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Q29460 (PA1B3_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 103. 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 gamma

EC=3.1.1.47
Alternative name(s):
PAF acetylhydrolase 29 kDa subunit
Short name=PAF-AH 29 kDa subunit
PAF-AH subunit gamma
Short name=PAFAH subunit gamma
Gene names
Name:PAFAH1B3
Synonyms:PAFAHG
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length232 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. Plays an important role during the development of brain.

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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 232231Platelet-activating factor acetylhydrolase IB subunit gamma
PRO_0000058154

Sites

Active site471
Active site1921
Active site1951

Amino acid modifications

Modified residue21N-acetylserine By similarity

Experimental info

Sequence conflict791Missing AA sequence Ref.1
Sequence conflict1501E → L AA sequence Ref.1

Secondary structure

....................................... 232
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q29460 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 81C2CECA8E2204ED

FASTA23225,865
        10         20         30         40         50         60 
MSGDENPASK PTPVQDVQGD GRWMSLHHRF VADSKDKEPE VVFIGDSLVQ LMHQCEIWRE 

        70         80         90        100        110        120 
LFSPLHALNF GIGGDSTQHV LWRLENGELE HIRPKIVVVW VGTNNHGHTA EQVTGGIKAI 

       130        140        150        160        170        180 
VQLVNERQPQ ARVVVLGLLP RGQHPNPLRE KNRRVNELVR AALAGHPRAH FLDADPGFVH 

       190        200        210        220        230 
SDGTISHHDM YDYLHLSRLG YTPVCRALHS LLLRLLTQDQ GQGGAPLPEP SP 

« Hide

References

« Hide 'large scale' references
[1]"The catalytic subunit of bovine brain platelet-activating factor acetylhydrolase is a novel type of serine esterase."
Hattori M., Adachi H., Tsujimoto M., Arai H., Inoue K.
J. Biol. Chem. 269:23150-23155(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 38-85; 96-111 AND 119-151.
Tissue: Brain.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal brain.
[3]"Brain acetylhydrolase that inactivates platelet-activating factor is a G-protein-like trimer."
Ho Y.S., Swenson L., Derewenda U., Serre L., Wei Y., Dauter Z., Hattori M., Adachi T., Aoki J., Arai H., Inoue K., Derewenda Z.S.
Nature 385:89-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D30789 mRNA. Translation: BAA06455.1.
BC120202 mRNA. Translation: AAI20203.1.
PIRA54754.
RefSeqNP_777090.1. NM_174665.2.
UniGeneBt.4040.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BWPX-ray2.10A1-232[»]
1BWQX-ray2.30A1-232[»]
1BWRX-ray2.40A1-232[»]
1ES9X-ray1.30A1-232[»]
1FXWX-ray2.10A1-232[»]
1WABX-ray1.70A1-232[»]
3DT6X-ray2.10A1-232[»]
3DT8X-ray1.85A1-232[»]
3DT9X-ray1.85A1-232[»]
ProteinModelPortalQ29460.
SMRQ29460. Positions 5-215.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ29460. 1 interaction.
MINTMINT-208804.

Proteomic databases

PaxDbQ29460.
PRIDEQ29460.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000026366; ENSBTAP00000026366; ENSBTAG00000019787.
GeneID282515.
KEGGbta:282515.

Organism-specific databases

CTD5050.

Phylogenomic databases

eggNOGNOG69837.
GeneTreeENSGT00390000016520.
HOGENOMHOG000232143.
HOVERGENHBG053477.
InParanoidQ29460.
KOK16795.
OMAFAPLHCL.
OrthoDBEOG7HB5BS.
TreeFamTF323955.

Family and domain databases

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

Other

EvolutionaryTraceQ29460.
NextBio20806265.

Entry information

Entry namePA1B3_BOVIN
AccessionPrimary (citable) accession number: Q29460
Secondary accession number(s): Q0VCF0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 103 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