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P68401 (PA1B2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Gene names
Name:PAFAH1B2
Synonyms:PAFAHB
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 229228Platelet-activating factor acetylhydrolase IB subunit beta
PRO_0000058149

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

Secondary structure

..................................... 229
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P68401 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 14CF5D48621AA504

FASTA22925,569
        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 QLLDTDGGFV 

       190        200        210        220 
HSDGAISCHD MFDFLHLTGG GYAKICKPLH ELIMQLLEET PEEKQTTIA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of a cDNA encoding the beta-subunit (30-kDa subunit) of bovine brain platelet-activating factor acetylhydrolase."
Hattori M., Adachi H., Aoki J., Tsujimoto M., Arai H., Inoue K.
J. Biol. Chem. 270:31345-31352(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 37-53; 134-152 AND 167-196.
Tissue: Brain.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Hypothalamus.
[3]"Preparation and crystal structure of the recombinant alpha(1)/alpha(2) catalytic heterodimer of bovine brain platelet-activating factor acetylhydrolase Ib."
Sheffield P.J., McMullen T.W., Li J., Ho Y.S., Garrard S.M., Derewenda U., Derewenda Z.S.
Protein Eng. 14:513-519(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Tissue: Brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D49678 mRNA. Translation: BAA08534.1.
BC103452 mRNA. Translation: AAI03453.1.
RefSeqNP_777089.1. NM_174664.2.
XP_005215864.1. XM_005215807.1.
UniGeneBt.49728.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FXWX-ray2.10F1-229[»]
ProteinModelPortalP68401.
SMRP68401. Positions 6-217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP68401. 1 interaction.

Proteomic databases

PaxDbP68401.
PRIDEP68401.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000007398; ENSBTAP00000007398; ENSBTAG00000005627.
GeneID282514.
KEGGbta:282514.

Organism-specific databases

CTD5049.

Phylogenomic databases

eggNOGNOG69837.
HOGENOMHOG000232143.
HOVERGENHBG053477.
InParanoidP68401.
KOK16795.
OMANIRPKVV.
OrthoDBEOG7HB5BS.
TreeFamTF323955.

Family and domain databases

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

Other

EvolutionaryTraceP68401.
NextBio20806264.

Entry information

Entry namePA1B2_BOVIN
AccessionPrimary (citable) accession number: P68401
Secondary accession number(s): O00687, Q29459, Q3ZBB8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: March 19, 2014
This is version 75 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references