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Q5R6X1 (PA1B3_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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·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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length231 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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 By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCytoplasm
   Molecular functionHydrolase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function1-alkyl-2-acetylglycerophosphocholine esterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 231230Platelet-activating factor acetylhydrolase IB subunit gamma
PRO_0000252685

Sites

Active site471 By similarity
Active site1921 By similarity
Active site1951 By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R6X1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: E5A47630AFB13356

FASTA23125,748
        10         20         30         40         50         60 
MSGEENPASK PTPVQDVQGD GRWMSLHHRF VADSKDKEPE VVFIGDSLVQ LMHQCEIWRE 

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

       130        140        150        160        170        180 
VQLVNERQPQ ARVVVLDLLP RGQHPNPLRE KNQRVNELVR AALAGHPRAH FLDADPGFVH 

       190        200        210        220        230 
SDGTISHHDM YDYLHLSRLG YAPVCRALHS LLLRLLAQDQ GQGAPLLDPA P 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR860358 mRNA. Translation: CAH92489.1.
RefSeqNP_001126468.1. NM_001132996.1.
UniGenePab.5941.

3D structure databases

ProteinModelPortalQ5R6X1.
SMRQ5R6X1. Positions 5-215.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5R6X1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100173455.
KEGGpon:100173455.

Organism-specific databases

CTD5050.

Phylogenomic databases

HOVERGENHBG053477.
KOK16795.

Family and domain databases

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

Entry information

Entry namePA1B3_PONAB
AccessionPrimary (citable) accession number: Q5R6X1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: December 21, 2004
Last modified: February 19, 2014
This is version 48 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