Q61206 (PA1B2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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

Gene names

Name:	Pafah1b2
Synonyms:	Pafahb

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	229 AA.
Sequence status	Complete.
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.
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.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Cytoplasm
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cellular component movement Traceable author statement. Source: ProtInc lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW spermatogenesis Inferred from mutant phenotype. Source: MGI
Molecular function	1-alkyl-2-acetylglycerophosphocholine esterase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 229	229	Platelet-activating factor acetylhydrolase IB subunit beta		PRO_0000058152
Sites
	Active site	48	1	By similarity
	Active site	193	1	By similarity
	Active site	196	1	By similarity
Amino acid modifications
	Modified residue	2	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	129 – 130	2	QP → HA in AAC52997. Ref.1
	Sequence conflict	188	1	C → W in AAH56211. Ref.3
	Sequence conflict	222	1	E → G in AAC52997. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q61206 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: B4D24048621AB182	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

References

	« Hide 'large scale' referencesShow '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: 8954729] [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: 16141072] [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: 15489334] [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, 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.
IPI	IPI00118821.
RefSeq	NP_032801.2. NM_008775.3.
UniGene	Mm.200859.
3D structure databases
ProteinModelPortal	Q61206.
SMR	Q61206. Positions 6-217.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4106420.
STRING	Q61206.
PTM databases
PhosphoSite	Q61206.
2D gel databases
REPRODUCTION-2DPAGE	IPI00118821. Q61206.
UCD-2DPAGE	Q61206.
Proteomic databases
PRIDE	Q61206.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000172450; ENSMUSP00000127851; ENSMUSG00000003131.
GeneID	18475.
KEGG	mmu:18475.
UCSC	uc009pgx.1. mouse.
Organism-specific databases
CTD	5049.
MGI	MGI:108415. Pafah1b2.
Phylogenomic databases
eggNOG	roNOG10533.
HOGENOM	HBG715888.
HOVERGEN	HBG053477.
InParanoid	Q61206.
OMA	RFVQECK.
OrthoDB	EOG45QHF4.
PhylomeDB	Q61206.
Gene expression databases
ArrayExpress	Q61206.
Bgee	Q61206.
Genevestigator	Q61206.
GermOnline	ENSMUSG00000003131. Mus musculus.
Family and domain databases
InterPro	IPR013830. Esterase_SGNH_hydro-type. IPR013831. Esterase_SGNH_hydro-type_subgr. IPR001087. Lipase_GDSL. [Graphical view]
Gene3D	G3DSA:3.40.50.1110. Esterase_SGNH_hydro-type_subgr. 1 hit.
KO	K01062.
Pfam	PF00657. Lipase_GDSL. 1 hit. [Graphical view]
SUPFAM	SSF52266. Esterase_SGNH_hydro-type. 1 hit.
PROSITE	PS01098. LIPASE_GDSL_SER. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	294170.
SOURCE	Search...

Entry information

Entry name

PA1B2_MOUSE

Accession

Primary (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:	November 16, 2011
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program