Q99JY8 (LPP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipid phosphate phosphohydrolase 3
EC=3.1.3.4

Alternative name(s):
PAP2-beta
Phosphatidate phosphohydrolase type 2b
Phosphatidic acid phosphatase 2b
Short name=PAP-2b
Short name=PAP2b

Gene names

Name:	Ppap2b
Synonyms:	Lpp3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	312 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. Essential to the formation of the chorioallantoic placenta and extraembryonic vasculature. Also mediates gastrulation and axis formation, probably by regulating the Wnt signaling pathway. Ref.4
Catalytic activity	A 1,2-diacylglycerol 3-phosphate + 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 Transmembrane helix
Molecular function	Developmental protein Hydrolase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood vessel development Inferred from mutant phenotype Ref.4. Source: MGI canonical Wnt receptor signaling pathway Inferred from direct assay PubMed 20123964. Source: BHF-UCL canonical Wnt receptor signaling pathway involved in positive regulation of cell-cell adhesion Inferred from electronic annotation. Source: Compara canonical Wnt receptor signaling pathway involved in positive regulation of endothelial cell migration Inferred from electronic annotation. Source: Compara canonical Wnt receptor signaling pathway involved in positive regulation of wound healing Inferred from electronic annotation. Source: Compara cell-cell adhesion Inferred from direct assay PubMed 16099422. Source: MGI gastrulation with mouth forming second Inferred from mutant phenotype Ref.4. Source: MGI homotypic cell-cell adhesion Inferred from electronic annotation. Source: Compara negative regulation of protein phosphorylation Inferred from direct assay PubMed 20123964. Source: BHF-UCL phospholipid metabolic process Inferred from mutant phenotype Ref.4. Source: MGI positive regulation of peptidyl-tyrosine phosphorylation Inferred from direct assay PubMed 16099422. Source: MGI positive regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 20123964. Source: BHF-UCL protein stabilization Inferred from direct assay PubMed 20123964. Source: BHF-UCL regulation of Wnt receptor signaling pathway Inferred from direct assay Ref.4. 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	integrin binding Inferred from direct assay PubMed 16099422. Source: MGI lipid phosphatase activity Inferred from mutant phenotype Ref.4. 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	Helical; Potential
	Topological domain	55 – 85	31	Lumenal Potential
	Transmembrane	86 – 106	21	Helical; Potential
	Topological domain	107 – 123	17	Cytoplasmic Potential
	Transmembrane	124 – 144	21	Helical; Potential
	Topological domain	145 – 194	50	Lumenal Potential
	Transmembrane	195 – 215	21	Helical; Potential
	Topological domain	216 – 226	11	Cytoplasmic Potential
	Transmembrane	227 – 247	21	Helical; Potential
	Topological domain	248 – 258	11	Lumenal Potential
	Transmembrane	259 – 279	21	Helical; Potential
	Topological domain	280 – 312	33	Cytoplasmic Potential
Amino acid modifications
	Modified residue	19	1	Phosphoserine 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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: FUNCTION, DISEASE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK159136 mRNA. Translation: BAE34848.1. AK160056 mRNA. Translation: BAE35594.1. BC005558 mRNA. Translation: AAH05558.1.
IPI	IPI00115626.
RefSeq	NP_542122.1. NM_080555.2.
UniGene	Mm.348326.
3D structure databases
ProteinModelPortal	Q99JY8.
SMR	Q99JY8. Positions 142-271.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99JY8. 3 interactions.
STRING	10090.ENSMUSP00000065719.
PTM databases
PhosphoSite	Q99JY8.
Proteomic databases
PaxDb	Q99JY8.
PRIDE	Q99JY8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000064139; ENSMUSP00000065719; ENSMUSG00000028517.
GeneID	67916.
KEGG	mmu:67916.
Organism-specific databases
CTD	8613.
MGI	MGI:1915166. Ppap2b.
Phylogenomic databases
eggNOG	COG0671.
GeneTree	ENSGT00620000087654.
HOGENOM	HOG000041307.
HOVERGEN	HBG002048.
InParanoid	Q99JY8.
KO	K01080.
OMA	CSEGYIQ.
OrthoDB	EOG40CHHS.
Gene expression databases
ArrayExpress	Q99JY8.
Bgee	Q99JY8.
CleanEx	MM_PPAP2B.
Genevestigator	Q99JY8.
GermOnline	ENSMUSG00000028517. Mus musculus.
Family and domain databases
Gene3D	1.20.144.10. 1 hit.
InterPro	IPR016118. P_Acid_Pase/Cl_peroxidase_N. IPR000326. P_Acid_Pase_2/haloperoxidase. [Graphical view]
Pfam	PF01569. PAP2. 1 hit. [Graphical view]
SMART	SM00014. acidPPc. 1 hit. [Graphical view]
SUPFAM	SSF48317. AcPase_VanPerase. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	PPAP2B. mouse.
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:	April 3, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program