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Q61206 (PA1B2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. 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·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
Gene names
Name:Pafah1b2
Synonyms:Pafahb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.

Developmental stage

Expressed already by the time of neurulation. By E10.5, expression is abundant in the developing central and peripheral nervous systems. Major sites include the neuroepithelium of the fore-, mid-, and hindbrain, the spinal cord, the dorsal root, and cranial ganglia.

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

NudcO356852EBI-7445518,EBI-911192

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 229228Platelet-activating factor acetylhydrolase IB subunit beta
PRO_0000058152

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

Experimental info

Sequence conflict129 – 1302QP → HA in AAC52997. Ref.1
Sequence conflict1881C → W in AAH56211. Ref.3
Sequence conflict2221E → G in AAC52997. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q61206 [UniParc].

Last modified May 1, 2007. Version 2.
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]"Platelet-activating factor acetylhydrolase expression and activity suggest a link between neuronal migration and platelet-activating factor."
Albrecht U., Abu-Issa R., Raetz B., Hattori M., Aoki J., Arai H., Inoue K., Eichele G.
Dev. Biol. 180:579-593(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow.
[3]"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].
Strain: C57BL/6J and FVB/N.
Tissue: Embryo and Mammary tumor.
[4]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 61-79 AND 134-142, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U57747 mRNA. Translation: AAC52997.1.
AK153424 mRNA. Translation: BAE31983.1.
BC002037 mRNA. Translation: AAH02037.1.
BC056211 mRNA. Translation: AAH56211.1.
RefSeqNP_032801.2. NM_008775.3.
XP_006510147.1. XM_006510084.1.
XP_006510148.1. XM_006510085.1.
UniGeneMm.200859.

3D structure databases

ProteinModelPortalQ61206.
SMRQ61206. Positions 6-217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202016. 1 interaction.
IntActQ61206. 2 interactions.
MINTMINT-4106420.

PTM databases

PhosphoSiteQ61206.

2D gel databases

REPRODUCTION-2DPAGEIPI00118821.
Q61206.
UCD-2DPAGEQ61206.

Proteomic databases

PaxDbQ61206.
PRIDEQ61206.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000172450; ENSMUSP00000127851; ENSMUSG00000003131.
GeneID18475.
KEGGmmu:18475.
UCSCuc009pgx.1. mouse.

Organism-specific databases

CTD5049.
MGIMGI:108415. Pafah1b2.

Phylogenomic databases

eggNOGNOG69837.
GeneTreeENSGT00390000016520.
HOGENOMHOG000232143.
HOVERGENHBG053477.
InParanoidQ61206.
KOK16795.
OMANIRPKVV.
OrthoDBEOG7HB5BS.
PhylomeDBQ61206.
TreeFamTF323955.

Gene expression databases

BgeeQ61206.
GenevestigatorQ61206.

Family and domain databases

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

Other

NextBio294170.
PROQ61206.
SOURCESearch...

Entry information

Entry namePA1B2_MOUSE
AccessionPrimary (citable) accession number: Q61206
Secondary accession number(s): Q6PKE6, Q7TNP3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 113 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot