Reviewed, UniProtKB/Swiss-Prot O43688 (LPP2_HUMAN)

Names and origin

Protein names

Recommended name:
    Lipid phosphate phosphohydrolase 2
    EC=3.1.3.4
Alternative name(s):
    Phosphatidic acid phosphatase 2c
      Short name=PAP-2c
      Short name=PAP2c
    Phosphatidate phosphohydrolase type 2c
    PAP2-gamma
      Short name=PAP2-G

Gene names

Name:	PPAP2C
Synonyms:	LPP2

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	288 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is PA > C-1-P > LPA > S-1-P.
Catalytic activity	A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
Enzyme regulation	Inhibited by sphingosine, zinc ions and propanolol.
Subunit structure	Homodimer By similarity.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Found mainly in brain, pancreas and placenta.
Sequence similarities	Belongs to the PA-phosphatase related phosphoesterase family.

Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	cytosol Ref.2 Inferred from Experiment. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	phosphatidate phosphatase activity Ref.2 Inferred from Experiment. Source: Reactome phosphoprotein phosphatase activity Ref.3 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 288	288	Lipid phosphate phosphohydrolase 2		PRO_0000220909
Regions
	Transmembrane	5 – 25	21	Potential
	Transmembrane	52 – 72	21	Potential
	Transmembrane	88 – 108	21	Potential
	Transmembrane	163 – 183	21	Potential
	Transmembrane	197 – 217	21	Potential
	Transmembrane	227 – 247	21	Potential
Amino acid modifications
	Glycosylation	139	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	O43688-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: F7C6A09A28DA9AC8	FASTA	288	32,574
	10 20 30 40 50 60 MQRRWVFVLL DVLCLLVASL PFAILTLVNA PYKRGFYCGD DSIRYPYRPD TITHGLMAGV 70 80 90 100 110 120 TITATVILVS AGEAYLVYTD RLYSRSDFNN YVAAVYKVLG TFLFGAAVSQ SLTDLAKYMI 130 140 150 160 170 180 GRLRPNFLAV CDPDWSRVNC SVYVQLEKVC RGNPADVTEA RLSFYSGHSS FGMYCMVFLA 190 200 210 220 230 240 LYVQARLCWK WARLLRPTVQ FFLVAFALYV GYTRVSDYKH HWSDVLVGLL QGALVAALTV 250 260 270 280 CYISDFFKAR PPQHCLKEEE LERKPSLSLT LTLGEADHNH YGYPHSSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells." Leung D.W., Tompkins C.K., White T. DNA Cell Biol. 17:377-385(1998) [PubMed: 9570154] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform." Roberts R., Sciorra V.A., Morris A.J. J. Biol. Chem. 273:22059-22067(1998) [PubMed: 9705349] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[3]	"Identification of a novel human phosphatidic acid phosphatase type 2 isoform." Hooks S.B., Ragan S.P., Lynch K.R. FEBS Lett. 427:188-192(1998) [PubMed: 9607309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: Ovary.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF035959 mRNA. Translation: AAC15968.1. AF047760 mRNA. Translation: AAC32104.1. AF056083 mRNA. Translation: AAC25666.1. BT007021 mRNA. Translation: AAP35667.1. BC002806 mRNA. Translation: AAH02806.1.
IPI	IPI00216620.
RefSeq	NP_003703.1. NP_803545.1. NP_808211.1.
UniGene	Hs.465506
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O43688. 2 interactions.
PTM databases
PhosphoSite	O43688.
Proteomic databases
PRIDE	O43688.
Genome annotation databases
Ensembl	ENSG00000141934. Homo sapiens. [Contig view]
GeneID	8612.
KEGG	hsa:8612.
UCSC	uc002loi.1. human.
Organism-specific databases
GeneCards	GC19M000232.
H-InvDB	HIX0014548.
HGNC	HGNC:9230. PPAP2C.
MIM	607126. gene.
PharmGKB	PA33554.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	O43688.
Enzyme and pathway databases
BRENDA	3.1.3.4. 247.
Reactome	REACT_602. Metabolism of lipids and lipoproteins.
Gene expression databases
ArrayExpress	O43688.
Bgee	O43688.
CleanEx	HS_PPAP2C.
GermOnline	ENSG00000141934. Homo sapiens.
Family and domain databases
InterPro	IPR016118. P_Acid_Pase/Cl_peroxidase_N. IPR000326. P_Acid_Pase_2/haloperoxidase. [Graphical view]
Gene3D	G3DSA:1.20.144.10. P_Acid_Pase/Cl_peroxidase_N. 1 hit.
Pfam	PF01569. PAP2. 1 hit. [Graphical view]
SMART	SM00014. acidPPc. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	32269.
SOURCE	Search...

Entry information

Entry name

LPP2_HUMAN

Accession

Primary (citable) accession number: O43688

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	June 1, 1998
Last modified:	July 7, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)