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Protein

Platelet-activating factor acetylhydrolase IB subunit beta

Gene

Pafah1b2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Inactivates PAF by removing the acetyl group at the sn-2 position. This is a catalytic subunit.

Catalytic activityi

1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei48 – 481By similarity
Active sitei193 – 1931By similarity
Active sitei196 – 1961By similarity

GO - Molecular functioni

GO - Biological processi

  • brain development Source: GO_Central
  • lipid catabolic process Source: UniProtKB-KW
  • movement of cell or subcellular component Source: ProtInc
  • positive regulation of macroautophagy Source: MGI
  • spermatogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.1.47. 3474.

Names & Taxonomyi

Protein namesi
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
Gene namesi
Name:Pafah1b2
Synonyms:Pafahb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:108415. Pafah1b2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: Ensembl
  • extracellular exosome Source: MGI
  • nucleolus Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 229228Platelet-activating factor acetylhydrolase IB subunit betaPRO_0000058152Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ61206.
PaxDbiQ61206.
PRIDEiQ61206.

2D gel databases

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

PTM databases

PhosphoSiteiQ61206.

Expressioni

Developmental stagei

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.

Gene expression databases

BgeeiQ61206.
GenevestigatoriQ61206.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
NudcO356852EBI-7445518,EBI-911192

Protein-protein interaction databases

BioGridi202016. 1 interaction.
IntActiQ61206. 2 interactions.
MINTiMINT-4106420.

Structurei

3D structure databases

ProteinModelPortaliQ61206.
SMRiQ61206. Positions 6-217.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG69837.
GeneTreeiENSGT00390000016520.
HOGENOMiHOG000232143.
HOVERGENiHBG053477.
InParanoidiQ61206.
KOiK16795.
OMAiNIRPKVV.
OrthoDBiEOG7HB5BS.
PhylomeDBiQ61206.
TreeFamiTF323955.

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR013830. SGNH_hydro.
[Graphical view]
SUPFAMiSSF52266. SSF52266. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61206-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQGDSNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV
60 70 80 90 100
QLMQQYEIWR ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV
110 120 130 140 150
WVGTNNHENT AEEVAGGIEA IVQLINTRQP QAKIIVLGLL PRGEKPNPLR
160 170 180 190 200
QKNAKVNQLL KVSLPKLANV QLLDIDGGFV HSDGAISCHD MFDFLHLTGG
210 220
GYAKICKPLH ELIMQLLEET PEEKQTTIA
Length:229
Mass (Da):25,581
Last modified:May 1, 2007 - v2
Checksum:iB4D24048621AB182
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1302QP → HA in AAC52997 (PubMed:8954729).Curated
Sequence conflicti188 – 1881C → W in AAH56211 (PubMed:15489334).Curated
Sequence conflicti222 – 2221E → G in AAC52997 (PubMed:8954729).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57747 mRNA. Translation: AAC52997.1.
AK153424 mRNA. Translation: BAE31983.1.
BC002037 mRNA. Translation: AAH02037.1.
BC056211 mRNA. Translation: AAH56211.1.
CCDSiCCDS23139.1.
RefSeqiNP_032801.2. NM_008775.3.
XP_006510147.1. XM_006510084.2.
XP_006510148.1. XM_006510085.1.
UniGeneiMm.200859.

Genome annotation databases

EnsembliENSMUST00000172450; ENSMUSP00000127851; ENSMUSG00000003131.
GeneIDi18475.
KEGGimmu:18475.
UCSCiuc009pgx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57747 mRNA. Translation: AAC52997.1.
AK153424 mRNA. Translation: BAE31983.1.
BC002037 mRNA. Translation: AAH02037.1.
BC056211 mRNA. Translation: AAH56211.1.
CCDSiCCDS23139.1.
RefSeqiNP_032801.2. NM_008775.3.
XP_006510147.1. XM_006510084.2.
XP_006510148.1. XM_006510085.1.
UniGeneiMm.200859.

3D structure databases

ProteinModelPortaliQ61206.
SMRiQ61206. Positions 6-217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202016. 1 interaction.
IntActiQ61206. 2 interactions.
MINTiMINT-4106420.

Chemistry

ChEMBLiCHEMBL3259481.

PTM databases

PhosphoSiteiQ61206.

2D gel databases

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

Proteomic databases

MaxQBiQ61206.
PaxDbiQ61206.
PRIDEiQ61206.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000172450; ENSMUSP00000127851; ENSMUSG00000003131.
GeneIDi18475.
KEGGimmu:18475.
UCSCiuc009pgx.1. mouse.

Organism-specific databases

CTDi5049.
MGIiMGI:108415. Pafah1b2.

Phylogenomic databases

eggNOGiNOG69837.
GeneTreeiENSGT00390000016520.
HOGENOMiHOG000232143.
HOVERGENiHBG053477.
InParanoidiQ61206.
KOiK16795.
OMAiNIRPKVV.
OrthoDBiEOG7HB5BS.
PhylomeDBiQ61206.
TreeFamiTF323955.

Enzyme and pathway databases

BRENDAi3.1.1.47. 3474.

Miscellaneous databases

NextBioi294170.
PROiQ61206.
SOURCEiSearch...

Gene expression databases

BgeeiQ61206.
GenevestigatoriQ61206.

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR013830. SGNH_hydro.
[Graphical view]
SUPFAMiSSF52266. SSF52266. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPA1B2_MOUSE
AccessioniPrimary (citable) accession number: Q61206
Secondary accession number(s): Q6PKE6, Q7TNP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 2007
Last modified: May 27, 2015
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.