Pdpn
entrez
14726
canonical
uniprot
Q62011
canonical
ensembl
ENSMUSG00000028583
resolver
ensp
ENSMUSP00000030317
resolver
ensp
ENSMUSP00000113776
resolver
enst
ENSMUST00000030317
resolver
enst
ENSMUST00000119654
resolver
genesymbol
Pdpn
resolver
genesymbol_syn
Gp38
resolver
genesymbol_syn
Ots8
resolver
uniprot
A2A8J3
resolver
uniprot
A8Y5F6
resolver
uniprot
Q546R8
resolver
uniprot
Q61612
resolver
uniprot_entry
A8Y5F6_MOUSE
resolver
uniprot_entry
PDPN_MOUSE
resolver
uniprot_sec
A2A8J3
resolver
uniprot_sec
Q546R8
resolver
uniprot_sec
Q61612
resolver
amino_acid_sequence
MWTVPVLFWVLGSVWFWDSAQGGTIGVNEDDIVTPGTGDGMVPPGIEDKITTTGATGGLNESTGKAPLVPTQRERGTKPPLEELSTSATSDHDHREHESTTTVKVVTSHSVDKKTSHPNRDNAGDETQTTDKKDGLPVVTLVGIIVGVLLAIGFVGGIFIVVMKKISGRFSP
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 (PubMed:14522983, PubMed:15231832, PubMed:17616532, PubMed:20110424). 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 (PubMed:25347465). Through binding with LGALS8 may participate in connection of the lymphatic endothelium to the surrounding extracellular matrix (By similarity). 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 (PubMed:10574709). 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 (PubMed:12654292). 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 (PubMed:12032185). {ECO:0000250|UniProtKB:Q86YL7, ECO:0000269|PubMed:10574709, ECO:0000269|PubMed:12032185, ECO:0000269|PubMed:12654292, ECO:0000269|PubMed:14522983, ECO:0000269|PubMed:15231832, ECO:0000269|PubMed:17616532, ECO:0000269|PubMed:20110424, ECO:0000269|PubMed:25347465}.
uniprot
proteins
mass_dalton
18233
uniprot
proteins
mutagenesis
MUTAGEN 34; /note="T->A: Eliminates platelet aggregation activity."; /evidence="ECO:0000269|PubMed:14522983"; MUTAGEN 167; /note="S->A: 50% decrease of cell growth; when associated with A-171. 50% increase of cell migration; when associated with A-171."; /evidence="ECO:0000269|PubMed:23530051"; MUTAGEN 167; /note="S->D: Does not significantly increase cell motility; when associated with D-171. Does not significantly decrease cell growth; when associated with A-171."; /evidence="ECO:0000269|PubMed:23530051"; MUTAGEN 171; /note="S->A: 50% decrease of cell growth; when associated with A-167. 50% increase of cell migration; when associated with A-167."; /evidence="ECO:0000269|PubMed:23530051"; MUTAGEN 171; /note="S->D: Does not significantly increase cell motility; when associated with D-171. Does not significantly decrease cell growth; when associated with A-171."; /evidence="ECO:0000269|PubMed:23530051
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:10574709, ECO:0000269|PubMed:15231832}.; PTM: Phosphorylated by PKA; decreases cell migration. {ECO:0000269|PubMed:23530051}.; PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:Q64294}.
uniprot
proteins
protein_family
Podoplanin family
uniprot
proteins
pubmed
10574709
uniprot
proteins
pubmed
12032185
uniprot
proteins
pubmed
12654292
uniprot
proteins
pubmed
1402691
uniprot
proteins
pubmed
14522983
uniprot
proteins
pubmed
15231832
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17616532
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20110424
uniprot
proteins
pubmed
20479270
uniprot
proteins
pubmed
2088477
uniprot
proteins
pubmed
20962267
uniprot
proteins
pubmed
23530051
uniprot
proteins
pubmed
25347465
uniprot
proteins
pubmed
28179430
uniprot
proteins
sequence_length
172
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10574709}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:10574709}; Single-pass type I membrane protein {ECO:0000269|PubMed:10574709}. Cell projection, filopodium membrane {ECO:0000269|PubMed:10574709}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, microvillus membrane {ECO:0000269|PubMed:10574709}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000269|PubMed:10574709}; 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:10574709). 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:10574709}.
uniprot
proteins
transmembrane_region
TRANSMEM 142..162; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins