PDPN
entrez
10630
canonical
uniprot
Q86YL7
canonical
ensembl
ENSG00000162493
resolver
ensp
ENSP00000365225
resolver
ensp
ENSP00000365229
resolver
ensp
ENSP00000426063
resolver
ensp
ENSP00000427537
resolver
ensp
ENSP00000478125
resolver
genesymbol
PDPN
resolver
genesymbol_syn
GP36
resolver
hgnc
HGNC:29602
resolver
uniprot
A9Z1Y2
resolver
uniprot
B2R6J8
resolver
uniprot
E9PB68
resolver
uniprot
F6QWX5
resolver
uniprot
O60836
resolver
uniprot
O95128
resolver
uniprot
Q7L375
resolver
uniprot
Q8NBQ8
resolver
uniprot
Q8NBR3
resolver
uniprot_entry
PDPN_HUMAN
resolver
uniprot_sec
A9Z1Y2
resolver
uniprot_sec
B2R6J8
resolver
uniprot_sec
E9PB68
resolver
uniprot_sec
F6QWX5
resolver
uniprot_sec
O60836
resolver
uniprot_sec
O95128
resolver
uniprot_sec
Q7L375
resolver
uniprot_sec
Q8NBQ8
resolver
uniprot_sec
Q8NBR3
resolver
amino_acid_sequence
MWKVSALLFVLGSASLWVLAEGASTGQPEDDTETTGLEGGVAMPGAEDDVVTPGTSEDRYKSGLTTLVATSVNSVTGIRIEDLPTSESTVHAQEQSPSATASNVATSHSTEKVDGDTQTTVEKDGLSTVTLVGIIVGVLLAIGFIGAIIVVVMRKMSGRYSP
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:17222411, PubMed:17616532, PubMed:18215137). Interaction with CD9, on the contrary, attenuates platelet aggregation induced by PDPN (PubMed:18541721). 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 (PubMed:17046996, PubMed:21376833). Interaction with CD44 promotes directional cell migration in epithelial and tumor cells (PubMed:20962267). 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 (PubMed:19268462). 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:15515019). 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 (PubMed:25486435). 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 (PubMed:9651190). Does not have any effect on folic acid or amino acid transport (By similarity). {ECO:0000250|UniProtKB:Q62011, ECO:0000269|PubMed:14522983, ECO:0000269|PubMed:15231832, ECO:0000269|PubMed:15515019, ECO:0000269|PubMed:17046996, ECO:0000269|PubMed:17222411, ECO:0000269|PubMed:17616532, ECO:0000269|PubMed:18215137, ECO:0000269|PubMed:18541721, ECO:0000269|PubMed:19268462, ECO:0000269|PubMed:20962267, ECO:0000269|PubMed:21376833, ECO:0000269|PubMed:25486435, ECO:0000269|PubMed:9651190}.
uniprot
proteins
mass_dalton
16698
uniprot
proteins
mutagenesis
MUTAGEN 52; /note="T->A: Eliminates induction of platelet aggregation."; /evidence="ECO:0000269|PubMed:14522983"; MUTAGEN 137; /note="Missing: Prevents self-assembly and association to lipid rafts. Reduces the recruitment to invadopodium. Disrupts assembly into adhesion rings. Fails invadopodia-mediated ECM degradation."; /evidence="ECO:0000269|PubMed:21376833, ECO:0000269|PubMed:25486435"; MUTAGEN 154..159; /note="RKMSGR->QNMGSN: Does not affect localization at cell surface protrusions. Does not induce reorganization of the actin cytoskeleton. Increases cell migration collectively. Does not significant change RHOA activation. No effect on interaction with CD44. Impairs interaction with the EZR and MSN. Impairs epithelial to mesenchymal transition. Does not change localization at invadopodium. Fails to assemble into rings. Fails invadopodia-mediated ECM degradation."; /evidence="ECO:0000269|PubMed:17046996, ECO:0000269|PubMed:20962267, ECO:0000269|PubMed:25486435"; MUTAGEN 154..155; /note="RK->QN: Impairs interaction with the EZR and MSN. Impairs epithelial to mesenchymal transition. Does not affect localization at cell surface protrusions. Does not induce reorganization of the actin cytoskeleton. Increases cell migration collectively."; /evidence="ECO:0000269|PubMed:17046996"; MUTAGEN 159; /note="R->N: Highly decreases interaction with the EZR and MSN. Induces an intermediate phenotype between epithelial and mesenchymal. Does not affect localization at cell surface protrusions. Induces reorganization of the actin cytoskeleton oncomitantly with the induced morphological changes. Increases cell migration individually. Increases invasiveness. Enhances RHOA activity. Colocalizes at cell-surface protrusions with RHOA and RAC1."; /evidence="ECO:0000269|PubMed:17046996
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 (PubMed:17222411, PubMed:25458834). {ECO:0000269|PubMed:10393083, ECO:0000269|PubMed:15231832, ECO:0000269|PubMed:15515019, ECO:0000269|PubMed:17222411, ECO:0000269|PubMed:25458834}.; PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:Q64294}.; PTM: Cleaved by a metalloprotease within its extracellular (EC) domain, generating a membrane-bound C-terminal fragment (PCTF33) and an extracellular fragment. The resulting membrane-bound C-terminal fragment (PCTF33) is further processed between Val-150 and Val-151 by PSEN1/gamma-secretase generating the intracellular domain of podoplanin (PICD). {ECO:0000269|PubMed:24275092}.
uniprot
proteins
protein_family
Podoplanin family
uniprot
proteins
pubmed
10393083
uniprot
proteins
pubmed
14522983
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14978162
uniprot
proteins
pubmed
15231832
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15515019
uniprot
proteins
pubmed
16303743
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17046996
uniprot
proteins
pubmed
17222411
uniprot
proteins
pubmed
17616532
uniprot
proteins
pubmed
18215137
uniprot
proteins
pubmed
18541721
uniprot
proteins
pubmed
19268462
uniprot
proteins
pubmed
20962267
uniprot
proteins
pubmed
21376833
uniprot
proteins
pubmed
23541579
uniprot
proteins
pubmed
24275092
uniprot
proteins
pubmed
25458834
uniprot
proteins
pubmed
25486435
uniprot
proteins
pubmed
26872787
uniprot
proteins
pubmed
9651190
uniprot
proteins
sequence_length
162
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Podoplanin]: Membrane {ECO:0000269|PubMed:17046996, ECO:0000269|PubMed:20962267, ECO:0000305|PubMed:18215137}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q62011}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:17046996, ECO:0000269|PubMed:20962267}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q62011}. Cell projection, filopodium membrane {ECO:0000269|PubMed:17046996}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q62011}. Cell projection, microvillus membrane {ECO:0000269|PubMed:17046996}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q62011}. Cell projection, ruffle membrane {ECO:0000269|PubMed:17046996}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q62011}. Membrane raft {ECO:0000269|PubMed:21376833}. Apical cell membrane {ECO:0000269|PubMed:20962267}. Basolateral cell membrane {ECO:0000269|PubMed:14978162}. Cell projection, invadopodium {ECO:0000269|PubMed:25486435}. Note=Localized to actin-rich microvilli and plasma membrane projections such as filopodia, lamellipodia and ruffles (By similarity). Association to the lipid rafts is required for PDPN-induced epithelial to mesenchymal transition (EMT) (PubMed:21376833). Colocalizes with CD9 in tetraspanin microdomains (PubMed:18541721). Localized at invadopodium adhesion rings in tumor cell. Association to the lipid rafts is essential for PDPN recruitment to invadopodia and ECM degradation (PubMed:25486435). {ECO:0000250|UniProtKB:Q62011, ECO:0000269|PubMed:18541721, ECO:0000269|PubMed:21376833, ECO:0000269|PubMed:25486435}.; SUBCELLULAR LOCATION: [29kDa cytosolic podoplanin intracellular domain]: Cytoplasm, cytosol {ECO:0000269|PubMed:24275092}.
uniprot
proteins
transmembrane_region
TRANSMEM 132..152; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins