Pdpn
entrez
54320
canonical
uniprot
Q64294
canonical
ensembl
ENSRNOG00000014961
resolver
ensembl
ENSRNOG00065026882
resolver
ensp
ENSRNOP00000020316
resolver
ensp
ENSRNOP00000090610
resolver
ensp
ENSRNOP00065038067
resolver
enst
ENSRNOT00000020316
resolver
enst
ENSRNOT00000111603
resolver
enst
ENSRNOT00065046427
resolver
genesymbol
Pdpn
resolver
uniprot
A0A0G2JSN8
resolver
uniprot
A0A8I6AE24
resolver
uniprot
O08731
resolver
uniprot
O55210
resolver
uniprot_entry
A0A0G2JSN8_RAT
resolver
uniprot_entry
A0A8I6AE24_RAT
resolver
uniprot_entry
PDPN_RAT
resolver
uniprot_sec
O08731
resolver
uniprot_sec
O55210
resolver
amino_acid_sequence
MWTAPVLLWVLGSVWFWDSAQGGAIGALEDDLVTPGPGDDMVNPGLEDRIETTDTTGELDKSTAKAPLVPTQPPIEELPTSGTSDHDHKEHESTTTVKAVTSHSTDKKTTHPNRDNAGGETQTTDKKDGLAVVTLVGIIIGVLLAIGFIGGIIIVVMRKISGRFSP
uniprot
proteins
function
FUNCTION: 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 in 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). {ECO:0000250|UniProtKB:Q62011, ECO:0000250|UniProtKB:Q86YL7}.
uniprot
proteins
mass_dalton
17579
uniprot
proteins
post_translational_modification
PTM: 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). {ECO:0000250|UniProtKB:Q86YL7, ECO:0000269|PubMed:9920397}.; PTM: The N-terminus is blocked. {ECO:0000269|PubMed:9920397}.
uniprot
proteins
protein_family
Podoplanin family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
7851650
uniprot
proteins
pubmed
8833206
uniprot
proteins
pubmed
9327748
uniprot
proteins
pubmed
9761764
uniprot
proteins
pubmed
9920397
uniprot
proteins
sequence_length
166
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9327748}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:9327748}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, filopodium membrane {ECO:0000269|PubMed:9327748}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, microvillus membrane {ECO:0000269|PubMed:9327748}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000269|PubMed:9327748}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:Q86YL7}. Apical cell membrane {ECO:0000250|UniProtKB:Q86YL7}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q86YL7}. Cell projection, invadopodium {ECO:0000250|UniProtKB:Q86YL7}. Note=Localized to actin-rich microvilli and plasma membrane projections such as filopodia, lamellipodia and ruffles (PubMed:9327748). Association to the lipid rafts is required for PDPN-induced epithelial to mesenchymal transition (EMT). Colocalizes with CD9 in tetraspanin microdomains. Localized at invadopodium adhesion rings in tumor cell. Association to the lipid rafts is essential for PDPN recruitment to invadopodia and ECM degradation (By similarity). {ECO:0000250|UniProtKB:Q86YL7, ECO:0000269|PubMed:9327748}.
uniprot
proteins
transmembrane_region
TRANSMEM 136..156; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins