Q15102 (PA1B3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Platelet-activating factor acetylhydrolase IB subunit gamma
EC=3.1.1.47

Alternative name(s):
PAF acetylhydrolase 29 kDa subunit
Short name=PAF-AH 29 kDa subunit
PAF-AH subunit gamma
Short name=PAFAH subunit gamma

Gene names

Name:	PAFAH1B3
Synonyms:	PAFAHG

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	231 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. Plays an important role during the development of brain.
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.
Tissue specificity	In the adult, expressed in brain, skeletal muscle, kidney, thymus, spleen, colon, testis, ovary and peripheral blood leukocytes. In the fetus, highest expression occurs in brain.
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
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	brain development Inferred from electronic annotation. Source: Compara lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW lipid metabolic process Traceable author statement Ref.1. Source: ProtInc nervous system development Traceable author statement Ref.1. Source: ProtInc spermatogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from electronic annotation. Source: Compara
Molecular_function	1-alkyl-2-acetylglycerophosphocholine esterase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LNX1	Q8TBB1	2	EBI-711522,EBI-739832

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 231	231	Platelet-activating factor acetylhydrolase IB subunit gamma		PRO_0000058155
Sites
	Active site	47	1	By similarity
	Active site	192	1	By similarity
	Active site	195	1	By similarity
Natural variations
	Natural variant	214	1	R → G. Corresponds to variant rs1043818 [ dbSNP | Ensembl ].		VAR_051261

Sequences

	Sequence		Length	Mass (Da)
	Q15102 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 58A4CB8E7076AE23	FASTA	231	25,734
	10 20 30 40 50 60 MSGEENPASK PTPVQDVQGD GRWMSLHHRF VADSKDKEPE VVFIGDSLVQ LMHQCEIWRE 70 80 90 100 110 120 LFSPLHALNF GIGGDGTQHV LWRLENGELE HIRPKIVVVW VGTNNHGHTA EQVTGGIKAI 130 140 150 160 170 180 VQLVNERQPQ ARVVVLGLLP RGQHPNPLRE KNRQVNELVR AALAGHPRAH FLDADPGFVH 190 200 210 220 230 SDGTISHHDM YDYLHLSRLG YTPVCRALHS LLLRLLAQDQ GQGAPLLEPA P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning of human cytosolic platelet-activating factor acetylhydrolase gamma-subunit and its mRNA expression in human tissues." Adachi H., Tsujimoto M., Hattori M., Arai H., Inoue K. Biochem. Biophys. Res. Commun. 214:180-187(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal liver.
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: Lung and Uterus.
[6]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 84-127; 133-141 AND 199-231, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D63391 mRNA. Translation: BAA09706.1. CR407626 mRNA. Translation: CAG28554.1. AC006486 Genomic DNA. Translation: AAD11989.1. CH471126 Genomic DNA. Translation: EAW57122.1. BC003016 mRNA. Translation: AAH03016.1. BC007863 mRNA. Translation: AAH07863.1.
IPI	IPI00014808.
PIR	JC4246.
RefSeq	NP_001139411.1. NM_001145939.1. NP_001139412.1. NM_001145940.1. NP_002564.1. NM_002573.3.
UniGene	Hs.466831.
3D structure databases
ProteinModelPortal	Q15102.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15102. 32 interactions.
MINT	MINT-1368260.
STRING	9606.ENSP00000262890.
PTM databases
PhosphoSite	Q15102.
Polymorphism databases
DMDM	3024344.
2D gel databases
REPRODUCTION-2DPAGE	IPI00014808.
Proteomic databases
PaxDb	Q15102.
PeptideAtlas	Q15102.
PRIDE	Q15102.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262890; ENSP00000262890; ENSG00000079462. ENST00000538771; ENSP00000444935; ENSG00000079462.
GeneID	5050.
KEGG	hsa:5050.
UCSC	uc002otg.2. human.
Organism-specific databases
CTD	5050.
GeneCards	GC19M042801.
HGNC	HGNC:8576. PAFAH1B3.
HPA	HPA035639.
MIM	603074. gene.
neXtProt	NX_Q15102.
PharmGKB	PA32907.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG69837.
HOGENOM	HOG000232143.
HOVERGEN	HBG053477.
InParanoid	Q15102.
KO	K16795.
OMA	FAPLHCL.
OrthoDB	EOG45QHF4.
PhylomeDB	Q15102.
Enzyme and pathway databases
Pathway_Interaction_DB	lis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development.
Gene expression databases
Bgee	Q15102.
CleanEx	HS_PAFAH1B3.
Genevestigator	Q15102.
GermOnline	ENSG00000079462. Homo sapiens.
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
ChEMBL	CHEMBL5108.
GenomeRNAi	5050.
NextBio	19460.
SOURCE	Search...

Entry information

Entry name

PA1B3_HUMAN

Accession

Primary (citable) accession number: Q15102
Secondary accession number(s): Q53X88

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.