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O35264 (PA1B2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Platelet-activating factor acetylhydrolase IB subunit beta

EC=3.1.1.47
Alternative name(s):
PAF acetylhydrolase 30 kDa subunit
Short name=PAF-AH 30 kDa subunit
PAF-AH subunit beta
Short name=PAFAH subunit beta
Platelet-activating factor acetylhydrolase alpha 2 subunit
Short name=PAF-AH alpha 2
Gene names
Name:Pafah1b2
Synonyms:Pafahb
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length229 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inactivates PAF by removing the acetyl group at the sn-2 position. This is a catalytic subunit.

Catalytic activity

1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate.

Subunit structure

Cytosolic PAF-AH IB is formed of three subunits of 45 kDa (alpha), 30 kDa (beta) and 29 kDa (gamma). The catalytic activity of the enzyme resides in the beta and gamma subunits, whereas the alpha subunit has regulatory activity. Trimer formation is not essential for the catalytic activity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Expressed in heart, brain, spleen, lung, liver, kidney and testis. Not expressed in skeletal muscle.

Sequence similarities

Belongs to the 'GDSL' lipolytic enzyme family. Platelet-activating factor acetylhydrolase IB beta/gamma subunits subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PAFAH1B1P430332EBI-915500,EBI-1007886From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 229228Platelet-activating factor acetylhydrolase IB subunit beta
PRO_0000058153

Sites

Active site481 By similarity
Active site1931 By similarity
Active site1961 By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue21Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
O35264 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: B4D24048621AB182

FASTA22925,581
        10         20         30         40         50         60 
MSQGDSNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV QLMQQYEIWR 

        70         80         90        100        110        120 
ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV WVGTNNHENT AEEVAGGIEA 

       130        140        150        160        170        180 
IVQLINTRQP QAKIIVLGLL PRGEKPNPLR QKNAKVNQLL KVSLPKLANV QLLDIDGGFV 

       190        200        210        220 
HSDGAISCHD MFDFLHLTGG GYAKICKPLH ELIMQLLEET PEEKQTTIA 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of cDNAs encoding alpha1, alpha2, and beta subunits of rat brain platelet-activating factor acetylhydrolase."
Watanabe M., Aoki J., Manya H., Arai H., Inoue K.
Biochim. Biophys. Acta 1401:73-79(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Brain.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[3]Lubec G., Chen W.-Q., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 61-79 AND 134-142, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF016048 mRNA. Translation: AAC27974.1.
BC081714 mRNA. Translation: AAH81714.1.
RefSeqNP_071782.1. NM_022387.3.
XP_006243019.1. XM_006242957.1.
XP_006243020.1. XM_006242958.1.
UniGeneRn.24751.

3D structure databases

ProteinModelPortalO35264.
SMRO35264. Positions 6-217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO35264. 2 interactions.
STRING10116.ENSRNOP00000024828.

PTM databases

PhosphoSiteO35264.

Proteomic databases

PaxDbO35264.
PRIDEO35264.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000024828; ENSRNOP00000024828; ENSRNOG00000018032.
GeneID64189.
KEGGrno:64189.
UCSCRGD:620332. rat.

Organism-specific databases

CTD5049.
RGD620332. Pafah1b2.

Phylogenomic databases

eggNOGNOG69837.
GeneTreeENSGT00390000016520.
HOGENOMHOG000232143.
HOVERGENHBG053477.
InParanoidO35264.
KOK16795.
OMANIRPKVV.
OrthoDBEOG7HB5BS.
PhylomeDBO35264.
TreeFamTF323955.

Gene expression databases

GenevestigatorO35264.

Family and domain databases

Gene3D3.40.50.1110. 1 hit.
InterProIPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]
ProtoNetSearch...

Other

NextBio612844.
PROO35264.

Entry information

Entry namePA1B2_RAT
AccessionPrimary (citable) accession number: O35264
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families