Q61206 · PA1B2_MOUSE

  • Protein
    Platelet-activating factor acetylhydrolase IB subunit alpha2
  • Gene
    Pafah1b2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Alpha2 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF. The activity and substrate specificity of PAF-AH (I) are affected by its subunit composition. The alpha2/alpha2 homodimer (PAFAH1B2/PAFAH1B2 homodimer) hydrolyzes PAF and 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE) more efficiently than 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA). In contrast, the alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B3 heterodimer) hydrolyzes AAGPA more efficiently than PAF, but has little hydrolytic activity towards AAGPE (By similarity).
May play a role in male germ cell meiosis during the late pachytenestage and meiotic divisions as well as early spermiogenesis (PubMed:12775763).

Miscellaneous

Originally the subunits of the type I platelet-activating factor (PAF) acetylhydrolase was named alpha (PAFAH1B1), beta (PAFAH1B2) and gamma (PAFAH1B3) (By similarity).
Now these subunits have been renamed beta (PAFAH1B1), alpha2 (PAFAH1B2) and alpha1 (PAFAH1B3) respectively (By similarity).

Catalytic activity

Activity regulation

Beta subunit (PAFAH1B1) stimulates the acetylhydrolase activity of the alpha2/alpha2 catalytic homodimer.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site48
Active site193
Active site196

GO annotations

AspectTerm
Cellular Component1-alkyl-2-acetylglycerophosphocholine esterase complex
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentfibrillar center
Cellular Componentplasma membrane
Molecular Function1-alkyl-2-acetylglycerophosphocholine esterase activity
Molecular Functionidentical protein binding
Molecular Functionplatelet-activating factor acetyltransferase activity
Molecular Functionprotein heterodimerization activity
Molecular Functionprotein homodimerization activity
Molecular Functionprotein-containing complex binding
Biological Processlipid catabolic process
Biological Processpositive regulation of macroautophagy
Biological Processspermatogenesis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Platelet-activating factor acetylhydrolase IB subunit alpha2
  • EC number
  • Alternative names
    • PAF acetylhydrolase 30 kDa subunit (PAF-AH 30 kDa subunit)
    • PAF-AH subunit beta (PAFAH subunit beta)

Gene names

    • Name
      Pafah1b2
    • Synonyms
      Pafahb

Organism names

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

Accessions

  • Primary accession
    Q61206
  • Secondary accessions
    • Q6PKE6
    • Q7TNP3

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Knockout mice which are homozygous for the PAFAH1B2 gene appear developmentally normal, and are born at the expected Mendelian rate (PubMed:12775763).
Females bred normally, whereas male are infertile, and spermatogenesis is disrupted at mid- or late pachytene stages of meiosis or early spermiogenesis (PubMed:12775763).
Double mutant female mice which are homozygous for PAFAH1B2 and PAFAH1B3 are grossly normal and fertile, whereas double-mutant males are infertile. Double mutan mice manifest an earlier disturbance of spermatogenesis with an onset at preleptotene or leptotene stages of meiosis (PubMed:12775763).

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 6 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
Modified residue2Phosphoserine
ChainPRO_00000581522-229Platelet-activating factor acetylhydrolase IB subunit alpha2
Modified residue64Phosphoserine
Modified residue220Phosphothreonine

Keywords

Proteomic databases

2D gel databases

PTM databases

Expression

Developmental stage

Expressed already by the time of neurulation. By 10.5 dpc, expression is abundant in the developing central and peripheral nervous systems. Major sites include the neuroepithelium of the fore-, mid-, and hindbrain, the spinal cord, the dorsal root, and cranial ganglia.

Gene expression databases

Interaction

Subunit

Forms a catalytic dimer which is either homodimer (alpha2/alpha2 homodimer) or heterodimer with PAFAH1B3 (alpha2/alpha1 heterodimer). Component of the cytosolic (PAF-AH (I)) heterotetrameric enzyme, which is composed of PAFAH1B1 (beta), PAFAH1B2 (alpha2) and PAFAH1B3 (alpha1) subunits. The catalytic activity of the enzyme resides in the alpha1 (PAFAH1B3) and alpha2 (PAFAH1B2) subunits, whereas the beta subunit (PAFAH1B1) has regulatory activity. Trimer formation is not essential for the catalytic activity (By similarity).
Interacts (homodimer form) with PAFAH1B1 (homodimer form); PAFAH1B2 competes with NDEL1 for PAFAH1B1 binding (By similarity).
Interacts with VLDLR; this interaction may modulate the Reelin pathway (PubMed:17330141).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q61206Nudc O356852EBI-7445518, EBI-911192

Protein-protein interaction databases

Chemistry

Miscellaneous

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    229
  • Mass (Da)
    25,581
  • Last updated
    2007-05-01 v2
  • Checksum
    B4D24048621AB182
MSQGDSNPAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQYEIWRELFSPLHALNFGIGGDTTRHVLWRLKNGELENIKPKVIVVWVGTNNHENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDIDGGFVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEETPEEKQTTIA

Computationally mapped potential isoform sequences

There are 6 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1L1SVK0A0A1L1SVK0_MOUSEPafah1b2197
A0A1L1SSP3A0A1L1SSP3_MOUSEPafah1b222
A0A1L1SSQ5A0A1L1SSQ5_MOUSEPafah1b278
A0A1L1SQV7A0A1L1SQV7_MOUSEPafah1b2107
A0A1L1SRD0A0A1L1SRD0_MOUSEPafah1b297
A0A1L1SQ76A0A1L1SQ76_MOUSEPafah1b288

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict129-130in Ref. 1; AAC52997
Sequence conflict188in Ref. 3; AAH56211
Sequence conflict222in Ref. 1; AAC52997

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U57747
EMBL· GenBank· DDBJ
AAC52997.1
EMBL· GenBank· DDBJ
mRNA
AK153424
EMBL· GenBank· DDBJ
BAE31983.1
EMBL· GenBank· DDBJ
mRNA
BC002037
EMBL· GenBank· DDBJ
AAH02037.1
EMBL· GenBank· DDBJ
mRNA
BC056211
EMBL· GenBank· DDBJ
AAH56211.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp