Reviewed, UniProtKB/Swiss-Prot Q15102 (PA1B3_HUMAN)

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
    PAFAH subunit gamma

Gene names

Name:	PAFAH1B3
Synonyms:	PAFAHG

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	231 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW nervous system development Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	1-alkyl-2-acetylglycerophosphocholine esterase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LNX1	Q8TBB1	1	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: dbSNP rs1043818.		VAR_051261

Sequences

	Sequence		Length	Mass (Da)
	Q15102-1 [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: 7669037] [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: 15057824] [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: 15489334] [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]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. NP_001139412.1. NP_002564.1.
UniGene	Hs.466831
3D structure databases
SMR	Q15102. Positions 5-215.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15102. 31 interactions.
STRING	Q15102.
2-D gel databases
REPRODUCTION-2DPAGE	IPI00014808.
Proteomic databases
PeptideAtlas	Q15102.
PRIDE	Q15102.
Genome annotation databases
Ensembl	ENST00000262890; ENSP00000262890; ENSG00000079462; Homo sapiens. [Genome view]
GeneID	5050.
KEGG	hsa:5050.
UCSC	uc002otg.1. human.
Organism-specific databases
CTD	5050.
GeneCards	GC19M047493.
H-InvDB	HIX0015176. HIX0027549.
HGNC	HGNC:8576. PAFAH1B3.
MIM	603074. gene.
PharmGKB	PA32907.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG715888.
HOVERGEN	Q15102.
InParanoid	Q15102.
OMA	NQRQPQA.
OrthoDB	EOG900445.
Enzyme and pathway databases
BRENDA	3.1.1.47. 247.
Pathway_Interaction_DB	lis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development.
Gene expression databases
ArrayExpress	Q15102.
Bgee	Q15102.
CleanEx	HS_PAFAH1B3.
Genevestigator	Q15102.
GermOnline	ENSG00000079462. Homo sapiens.
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.
Pfam	PF00657. Lipase_GDSL. 1 hit. [Graphical view]
PROSITE	PS01098. LIPASE_GDSL_SER. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
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:	December 15, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.