Platelet-activating factor acetylhydrolase IB subunit beta

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O35264 (PA1B2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	229 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Cytoplasm
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	brain development Inferred from expression pattern PubMed 9660828. Source: RGD lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of macroautophagy Inferred from electronic annotation. Source: Compara spermatogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from direct assay PubMed 9660828. Source: RGD nucleolus Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	1-alkyl-2-acetylglycerophosphocholine esterase activity Inferred from electronic annotation. Source: EC platelet-activating factor acetyltransferase activity Inferred from direct assay PubMed 9660828. Source: RGD protein homodimerization activity Inferred from direct assay PubMed 9660828. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PAFAH1B1	P43033	2	EBI-915500,EBI-1007886	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 229

228

Platelet-activating factor acetylhydrolase IB subunit beta

PRO_0000058153

Sites

Active site

By similarity

Active site

193

By similarity

Active site

196

By similarity

Amino acid modifications

Modified residue

N-acetylserine By similarity

Modified residue

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O35264 [UniParc].

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

FASTA

229

25,581

        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' referencesShow '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, 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.
IPI	IPI00207335.
RefSeq	NP_071782.1. NM_022387.3.
UniGene	Rn.24751.
3D structure databases
ProteinModelPortal	O35264.
SMR	O35264. Positions 6-217.
ModBase	Search...
Protein-protein interaction databases
IntAct	O35264. 2 interactions.
STRING	10116.ENSRNOP00000024828.
PTM databases
PhosphoSite	O35264.
Proteomic databases
PaxDb	O35264.
PRIDE	O35264.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000024828; ENSRNOP00000024828; ENSRNOG00000018032.
GeneID	64189.
KEGG	rno:64189.
UCSC	RGD:620332. rat.
Organism-specific databases
CTD	5049.
RGD	620332. Pafah1b2.
Phylogenomic databases
eggNOG	NOG69837.
GeneTree	ENSGT00390000016520.
HOGENOM	HOG000232143.
HOVERGEN	HBG053477.
InParanoid	O35264.
KO	K16795.
OMA	LQQYEIW.
OrthoDB	EOG45QHF4.
Gene expression databases
Genevestigator	O35264.
GermOnline	ENSRNOG00000018032. Rattus norvegicus.
Family and domain databases
Gene3D	3.40.50.1110. 1 hit.
InterPro	IPR013831. SGNH_hydro-type_esterase_dom. [Graphical view]
PROSITE	PS01098. LIPASE_GDSL_SER. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	612844.

Entry information

Entry name

PA1B2_RAT

Accession

Primary (citable) accession number: O35264

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 1, 1998
Last modified:	April 3, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents