Reviewed, UniProtKB/Swiss-Prot Q99JY8 (LPP3_MOUSE)

Names and origin

Protein names

Recommended name:
    Lipid phosphate phosphohydrolase 3
    EC=3.1.3.4
Alternative name(s):
    Phosphatidic acid phosphatase 2b
    PAP2-beta
      Short name=PAP-2b
      Short name=PAP2b
    Phosphatidate phosphohydrolase type 2b

Gene names

Name:	Ppap2b
Synonyms:	Lpp3

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

Protein attributes

Sequence length	312 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) By similarity. Essential to the formation of the chorioallantoic placenta and extraembryonic vasculature. Also mediates gastrulation and axis formation, probably by regulating the Wnt signaling pathway.
Catalytic activity	A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
Subunit structure	Homodimer By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Involvement in disease	Ppap2b deficient embryos fail to form a chorioallantoic placenta and yolk sac vasculature. A subset of embryos also show a shortening of the anterior-posterior axis and frequent duplication of axial structures. Loss of Ppap2b results in a marked increase in beta-catenin-mediated T-cell factor (TCF) transcription. Ref.4
Sequence similarities	Belongs to the PA-phosphatase related phosphoesterase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Molecular function	Developmental protein Hydrolase
PTM	Glycoprotein Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	blood vessel development Ref.4 Inferred from mutant phenotype. Source: MGI gastrulation with mouth forming second Ref.4 Inferred from mutant phenotype. Source: MGI phospholipid metabolic process Ref.4 Inferred from mutant phenotype. Source: MGI regulation of Wnt receptor signaling pathway Ref.4 Inferred from direct assay. Source: MGI
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	lipid phosphatase activity Ref.4 Inferred from mutant phenotype. Source: MGI phosphatidate phosphatase 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 – 312	312	Lipid phosphate phosphohydrolase 3		PRO_0000220913
Regions
	Topological domain	1 – 33	33	Cytoplasmic Potential
	Transmembrane	34 – 54	21	Potential
	Topological domain	55 – 85	31	Lumenal Potential
	Transmembrane	86 – 106	21	Potential
	Topological domain	107 – 123	17	Cytoplasmic Potential
	Transmembrane	124 – 144	21	Potential
	Topological domain	145 – 194	50	Lumenal Potential
	Transmembrane	195 – 215	21	Potential
	Topological domain	216 – 226	11	Cytoplasmic Potential
	Transmembrane	227 – 247	21	Potential
	Topological domain	248 – 258	11	Lumenal Potential
	Transmembrane	259 – 279	21	Potential
	Topological domain	280 – 312	33	Cytoplasmic Potential
Amino acid modifications
	Modified residue	19	1	Phosphoserine By similarity
	Modified residue	110	1	Phosphotyrosine By similarity
	Modified residue	298	1	Phosphoserine By similarity
	Glycosylation	171	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	187	1	S → C in BAE34848. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q99JY8-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: D782986E04B57D7D	FASTA	312	35,216
	10 20 30 40 50 60 MQSYKYDKAI VPESKNGGSP ALNNNPRKGG SKRVLLICLD LFCLFMAALP FLIIETSTIK 70 80 90 100 110 120 PYRRGFYCND ESIKYPLKVS ETINDAVLCA VGIVIAILAI ITGEFYRIYY LKEKSRSTTQ 130 140 150 160 170 180 NPYVAALYKQ VGCFLFGCAI SQSFTDIAKV SIGRLRPHFL SVCDPDFSQI NCSEGYIQNY 190 200 210 220 230 240 RCRGEDSKVQ EARKSFFSGH ASFSMFTMLY LVLYLQARFT WRGARLLRPL LQFTLLMMAF 250 260 270 280 290 300 YTGLSRVSDY KHHPSDVLAG FAQGALVACC IVFFVSDLFK TKTSLSLPAP AIRREILSPV 310 DIIDRNNHHN MV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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: FVB/N. Tissue: Mammary gland.
[3]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 283-293, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[4]	"The lipid phosphatase LPP3 regulates extra-embryonic vasculogenesis and axis patterning." Escalante-Alcalde D., Hernandez L., Le Stunff H., Maeda R., Lee H.-S., Cheng G. Jr., Sciorra V.A., Daar I., Spiegel S., Morris A.J., Stewart C.L. Development 130:4623-4637(2003) [PubMed: 12925589] [Abstract] Cited for: FUNCTION, DISEASE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK159136 mRNA. Translation: BAE34848.1. AK160056 mRNA. Translation: BAE35594.1. BC005558 mRNA. Translation: AAH05558.1.
IPI	IPI00115626.
RefSeq	NP_542122.1.
UniGene	Mm.348326
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q99JY8.
Proteomic databases
PRIDE	Q99JY8.
Genome annotation databases
Ensembl	ENSMUSG00000028517. Mus musculus. [Contig view]
GeneID	67916.
KEGG	mmu:67916.
Organism-specific databases
MGI	MGI:1915166. Ppap2b.
Phylogenomic databases
HOGENOM	Q99JY8.
HOVERGEN	Q99JY8.
OMA	Q99JY8. YIQNYRC.
Enzyme and pathway databases
BRENDA	3.1.3.4. 244.
Gene expression databases
ArrayExpress	Q99JY8.
Bgee	Q99JY8.
CleanEx	MM_PPAP2B.
GermOnline	ENSMUSG00000028517. 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.
Pfam	PF01569. PAP2. 1 hit. [Graphical view]
SMART	SM00014. acidPPc. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	325938.
SOURCE	Search...

Entry information

Entry name

LPP3_MOUSE

Accession

Primary (citable) accession number: Q99JY8
Secondary accession number(s): Q3TVM4, Q3TXR7, Q8BTB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	June 1, 2001
Last modified:	May 5, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)