Q9DAX2 (LPP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipid phosphate phosphohydrolase 2
EC=3.1.3.4

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

Gene names

Name:	Ppap2c
Synonyms:	Lpp2

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	276 AA.
Sequence status	Complete.
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) By similarity.
Catalytic activity	A 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
Subunit structure	Homodimer By similarity.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Expressed at high levels in lung, liver and kidney; at low levels in heart and brain, and was not detected in skeletal muscle.
Sequence similarities	Belongs to the PA-phosphatase related phosphoesterase family.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	phosphatidate phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9DAX2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9DAX2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     240-250: RYVSDFFKSRP → SPTCLTHRLCF
     251-276: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 276	276	Lipid phosphate phosphohydrolase 2		PRO_0000220910
Regions
	Transmembrane	5 – 25	21	Helical; Potential
	Transmembrane	52 – 72	21	Helical; Potential
	Transmembrane	88 – 108	21	Helical; Potential
	Transmembrane	162 – 182	21	Helical; Potential
	Transmembrane	190 – 210	21	Helical; Potential
	Transmembrane	219 – 239	21	Helical; Potential
Amino acid modifications
	Glycosylation	139	1	N-linked (GlcNAc...) Potential
	Glycosylation	155	1	N-linked (GlcNAc...) Ref.4
Natural variations
	Alternative sequence	240 – 250	11	RYVSDFFKSRP → SPTCLTHRLCF in isoform 2.		VSP_009654
	Alternative sequence	251 – 276	26	Missing in isoform 2.		VSP_009655

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 978A83D4681113D2	FASTA	276	31,193
	10 20 30 40 50 60 MERRWVFVLL DVLCVLVASL PFIILTLVNA PYKRGFYCGD DSIRYPYRPD TITHGLMAGV 70 80 90 100 110 120 IITATVILVS LGEAYLVYTD RLYSRSNFNN YVAAIYKVLG TFLFGAAVSQ SLTDLAKYMI 130 140 150 160 170 180 GRLRPSFLAV CDPDWSQVNC SGYVQLEVCR GSPANVTEAR LSFYSGHSSF GMYCMLFLAL 190 200 210 220 230 240 YVQARLCWKW ARLLRPTVQF FLVAFAIYVG YTRVSDHKHH WSDVLVGLLQ GALVACLTVR 250 260 270 YVSDFFKSRP PQPCQEDEVP ERKPSLSLTL TLGDRP
	Isoform 2 [UniParc]. Checksum: D2FFB4C25244781E	FASTA	250	28,181
	10 20 30 40 50 60 MERRWVFVLL DVLCVLVASL PFIILTLVNA PYKRGFYCGD DSIRYPYRPD TITHGLMAGV 70 80 90 100 110 120 IITATVILVS LGEAYLVYTD RLYSRSNFNN YVAAIYKVLG TFLFGAAVSQ SLTDLAKYMI 130 140 150 160 170 180 GRLRPSFLAV CDPDWSQVNC SGYVQLEVCR GSPANVTEAR LSFYSGHSSF GMYCMLFLAL 190 200 210 220 230 240 YVQARLCWKW ARLLRPTVQF FLVAFAIYVG YTRVSDHKHH WSDVLVGLLQ GALVACLTVS 250 PTCLTHRLCF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, expression, and chromosomal localization of a mouse gene homologous to the germ cell migration regulator wunen and to type 2 phosphatidic acid phosphatases." Zhang N., Copeland N.G., Gilbert D.J., Jenkins N.A., Gridley T. Genomics 63:142-144(2000) [PubMed: 10662554] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Strain: C57BL/6J.
[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] (ISOFORM 1). Strain: C57BL/6J. Tissue: Embryo and Placenta.
[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] (ISOFORM 1). Tissue: Mammary tumor.
[4]	"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation." Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B. Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed: 19656770] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-155, MASS SPECTROMETRY. Tissue: Myoblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF123611 mRNA. Translation: AAD24061.1. AK005452 mRNA. Translation: BAB24045.1. AK049581 mRNA. Translation: BAC33824.1. BC010332 mRNA. Translation: AAH10332.1.
IPI	IPI00119129. IPI00409902.
RefSeq	NP_056632.2. NM_015817.2.
UniGene	Mm.28873.
3D structure databases
ProteinModelPortal	Q9DAX2.
SMR	Q9DAX2. Positions 111-238.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9DAX2. 1 interaction.
STRING	Q9DAX2.
PTM databases
PhosphoSite	Q9DAX2.
Proteomic databases
PRIDE	Q9DAX2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000063879; ENSMUSP00000069670; ENSMUSG00000052151.
GeneID	50784.
KEGG	mmu:50784.
UCSC	uc007fyr.1. mouse. uc007fyt.1. mouse.
Organism-specific databases
CTD	8612.
MGI	MGI:1354945. Ppap2c.
Phylogenomic databases
GeneTree	ENSGT00550000074203.
HOVERGEN	HBG002048.
InParanoid	Q9DAX2.
OMA	CRGSPAN.
OrthoDB	EOG43FGXK.
PhylomeDB	Q9DAX2.
Gene expression databases
ArrayExpress	Q9DAX2.
Bgee	Q9DAX2.
CleanEx	MM_PPAP2C.
Genevestigator	Q9DAX2.
GermOnline	ENSMUSG00000052151. Mus musculus.
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.
KO	K01080.
Pfam	PF01569. PAP2. 1 hit. [Graphical view]
SMART	SM00014. acidPPc. 1 hit. [Graphical view]
SUPFAM	SSF48317. AcPase_VanPerase. 1 hit.
ProtoNet	Search...
Other
NextBio	307745.
SOURCE	Search...

Entry information

Entry name

LPP2_MOUSE

Accession

Primary (citable) accession number: Q9DAX2
Secondary accession number(s): Q9WUA4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	June 1, 2001
Last modified:	November 16, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program