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Protein

Podoplanin

Gene

Pdpn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates effects on cell migration and adhesion through its different partners. During development plays a role in blood and lymphatic vessels separation by binding CLEC1B, triggering CLEC1B activation in platelets and leading to platelet activation and/or aggregation. Interaction with CD9, on the contrary, attenuates platelet aggregation and pulmonary metastasis induced by PDPN. Mediates effects on cell migration and adhesion through its different partners. Through MSN or EZR interaction promotes epithelial-mesenchymal transition (EMT) leading to ERZ phosphorylation and triggering RHOA activation leading to cell migration increase and invasiveness. Interaction with CD44 promotes directional cell migration in epithelial and tumor cells (By similarity). In lymph nodes (LNs), controls fibroblastic reticular cells (FRCs) adhesion to the extracellular matrix (ECM) and contraction of the actomyosin by maintaining ERM proteins (EZR; MSN and RDX) and MYL9 activation through association with unknown transmembrane proteins. Engagement of CLEC1B by PDPN promotes FRCs relaxation by blocking lateral membrane interactions leading to reduction of ERM proteins (EZR; MSN and RDX) and MYL9 activation (By similarity). Through binding with LGALS8 may participate to connection of the lymphatic endothelium to the surrounding extracellular matrix. In keratinocytes, induces changes in cell morphology showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion. Controls invadopodia stability and maturation leading to efficient degradation of the extracellular matrix (ECM) in tumor cells through modulation of RHOC activity in order to activate ROCK1/ROCK2 and LIMK1/LIMK2 and inactivation of CFL1 (By similarity). Required for normal lung cell proliferation and alveolus formation at birth (By similarity). Does not function as a water channel or as a regulator of aquaporin-type water channels (By similarity). Does not have any effect on folic acid or amino acid transport (By similarity).By similarity

Miscellaneous

Down-regulated in puromycin aminonucleoside nephrosis (PAN).

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein
Biological processCell shape
LigandSialic acid

Names & Taxonomyi

Protein namesi
Recommended name:
Podoplanin1 Publication
Alternative name(s):
E11 antigen epitope1 Publication
RTI1402 Publications
T1-alpha1 Publication
Short name:
T1A1 Publication
Type I cell 40 kDa protein
Gene namesi
Name:PdpnImported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61819. Pdpn.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini23 – 135ExtracellularSequence analysisAdd BLAST113
Transmembranei136 – 156HelicalSequence analysisAdd BLAST21
Topological domaini157 – 166CytoplasmicSequence analysis10

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22By similarityAdd BLAST22
ChainiPRO_000002135323 – 166PodoplaninAdd BLAST144

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi34O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi52O-linked (GalNAc...) threonineBy similarity1
Glycosylationi55O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi56O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi62O-linked (GalNAc...) serineSequence analysis1
Glycosylationi63O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi71O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi80O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi81O-linked (GalNAc...) serineSequence analysis1
Glycosylationi83O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi84O-linked (GalNAc...) serineSequence analysis1
Glycosylationi94O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi95O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi96O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi101O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi105O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi109O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi110O-linked (GalNAc...) threonineSequence analysis1

Post-translational modificationi

Extensively O-glycosylated. Contains sialic acid residues. O-glycosylation is necessary for platelet aggregation activity. Disialylated at Thr-52; sialic acid is critical for platelet-aggregating activity and for CLEC1B interaction (By similarity).By similarity1 Publication
The N-terminus is blocked.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ64294.
PRIDEiQ64294.

Expressioni

Tissue specificityi

In adult kidney, expressed on the urinary surface and foot processes of podocytes and in parietal epithelial cells of Bowman's capsule where it is localized to luminal surfaces. In lung, expressed exclusively on luminal surfaces of type I alveolar epithelial cells and pleural mesothelial cells. Not expressed in type II alveolar cells. In bone, expressed in osteocytes and osteoblasts. In spleen, liver, stomach and intestine, expressed in mesoepithelium. Also expressed in thymic epithelial cells, choroid plexus and leptomeninges.2 Publications

Developmental stagei

In newborn kidney, not detected at the vesicle stage. First detected in S-shaped bodies.1 Publication

Interactioni

Subunit structurei

Homodimer. Interacts with CLEC1B; the interaction is independent of CLEC1B glycosylation and activates CLEC1B; the interaction is dependent of sialic acid on O-glycans. Interacts with CD9; this interaction is homophilic and attenuates platelet aggregation and pulmonary metastasis induced by PDPN. Interacts with LGALS8; the interaction is glycosylation-dependent; may participate to connection of the lymphatic endothelium to the surrounding extracellular matrix. Interacts with HSPA9. Interacts (via extracellular domain) with CD44; this interaction is required for PDPN-mediated directional migration and regulation of lamellipodia extension/stabilization during cell spreading and migration. Interacts (via cytoplasmic domain) with MSN and EZR; activates RHOA and promotes epithelial-mesenchymal transition. Interacts with CCL21; relocalized PDPN to the basolateral membrane.By similarity

GO - Molecular functioni

Protein-protein interaction databases

CORUMiQ64294.
STRINGi10116.ENSRNOP00000020316.

Structurei

3D structure databases

SMRiQ64294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni137 – 141Requires for dimerization and lipid rafts associationBy similarity5
Regioni158 – 159Requires for interaction with MSN and EZRBy similarity2

Domaini

The cytoplasmic domain controls FRC elongation but is dispensable for contraction (By similarity). The cytoplasmic domain is essential for recruitment to invadopodia and ECM degradation (By similarity).By similarity

Sequence similaritiesi

Belongs to the podoplanin family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410J49G. Eukaryota.
ENOG41116TP. LUCA.
HOGENOMiHOG000231122.
HOVERGENiHBG080131.
InParanoidiQ64294.
KOiK16778.
PhylomeDBiQ64294.
TreeFamiTF337068.

Family and domain databases

InterProiView protein in InterPro
IPR008783. Podoplanin.
PfamiView protein in Pfam
PF05808. Podoplanin. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q64294-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWTAPVLLWV LGSVWFWDSA QGGAIGALED DLVTPGPGDD MVNPGLEDRI
60 70 80 90 100
ETTDTTGELD KSTAKAPLVP TQPPIEELPT SGTSDHDHKE HESTTTVKAV
110 120 130 140 150
TSHSTDKKTT HPNRDNAGGE TQTTDKKDGL AVVTLVGIII GVLLAIGFIG
160
GIIIVVMRKI SGRFSP
Length:166
Mass (Da):17,579
Last modified:November 1, 1996 - v1
Checksum:iB97C58292B664468
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti112P → S in AAB86438 (PubMed:9327748).Curated1
Sequence conflicti112P → S in AAH72492 (PubMed:15489334).Curated1
Sequence conflicti135 – 137LVG → WSA in AAB93880 (PubMed:9761764).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07797 mRNA. Translation: AAA92789.1.
U32115 mRNA. Translation: AAA74431.1.
U96449 mRNA. Translation: AAB86438.1.
U92440, U92081 Genomic DNA. Translation: AAB93880.1.
BC072492 mRNA. Translation: AAH72492.1.
RefSeqiNP_062231.1. NM_019358.1.
UniGeneiRn.794.

Genome annotation databases

GeneIDi54320.
KEGGirno:54320.
UCSCiRGD:61819. rat.

Similar proteinsi

Entry informationi

Entry nameiPDPN_RAT
AccessioniPrimary (citable) accession number: Q64294
Secondary accession number(s): O08731, O55210
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 22, 2017
This is version 108 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families