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Protein

Podoplanin

Gene

Pdpn

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

Functioni

May be involved in cell migration and/or actin cytoskeleton organization. When expressed in keratinocytes, induces changes in cell morphology with transfected cells showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion. Required for normal lung cell proliferation and alveolus formation at birth. Induces platelet aggregation. Does not have any effect on folic acid or amino acid transport. Does not function as a water channel or as a regulator of aquaporin-type water channels.5 Publications

GO - Biological processi

  • cell adhesion Source: MGI
  • cell morphogenesis Source: UniProtKB
  • cell motility Source: GO_Central
  • cell proliferation Source: MGI
  • lung alveolus development Source: MGI
  • lung development Source: MGI
  • lymphangiogenesis Source: MGI
  • positive regulation of cell migration Source: MGI
  • positive regulation of cellular component movement Source: UniProtKB
  • prostaglandin metabolic process Source: MGI
  • regulation of cell shape Source: UniProtKB-KW
  • regulation of G1/S transition of mitotic cell cycle Source: MGI
  • signal transduction Source: MGI
  • single organismal cell-cell adhesion Source: MGI
  • tube morphogenesis Source: MGI
  • visceral serous pericardium development Source: DFLAT
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell shape

Keywords - Ligandi

Sialic acid

Enzyme and pathway databases

ReactomeiR-MMU-114604. GPVI-mediated activation cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Podoplanin
Alternative name(s):
Aggrus
Glycoprotein 38
Short name:
Gp38
OTS-8
PA2.26 antigen
T1-alpha
Short name:
T1A
Transmembrane glycoprotein E11
Gene namesi
Name:Pdpn
Synonyms:Gp38, Ots8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:103098. Pdpn.

Subcellular locationi

  • Membrane 1 Publication; Single-pass type I membrane protein 1 Publication
  • Cell projectionlamellipodium membrane 1 Publication; Single-pass type I membrane protein 1 Publication
  • Cell projectionfilopodium membrane 1 Publication; Single-pass type I membrane protein 1 Publication
  • Cell projectionmicrovillus membrane 1 Publication; Single-pass type I membrane protein 1 Publication
  • Cell projectionruffle membrane 1 Publication; Single-pass type I membrane protein 1 Publication

  • Note: Localized to actin-rich microvilli and plasma membrane projections such as filopodia, lamellipodia and ruffles.

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini23 – 141ExtracellularSequence analysisAdd BLAST119
Transmembranei142 – 162HelicalSequence analysisAdd BLAST21
Topological domaini163 – 172Cytoplasmic10

GO - Cellular componenti

  • external side of plasma membrane Source: MGI
  • filopodium Source: UniProtKB
  • filopodium membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • lamellipodium Source: UniProtKB
  • lamellipodium membrane Source: UniProtKB-SubCell
  • microvillus membrane Source: UniProtKB-SubCell
  • plasma membrane Source: MGI
  • ruffle Source: UniProtKB
  • ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice die at birth of respiratory failure due to a low number of attenuated type I cells, narrow and irregular air spaces, and defective formation of alveolar saccules.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi34T → A: Eliminates platelet aggregation activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000002135223 – 172PodoplaninAdd BLAST150

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi37O-linked (GalNAc...)Sequence analysis1
Glycosylationi51O-linked (GalNAc...)Sequence analysis1
Glycosylationi52O-linked (GalNAc...)Sequence analysis1
Glycosylationi53O-linked (GalNAc...)Sequence analysis1
Glycosylationi56O-linked (GalNAc...)Sequence analysis1
Glycosylationi60N-linked (GlcNAc...)Sequence analysis1
Glycosylationi63O-linked (GalNAc...)Sequence analysis1
Glycosylationi71O-linked (GalNAc...)Sequence analysis1
Glycosylationi77O-linked (GalNAc...)Sequence analysis1
Glycosylationi85O-linked (GalNAc...)Sequence analysis1
Glycosylationi86O-linked (GalNAc...)Sequence analysis1
Glycosylationi87O-linked (GalNAc...)Sequence analysis1
Glycosylationi89O-linked (GalNAc...)Sequence analysis1
Glycosylationi90O-linked (GalNAc...)Sequence analysis1
Glycosylationi100O-linked (GalNAc...)Sequence analysis1
Glycosylationi101O-linked (GalNAc...)Sequence analysis1
Glycosylationi102O-linked (GalNAc...)Sequence analysis1
Glycosylationi107O-linked (GalNAc...)Sequence analysis1
Glycosylationi115O-linked (GalNAc...)Sequence analysis1

Post-translational modificationi

Extensively O-glycosylated. Contains sialic acid residues. O-glycosylation is necessary for platelet aggregation activity.2 Publications
The N-terminus is blocked.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ62011.
PaxDbiQ62011.
PRIDEiQ62011.

PTM databases

iPTMnetiQ62011.
PhosphoSitePlusiQ62011.

Expressioni

Tissue specificityi

Detected at high levels in lung and brain, at lower levels in kidney, stomach, liver, spleen and esophagus, and not detected in skin and small intestine. Expressed in epithelial cells of choroid plexus, ependyma, glomerulus and alveolus, in mesothelial cells and in endothelia of lymphatic vessels. Also expressed in stromal cells of peripheral lymphoid tissue and thymic epithelial cells. Detected in carcinoma cell lines and cultured fibroblasts. Expressed at higher levels in colon carcinomas than in normal colon tissue.3 Publications

Inductioni

Down-regulated by treatment with puromycin aminonucleoside.1 Publication

Gene expression databases

BgeeiENSMUSG00000028583.
CleanExiMM_PDPN.
ExpressionAtlasiQ62011. baseline and differential.
GenevisibleiQ62011. MM.

Interactioni

Protein-protein interaction databases

IntActiQ62011. 1 interactor.
STRINGi10090.ENSMUSP00000030317.

Structurei

Secondary structure

1172
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi81 – 83Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IETX-ray2.20Q/X76-84[»]
ProteinModelPortaliQ62011.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the podoplanin family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410J49G. Eukaryota.
ENOG41116TP. LUCA.
GeneTreeiENSGT00390000000013.
HOGENOMiHOG000231122.
HOVERGENiHBG080131.
InParanoidiQ62011.
KOiK16778.
OMAiETTGMEG.
OrthoDBiEOG091G0ZYJ.
PhylomeDBiQ62011.
TreeFamiTF337068.

Family and domain databases

InterProiIPR008783. Podoplanin.
[Graphical view]
PfamiPF05808. Podoplanin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q62011-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWTVPVLFWV LGSVWFWDSA QGGTIGVNED DIVTPGTGDG MVPPGIEDKI
60 70 80 90 100
TTTGATGGLN ESTGKAPLVP TQRERGTKPP LEELSTSATS DHDHREHEST
110 120 130 140 150
TTVKVVTSHS VDKKTSHPNR DNAGDETQTT DKKDGLPVVT LVGIIVGVLL
160 170
AIGFVGGIFI VVMKKISGRF SP
Length:172
Mass (Da):18,233
Last modified:November 1, 1997 - v2
Checksum:iC035ED251918CE6F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti29 – 31EDD → KNN in AAA37724 (PubMed:1402691).Curated3
Sequence conflicti38 – 39GD → EN in AAA37724 (PubMed:1402691).Curated2
Sequence conflicti170 – 172FSP → SRPKELNRTGCSPNTSENKR ASNLPCSPSSSCGGR in AAA39866 (PubMed:2088477).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73748 mRNA. Translation: AAA39866.1.
M96645 mRNA. Translation: AAA37724.1.
AJ250246 mRNA. Translation: CAB58997.1.
AJ297944 mRNA. Translation: CAC16152.1.
AY115493 Genomic DNA. Translation: AAM66761.1.
AK158855 mRNA. Translation: BAE34695.1.
AL611982 Genomic DNA. Translation: CAM21724.1.
BC026551 mRNA. Translation: AAH26551.1.
CCDSiCCDS38943.1.
PIRiA54560.
RefSeqiNP_001277751.1. NM_001290822.1.
NP_034459.2. NM_010329.3.
UniGeneiMm.2976.

Genome annotation databases

EnsembliENSMUST00000030317; ENSMUSP00000030317; ENSMUSG00000028583.
ENSMUST00000181754; ENSMUSP00000137969; ENSMUSG00000096951.
GeneIDi14726.
KEGGimmu:14726.
UCSCiuc008vqa.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73748 mRNA. Translation: AAA39866.1.
M96645 mRNA. Translation: AAA37724.1.
AJ250246 mRNA. Translation: CAB58997.1.
AJ297944 mRNA. Translation: CAC16152.1.
AY115493 Genomic DNA. Translation: AAM66761.1.
AK158855 mRNA. Translation: BAE34695.1.
AL611982 Genomic DNA. Translation: CAM21724.1.
BC026551 mRNA. Translation: AAH26551.1.
CCDSiCCDS38943.1.
PIRiA54560.
RefSeqiNP_001277751.1. NM_001290822.1.
NP_034459.2. NM_010329.3.
UniGeneiMm.2976.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IETX-ray2.20Q/X76-84[»]
ProteinModelPortaliQ62011.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ62011. 1 interactor.
STRINGi10090.ENSMUSP00000030317.

PTM databases

iPTMnetiQ62011.
PhosphoSitePlusiQ62011.

Proteomic databases

MaxQBiQ62011.
PaxDbiQ62011.
PRIDEiQ62011.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030317; ENSMUSP00000030317; ENSMUSG00000028583.
ENSMUST00000181754; ENSMUSP00000137969; ENSMUSG00000096951.
GeneIDi14726.
KEGGimmu:14726.
UCSCiuc008vqa.2. mouse.

Organism-specific databases

CTDi10630.
MGIiMGI:103098. Pdpn.

Phylogenomic databases

eggNOGiENOG410J49G. Eukaryota.
ENOG41116TP. LUCA.
GeneTreeiENSGT00390000000013.
HOGENOMiHOG000231122.
HOVERGENiHBG080131.
InParanoidiQ62011.
KOiK16778.
OMAiETTGMEG.
OrthoDBiEOG091G0ZYJ.
PhylomeDBiQ62011.
TreeFamiTF337068.

Enzyme and pathway databases

ReactomeiR-MMU-114604. GPVI-mediated activation cascade.

Miscellaneous databases

ChiTaRSiPdpn. mouse.
PROiQ62011.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028583.
CleanExiMM_PDPN.
ExpressionAtlasiQ62011. baseline and differential.
GenevisibleiQ62011. MM.

Family and domain databases

InterProiIPR008783. Podoplanin.
[Graphical view]
PfamiPF05808. Podoplanin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPDPN_MOUSE
AccessioniPrimary (citable) accession number: Q62011
Secondary accession number(s): A2A8J3, Q546R8, Q61612
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.