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Q5VZY2 (PPC1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidate phosphatase PPAPDC1A

EC=3.1.3.4
Alternative name(s):
Phosphatidic acid phosphatase type 2 domain-containing protein 1A
Gene names
Name:PPAPDC1A
Synonyms:DPPL2, PPAPDC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Displays magnesium-independent phosphatidate phosphatase activity in vitro. Catalyzes the conversion of phosphatidic acid to diacylglycerol. Ref.1

Catalytic activity

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

Enzyme regulation

Inhibited by N-ethylmaleimide. Ref.1

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

Expressed mainly to the brain, kidney and testis, and to a lesser extent the bone marrow, thymus, prostate, liver and uterus. Ref.1

Sequence similarities

Belongs to the PA-phosphatase related phosphoesterase family.

Biophysicochemical properties

Kinetic parameters:

KM=104 µM for diacylglycerol pyrophosphate Ref.1

KM=506 µM for phosphatidate

KM=580 µM for lysophosphatidate

Sequence caution

The sequence CAH70333.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5VZY2-1)

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: Q5VZY2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     86-149: AVSLALALNGVCTNTIKLIVGRPRPDFFYRCFPDGVMNSEMHCTGDPDLVSEGRKSFPSIHSSF → V
Note: No experimental confirmation available.
Isoform 3 (identifier: Q5VZY2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-189: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q5VZY2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     56-96: AISFLTPLAV...VSLALALNGV → IPLWVESSAS...PTLVCESQPH
     97-271: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Phosphatidate phosphatase PPAPDC1A
PRO_0000286943

Regions

Transmembrane4 – 2421Helical; Potential
Transmembrane49 – 6921Helical; Potential
Transmembrane84 – 10421Helical; Potential
Transmembrane142 – 16221Helical; Potential
Transmembrane179 – 19921Helical; Potential
Transmembrane202 – 22221Helical; Potential
Region102 – 1109Phosphatase sequence motif I
Region143 – 1464Phosphatase sequence motif II
Region195 – 20511Phosphatase sequence motif III

Natural variations

Alternative sequence1 – 189189Missing in isoform 3.
VSP_025237
Alternative sequence56 – 9641AISFL…ALNGV → IPLWVESSASFLHTFATDST ILLWPTQLAINPTLVCESQP H in isoform 4.
VSP_025239
Alternative sequence86 – 14964AVSLA…IHSSF → V in isoform 2.
VSP_025238
Alternative sequence97 – 271175Missing in isoform 4.
VSP_025240

Experimental info

Mutagenesis1091R → A: Loss of phosphatase activity; when associated with A-146 and with A-202. Ref.1
Mutagenesis1461H → A: Loss of phosphatase activity; when associated with A-109 and with A-202. Ref.1
Mutagenesis2021H → A: Loss of phosphatase activity; when associated with A-109 and with A-146. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 15, 2007. Version 2.
Checksum: C534549E44DDB9A1

FASTA27130,395
        10         20         30         40         50         60 
MRELAIEIGV RALLFGVFVF TEFLDPFQRV IQPEEIWLYK NPLVQSDNIP TRLMFAISFL 

        70         80         90        100        110        120 
TPLAVICVVK IIRRTDKTEI KEAFLAVSLA LALNGVCTNT IKLIVGRPRP DFFYRCFPDG 

       130        140        150        160        170        180 
VMNSEMHCTG DPDLVSEGRK SFPSIHSSFA FSGLGFTTFY LAGKLHCFTE SGRGKSWRLC 

       190        200        210        220        230        240 
AAILPLYCAM MIALSRMCDY KHHWQDSFVG GVIGLIFAYI CYRQHYPPLA NTACHKPYVS 

       250        260        270 
LRVPASLKKE ERPTADSAPS LPLEGITEGP V 

« Hide

Isoform 2 [UniParc].

Checksum: 9C4052029FE63D0F
Show »

FASTA20823,509
Isoform 3 [UniParc].

Checksum: A228474E1B007DBA
Show »

FASTA829,175
Isoform 4 [UniParc].

Checksum: DE39DF5B00D26259
Show »

FASTA9611,089

References

« Hide 'large scale' references
[1]"Cloning and characterization of DPPL1 and DPPL2, representatives of a novel type of mammalian phosphatidate phosphatase."
Takeuchi M., Harigai M., Momohara S., Ball E., Abe J., Furuichi K., Kamatani N.
Gene 399:174-180(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, ENZYME REGULATION, CATALYTIC ACTIVITY, REGION, MUTAGENESIS OF ARG-109; HIS-146 AND HIS-202, BIOPHYSICOCHEMICAL PROPERTIES.
[2]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BD418666 mRNA. No translation available.
AL157782, AC073587, AC023282 Genomic DNA. Translation: CAH70332.1. Different termination.
AL157782, AC023282, AC073587 Genomic DNA. Translation: CAH70333.1. Sequence problems.
BC101267 mRNA. Translation: AAI01268.1.
BC101268 mRNA. Translation: AAI01269.1.
BC101269 mRNA. Translation: AAI01270.1.
BC122535 mRNA. Translation: AAI22536.1.
BC132787 mRNA. Translation: AAI32788.1.
CCDSCCDS41573.1. [Q5VZY2-1]
RefSeqNP_001025230.1. NM_001030059.1. [Q5VZY2-1]
UniGeneHs.40479.

3D structure databases

ProteinModelPortalQ5VZY2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000381302.

PTM databases

PhosphoSiteQ5VZY2.

Polymorphism databases

DMDM147721098.

Proteomic databases

PaxDbQ5VZY2.
PRIDEQ5VZY2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398248; ENSP00000381300; ENSG00000203805. [Q5VZY2-4]
ENST00000398250; ENSP00000381302; ENSG00000203805. [Q5VZY2-1]
ENST00000439221; ENSP00000403508; ENSG00000203805. [Q5VZY2-2]
GeneID196051.
KEGGhsa:196051.
UCSCuc001lev.1. human. [Q5VZY2-1]
uc001lew.1. human. [Q5VZY2-4]
uc009xzl.1. human. [Q5VZY2-2]

Organism-specific databases

CTD196051.
GeneCardsGC10P122207.
HGNCHGNC:23531. PPAPDC1A.
HPAHPA045188.
neXtProtNX_Q5VZY2.
PharmGKBPA134907381.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0671.
HOGENOMHOG000215098.
HOVERGENHBG056764.
InParanoidQ5VZY2.
OMANTACHKS.
OrthoDBEOG79CZ0D.
PhylomeDBQ5VZY2.
TreeFamTF323722.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ5VZY2.
BgeeQ5VZY2.
CleanExHS_PPAPDC1A.
GenevestigatorQ5VZY2.

Family and domain databases

Gene3D1.20.144.10. 1 hit.
InterProIPR000326. P_Acid_Pase_2/haloperoxidase.
IPR028668. PPAPDC1A/PPAPDC1B.
[Graphical view]
PANTHERPTHR10165:SF90. PTHR10165:SF90. 1 hit.
PfamPF01569. PAP2. 1 hit.
[Graphical view]
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMSSF48317. SSF48317. 1 hit.
ProtoNetSearch...

Other

GeneWikiPPAPDC1A.
GenomeRNAi196051.
NextBio89410.
PROQ5VZY2.

Entry information

Entry namePPC1A_HUMAN
AccessionPrimary (citable) accession number: Q5VZY2
Secondary accession number(s): A2RU82 expand/collapse secondary AC list , Q08EQ2, Q0IIP2, Q495B4, Q5VZY1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: July 9, 2014
This is version 79 of the entry and version 2 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

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM