

Gene names

    • Name
      Plaat1
    • Synonyms
      Hrasls
      , Hrasrs

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9QZU4
  • Secondary accessions
    • Q5D099
    • Q9D0S3

Proteomes

Organism-specific databases

Subcellular Location

Isoform 1

Membrane
; Single-pass membrane protein
Cytoplasm

Isoform 2

Nucleus
Cytoplasm

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-138Cytoplasmic
Transmembrane139-159Helical
Topological domain160-167Lumenal

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001524821-167Phospholipase A and acyltransferase 1

Proteomic databases

PTM databases

Expression

Tissue specificity

Isoform 1

Expressed in skeletal muscle, heart, brain, bone marrow and testis.

Isoform 2

Abundantly expressed in brain, heart, and skeletal muscle.

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain20-135LRAT

Sequence similarities

Belongs to the H-rev107 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q9QZU4-1

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.

  • Name
    1
  • Synonyms
    PLAAT-1S
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    167
  • Mass (Da)
    18,810
  • Last updated
    2000-05-01 v1
  • Checksum
    619C43691DCC86C8
MAVNDCFSLTYPHNPHPGDLIEVFRPCYQHWALYLGDGYVINIAPIDGIRSSFTSAKSVFSTKALVKMQLLKDVVGNDTYRINNKYDTTYPPLPVEEVIQRSEFPIGQEVAYDLLVNNCEHFVTLLRYGEGVSEQANRAIGTIGLVAAGIDIFTFLGLFPKRQRTKY

Q9QZU4-2

  • Name
    2
  • Synonyms
    PLAAT-1L
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-1: M → MPEACLEDLGGGEGAGLGRAPKTRGRRQGPQDAVWQARARNPRRDQRWRGARTLALTQRREAVVALAVALASGRCGWSHPGSASGTAASPWRTREARHCLQGTKTTQLEQM

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0R4J130A0A0R4J130_MOUSEPlaat1167
E0CYE9E0CYE9_MOUSEPlaat150

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0601911in isoform 2
Sequence conflict105in Ref. 1; BAB23348

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF163095
EMBL· GenBank· DDBJ
AAF13304.1
EMBL· GenBank· DDBJ
mRNA
AB510982
EMBL· GenBank· DDBJ
BAI63211.1
EMBL· GenBank· DDBJ
mRNA
AK004528
EMBL· GenBank· DDBJ
BAB23348.1
EMBL· GenBank· DDBJ
mRNA
AK039471
EMBL· GenBank· DDBJ
BAC30361.1
EMBL· GenBank· DDBJ
mRNA
AC154448
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH466521
EMBL· GenBank· DDBJ
EDK97707.1
EMBL· GenBank· DDBJ
Genomic DNA
CH466521
EMBL· GenBank· DDBJ
EDK97708.1
EMBL· GenBank· DDBJ
Genomic DNA
BC048482
EMBL· GenBank· DDBJ
AAH48482.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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