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O14495 (LPP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Vascular endothelial growth factor and type I collagen-inducible protein
Short name=VCIP
Gene names
Name:PPAP2B
Synonyms:LPP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Protein existenceEvidence 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 LPA = PA > C-1-P > S-1-P. May be involved in cell adhesion and in cell-cell interactions.

Catalytic activity

A 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.

Enzyme regulation

Inhibited by sphingosine, zinc ions and propanolol. Not inhibited by N-ethylmaleimide treatment.

Subunit structure

Homodimer. This complex seems not to be involved in substrate recognition, it may confer only structural or functional stability. Ref.10

Subcellular location

Golgi apparatustrans-Golgi network membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.

Tissue specificity

Ubiquitously expressed. Highly expressed in heart and placenta.

Induction

By EGF, VEGF, FGF2 and phorbol myristate acetate (PMA). Ref.1

Post-translational modification

N-glycosylated. Contains high-mannose oligosaccharides.

Sequence similarities

Belongs to the PA-phosphatase related phosphoesterase family.

Sequence caution

The sequence AAB50222.1 differs from that shown. Reason: Frameshift at position 225.

Ontologies

Keywords
   Cellular componentCell membrane
Golgi apparatus
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood vessel development

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway involved in positive regulation of cell-cell adhesion

Inferred from mutant phenotype PubMed 20123964. Source: BHF-UCL

canonical Wnt signaling pathway involved in positive regulation of endothelial cell migration

Inferred from mutant phenotype PubMed 20123964. Source: BHF-UCL

canonical Wnt signaling pathway involved in positive regulation of wound healing

Inferred from mutant phenotype PubMed 20123964. Source: BHF-UCL

dephosphorylation

Traceable author statement Ref.2. Source: GOC

gastrulation with mouth forming second

Inferred from electronic annotation. Source: Ensembl

germ cell migration

Traceable author statement Ref.1. Source: ProtInc

homotypic cell-cell adhesion

Inferred from direct assay PubMed 20123964. Source: BHF-UCL

lipid metabolic process

Non-traceable author statement Ref.2. Source: ProtInc

negative regulation of protein phosphorylation

Inferred from direct assay PubMed 20123964. Source: BHF-UCL

phospholipid metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

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 signaling pathway

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

sphingolipid biosynthetic process

Traceable author statement. Source: Reactome

sphingolipid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

adherens junction

Traceable author statement PubMed 20123964. Source: BHF-UCL

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionlipid phosphatase activity

Inferred from electronic annotation. Source: Ensembl

phosphatidate phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphoprotein phosphatase activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CTNND1O607169EBI-766232,EBI-701927

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 311311Lipid phosphate phosphohydrolase 3
PRO_0000220912

Regions

Topological domain1 – 3333Cytoplasmic Potential
Transmembrane34 – 5421Helical; Potential
Topological domain55 – 8531Lumenal Potential
Transmembrane86 – 10621Helical; Potential
Topological domain107 – 12216Cytoplasmic Potential
Transmembrane123 – 14321Helical; Potential
Topological domain144 – 19350Lumenal Potential
Transmembrane194 – 21421Helical; Potential
Topological domain215 – 22713Cytoplasmic Potential
Transmembrane228 – 24821Helical; Potential
Topological domain249 – 2579Lumenal Potential
Transmembrane258 – 27821Helical; Potential
Topological domain279 – 31133Cytoplasmic Potential

Amino acid modifications

Modified residue191Phosphoserine Ref.11 Ref.13
Modified residue2971Phosphoserine Ref.11
Glycosylation1701N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict321K → M in AAV38396. Ref.7
Sequence conflict2821T → M in AAH09196. Ref.9

Sequences

Sequence LengthMass (Da)Tools
O14495 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: CB3F60189044DA31

FASTA31135,116
        10         20         30         40         50         60 
MQNYKYDKAI VPESKNGGSP ALNNNPRRSG SKRVLLICLD LFCLFMAGLP FLIIETSTIK 

        70         80         90        100        110        120 
PYHRGFYCND ESIKYPLKTG ETINDAVLCA VGIVIAILAI ITGEFYRIYY LKKSRSTIQN 

       130        140        150        160        170        180 
PYVAALYKQV GCFLFGCAIS QSFTDIAKVS IGRLRPHFLS VCNPDFSQIN CSEGYIQNYR 

       190        200        210        220        230        240 
CRGDDSKVQE ARKSFFSGHA SFSMYTMLYL VLYLQARFTW RGARLLRPLL QFTLIMMAFY 

       250        260        270        280        290        300 
TGLSRVSDHK HHPSDVLAGF AQGALVACCI VFFVSDLFKT KTTLSLPAPA IRKEILSPVD 

       310 
IIDRNNHHNM M 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase."
Kai M., Wada I., Imai S., Sakane F., Kanoh H.
J. Biol. Chem. 272:24572-24578(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, INDUCTION.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[3]"Regulation of cell-cell interactions by phosphatidic acid phosphatase 2b/VCIP."
Humtsoe J.O., Feng S., Thakker G.D., Yang J., Hong J., Wary K.K.
EMBO J. 22:1539-1554(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Molecular cloning of and expression of an isoform of human phosphatidic acid phosphatase cDNA."
Leung D.W., Tompkins C.K.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Large-scale concatenation cDNA sequencing."
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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].
Tissue: Placenta.
[10]"Lipid phosphate phosphatases dimerise, but this interaction is not required for in vivo activity."
Burnett C., Makridou P., Hewlett L., Howard K.
BMC Biochem. 5:2-2(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB000889 mRNA. Translation: BAA22594.1.
AF017786 mRNA. Translation: AAC63433.1.
AF480883 mRNA. Translation: AAO84481.1.
AF043329 mRNA. Translation: AAD02271.1.
U79294 mRNA. Translation: AAB50222.1. Frameshift.
AK312439 mRNA. Translation: BAG35348.1.
BT019589 mRNA. Translation: AAV38396.1.
CH471059 Genomic DNA. Translation: EAX06651.1.
CH471059 Genomic DNA. Translation: EAX06652.1.
CH471059 Genomic DNA. Translation: EAX06653.1.
BC009196 mRNA. Translation: AAH09196.1.
RefSeqNP_003704.3. NM_003713.4.
UniGeneHs.405156.
Hs.619002.

3D structure databases

ProteinModelPortalO14495.
SMRO14495. Positions 140-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114171. 3 interactions.
IntActO14495. 4 interactions.
MINTMINT-4648964.
STRING9606.ENSP00000294390.

PTM databases

PhosphoSiteO14495.

Proteomic databases

PaxDbO14495.
PRIDEO14495.

Protocols and materials databases

DNASU8613.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371250; ENSP00000360296; ENSG00000162407.
GeneID8613.
KEGGhsa:8613.
UCSCuc001cyj.2. human.

Organism-specific databases

CTD8613.
GeneCardsGC01M056879.
HGNCHGNC:9229. PPAP2B.
HPAHPA028892.
MIM607125. gene.
neXtProtNX_O14495.
PharmGKBPA33553.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0671.
HOGENOMHOG000041307.
HOVERGENHBG002048.
InParanoidO14495.
KOK01080.
OMANNNCKDH.
OrthoDBEOG7C5M9Q.
PhylomeDBO14495.
TreeFamTF316040.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SignaLinkO14495.

Gene expression databases

BgeeO14495.
CleanExHS_PPAP2B.
GenevestigatorO14495.

Family and domain databases

Gene3D1.20.144.10. 1 hit.
InterProIPR028675. LPP3.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PANTHERPTHR10165:SF24. PTHR10165:SF24. 1 hit.
PfamPF01569. PAP2. 1 hit.
[Graphical view]
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMSSF48317. SSF48317. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPPAP2B. human.
GeneWikiPPAP2B.
GenomeRNAi8613.
NextBio32277.
PROO14495.
SOURCESearch...

Entry information

Entry nameLPP3_HUMAN
AccessionPrimary (citable) accession number: O14495
Secondary accession number(s): B2R651 expand/collapse secondary AC list , D3DQ52, Q5U0F7, Q96GW0, Q99782
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM