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Q61206

- PA1B2_MOUSE

UniProt

Q61206 - PA1B2_MOUSE

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Protein

Platelet-activating factor acetylhydrolase IB subunit beta

Gene

Pafah1b2

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. 1-alkyl-2-acetylglycerophosphocholine esterase activity Source: UniProtKB-EC

GO - Biological processi

  1. brain development Source: Ensembl
  2. cellular component movement Source: ProtInc
  3. lipid catabolic process Source: UniProtKB-KW
  4. positive regulation of macroautophagy Source: Ensembl
  5. spermatogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

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: Chromosome 9

Organism-specific databases

MGIiMGI:108415. Pafah1b2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
  4. nucleolus Source: Ensembl
  5. plasma membrane Source: Ensembl
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.
InterProiIPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]

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_006510084.1.
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 .
CCDSi CCDS23139.1.
RefSeqi NP_032801.2. NM_008775.3.
XP_006510147.1. XM_006510084.1.
XP_006510148.1. XM_006510085.1.
UniGenei Mm.200859.

3D structure databases

ProteinModelPortali Q61206.
SMRi Q61206. Positions 6-217.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202016. 1 interaction.
IntActi Q61206. 2 interactions.
MINTi MINT-4106420.

PTM databases

PhosphoSitei Q61206.

2D gel databases

REPRODUCTION-2DPAGE IPI00118821.
Q61206.
UCD-2DPAGE Q61206.

Proteomic databases

MaxQBi Q61206.
PaxDbi Q61206.
PRIDEi Q61206.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000172450 ; ENSMUSP00000127851 ; ENSMUSG00000003131 .
GeneIDi 18475.
KEGGi mmu:18475.
UCSCi uc009pgx.1. mouse.

Organism-specific databases

CTDi 5049.
MGIi MGI:108415. Pafah1b2.

Phylogenomic databases

eggNOGi NOG69837.
GeneTreei ENSGT00390000016520.
HOGENOMi HOG000232143.
HOVERGENi HBG053477.
InParanoidi Q61206.
KOi K16795.
OMAi NIRPKVV.
OrthoDBi EOG7HB5BS.
PhylomeDBi Q61206.
TreeFami TF323955.

Miscellaneous databases

NextBioi 294170.
PROi Q61206.
SOURCEi Search...

Gene expression databases

Bgeei Q61206.
Genevestigatori Q61206.

Family and domain databases

Gene3Di 3.40.50.1110. 1 hit.
InterProi IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 118 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