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Protein

Phospholipid phosphatase 6

Gene

Plpp6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Phosphatase that dephosphorylates presqualene diphosphate (PSDP) into presqualene monophosphate (PSMP), suggesting that it may be indirectly involved in innate immunity. PSDP is a bioactive lipid that rapidly remodels to presqualene monophosphate PSMP upon cell activation. Displays diphosphate phosphatase activity with a substrate preference for PSDP > FDP > phosphatidic acid (By similarity).By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipid phosphatase 6By similarity (EC:3.1.3.-)
Alternative name(s):
Phosphatidic acid phosphatase type 2 domain-containing protein 2
Presqualene diphosphate phosphatase
Gene namesi
Name:Plpp6By similarity
Synonyms:Ppapdc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1921661. Plpp6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei132 – 15221HelicalSequence analysisAdd
BLAST
Transmembranei162 – 18221HelicalSequence analysisAdd
BLAST
Transmembranei226 – 24621HelicalSequence analysisAdd
BLAST
Transmembranei258 – 27821HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 292292Phospholipid phosphatase 6PRO_0000239397Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphoserineBy similarity
Modified residuei67 – 671PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9D4F2.
MaxQBiQ9D4F2.
PaxDbiQ9D4F2.
PRIDEiQ9D4F2.

PTM databases

iPTMnetiQ9D4F2.
PhosphoSiteiQ9D4F2.

Expressioni

Gene expression databases

BgeeiQ9D4F2.
GenevisibleiQ9D4F2. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000047776.

Structurei

3D structure databases

ProteinModelPortaliQ9D4F2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4268. Eukaryota.
ENOG410ZVFK. LUCA.
GeneTreeiENSGT00390000012789.
HOGENOMiHOG000231931.
HOVERGENiHBG054746.
InParanoidiQ9D4F2.
OMAiLGYMQYS.
OrthoDBiEOG7BW0MW.
PhylomeDBiQ9D4F2.
TreeFamiTF323272.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
InterProiIPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9D4F2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSPRRTIEG RPLGSSGGSS VPGSPAHGGG SGGGRFEFQS LLNCRAGADP
60 70 80 90 100
ACARLRASDS PVHRRGSFPL AASGPAQAAP APPPEDARMN LNPSFLGIAL
110 120 130 140 150
RSLLAIDLWL SKKLGVCAGE SSAWGSVRPL MKLLEISGHG IPWLLGTLYC
160 170 180 190 200
LLRSDSWAGR EVLMNLLFAL LLDLLLVAVI KGLVRRRRPA HNQKDMFFTL
210 220 230 240 250
SVDRYSFPSG HATRAALVSR FILNHLVLAI PLRVLVVLWA FVLGLSRVML
260 270 280 290
GRHNVTDVAF GFFLGYMQYS IVDYCWLSPH NVPVLFVLWN QQ
Length:292
Mass (Da):31,744
Last modified:June 1, 2001 - v1
Checksum:i8B28C6DCA0BE7F17
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK016572 mRNA. Translation: BAB30313.1.
BC052412 mRNA. Translation: AAH52412.1.
CCDSiCCDS29728.1.
RefSeqiNP_083198.1. NM_028922.3.
UniGeneiMm.441887.

Genome annotation databases

EnsembliENSMUST00000045674; ENSMUSP00000047776; ENSMUSG00000040105.
GeneIDi74411.
KEGGimmu:74411.
UCSCiuc008hcr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK016572 mRNA. Translation: BAB30313.1.
BC052412 mRNA. Translation: AAH52412.1.
CCDSiCCDS29728.1.
RefSeqiNP_083198.1. NM_028922.3.
UniGeneiMm.441887.

3D structure databases

ProteinModelPortaliQ9D4F2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000047776.

PTM databases

iPTMnetiQ9D4F2.
PhosphoSiteiQ9D4F2.

Proteomic databases

EPDiQ9D4F2.
MaxQBiQ9D4F2.
PaxDbiQ9D4F2.
PRIDEiQ9D4F2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045674; ENSMUSP00000047776; ENSMUSG00000040105.
GeneIDi74411.
KEGGimmu:74411.
UCSCiuc008hcr.2. mouse.

Organism-specific databases

CTDi403313.
MGIiMGI:1921661. Plpp6.

Phylogenomic databases

eggNOGiKOG4268. Eukaryota.
ENOG410ZVFK. LUCA.
GeneTreeiENSGT00390000012789.
HOGENOMiHOG000231931.
HOVERGENiHBG054746.
InParanoidiQ9D4F2.
OMAiLGYMQYS.
OrthoDBiEOG7BW0MW.
PhylomeDBiQ9D4F2.
TreeFamiTF323272.

Miscellaneous databases

PROiQ9D4F2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D4F2.
GenevisibleiQ9D4F2. MM.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
InterProiIPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.
    Tissue: Testis.
  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: C57BL/6J.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung and Spleen.

Entry informationi

Entry nameiPLPP6_MOUSE
AccessioniPrimary (citable) accession number: Q9D4F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.