PDPN_MOUSE
ID PDPN_MOUSE Reviewed; 172 AA.
AC Q62011; A2A8J3; Q546R8; Q61612;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Podoplanin {ECO:0000250|UniProtKB:Q86YL7};
DE AltName: Full=Glycoprotein 38 {ECO:0000303|PubMed:1402691};
DE Short=Gp38 {ECO:0000303|PubMed:1402691};
DE AltName: Full=OTS-8 {ECO:0000303|PubMed:2088477};
DE AltName: Full=PA2.26 antigen {ECO:0000303|PubMed:10574709};
DE AltName: Full=Transmembrane glycoprotein E11 {ECO:0000303|Ref.5};
DE Short=E11 {ECO:0000303|Ref.5};
DE Flags: Precursor;
GN Name=Pdpn {ECO:0000312|MGI:MGI:103098};
GN Synonyms=Gp38 {ECO:0000303|PubMed:1402691}, Ots8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2088477;
RA Nose K., Saito H., Kuroki T.;
RT "Isolation of a gene sequence induced later by tumor-promoting 12-O-
RT tetradecanoylphorbol-13-acetate in mouse osteoblastic cells (MC3T3-E1) and
RT expressed constitutively in ras-transformed cells.";
RL Cell Growth Differ. 1:511-518(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=1402691; DOI=10.1084/jem.176.5.1477;
RA Farr A.G., Berry M.L., Kim A., Nelson A.J., Welch M.P., Aruffo A.;
RT "Characterization and cloning of a novel glycoprotein expressed by stromal
RT cells in T-dependent areas of peripheral lymphoid tissues.";
RL J. Exp. Med. 176:1477-1482(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-30 AND 66-73, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=10574709; DOI=10.1242/jcs.112.24.4601;
RA Scholl F.G., Gamallo C., Vilaro S., Quintanilla M.;
RT "Identification of PA2.26 antigen as a novel cell-surface mucin-type
RT glycoprotein that induces plasma membrane extensions and increased motility
RT in keratinocytes.";
RL J. Cell Sci. 112:4601-4613(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Kidney;
RX PubMed=12032185; DOI=10.1093/ndt/17.6.978;
RA Boucherot A., Schreiber R., Pavenstaedt H., Kunzelmann K.;
RT "Cloning and expression of the mouse glomerular podoplanin homologue
RT gp38P.";
RL Nephrol. Dial. Transplant. 17:978-984(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RA Lu Y., Zhang J., Harris M.A., Harris S.E., Bonewald L., Feng J.;
RT "Cloning and characterization studies of mouse E11 gene and its spatial and
RT temporal expression pattern during development.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12654292; DOI=10.1016/s0012-1606(02)00098-2;
RA Ramirez M.I., Millien G., Hinds A., Cao Y., Seldin D.C., Williams M.C.;
RT "T1alpha, a lung type I cell differentiation gene, is required for normal
RT lung cell proliferation and alveolus formation at birth.";
RL Dev. Biol. 256:61-72(2003).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF THR-34.
RX PubMed=14522983; DOI=10.1074/jbc.m309935200;
RA Kato Y., Fujita N., Kunita A., Sato S., Kaneko M., Osawa M., Tsuruo T.;
RT "Molecular identification of aggrus/T1alpha as a platelet aggregation-
RT inducing factor expressed in colorectal tumors.";
RL J. Biol. Chem. 278:51599-51605(2003).
RN [11]
RP FUNCTION, AND GLYCOSYLATION.
RX PubMed=15231832; DOI=10.1074/jbc.m407210200;
RA Kaneko M., Kato Y., Kunita A., Fujita N., Tsuruo T., Osawa M.;
RT "Functional sialylated O-glycan to platelet aggregation on Aggrus
RT (T1alpha/Podoplanin) molecules expressed in Chinese hamster ovary cells.";
RL J. Biol. Chem. 279:38838-38843(2004).
RN [12]
RP FUNCTION, AND INTERACTION WITH CLEC1B.
RX PubMed=17616532; DOI=10.1074/jbc.m702327200;
RA Suzuki-Inoue K., Kato Y., Inoue O., Kaneko M.K., Mishima K., Yatomi Y.,
RA Yamazaki Y., Narimatsu H., Ozaki Y.;
RT "Involvement of the snake toxin receptor CLEC-2, in podoplanin-mediated
RT platelet activation, by cancer cells.";
RL J. Biol. Chem. 282:25993-26001(2007).
RN [13]
RP DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=20110424; DOI=10.1182/blood-2009-04-216069;
RA Uhrin P., Zaujec J., Breuss J.M., Olcaydu D., Chrenek P., Stockinger H.,
RA Fuertbauer E., Moser M., Haiko P., Faessler R., Alitalo K., Binder B.R.,
RA Kerjaschki D.;
RT "Novel function for blood platelets and podoplanin in developmental
RT separation of blood and lymphatic circulation.";
RL Blood 115:3997-4005(2010).
RN [14]
RP INDUCTION.
RX PubMed=20962267; DOI=10.1091/mbc.e10-06-0489;
RA Martin-Villar E., Fernandez-Munoz B., Parsons M., Yurrita M.M., Megias D.,
RA Perez-Gomez E., Jones G.E., Quintanilla M.;
RT "Podoplanin associates with CD44 to promote directional cell migration.";
RL Mol. Biol. Cell 21:4387-4399(2010).
RN [15]
RP PHOSPHORYLATION, AND MUTAGENESIS OF SER-167 AND SER-171.
RX PubMed=23530051; DOI=10.1074/jbc.c112.446823;
RA Krishnan H., Ochoa-Alvarez J.A., Shen Y., Nevel E., Lakshminarayanan M.,
RA Williams M.C., Ramirez M.I., Miller W.T., Goldberg G.S.;
RT "Serines in the intracellular tail of podoplanin (PDPN) regulate cell
RT motility.";
RL J. Biol. Chem. 288:12215-12221(2013).
RN [16]
RP FUNCTION, AND DOMAIN.
RX PubMed=25347465; DOI=10.1038/ni.3035;
RA Astarita J.L., Cremasco V., Fu J., Darnell M.C., Peck J.R.,
RA Nieves-Bonilla J.M., Song K., Kondo Y., Woodruff M.C., Gogineni A.,
RA Onder L., Ludewig B., Weimer R.M., Carroll M.C., Mooney D.J., Xia L.,
RA Turley S.J.;
RT "The CLEC-2-podoplanin axis controls the contractility of fibroblastic
RT reticular cells and lymph node microarchitecture.";
RL Nat. Immunol. 16:75-84(2015).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 76-84 IN COMPLEX WITH
RP IMMUNOGLOBULIN.
RX PubMed=20479270; DOI=10.1073/pnas.0915176107;
RA Brooks C.L., Schietinger A., Borisova S.N., Kufer P., Okon M., Hirama T.,
RA Mackenzie C.R., Wang L.X., Schreiber H., Evans S.V.;
RT "Antibody recognition of a unique tumor-specific glycopeptide antigen.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10056-10061(2010).
CC -!- FUNCTION: Mediates effects on cell migration and adhesion through its
CC different partners. During development plays a role in blood and
CC lymphatic vessels separation by binding CLEC1B, triggering CLEC1B
CC activation in platelets and leading to platelet activation and/or
CC aggregation (PubMed:14522983, PubMed:15231832, PubMed:20110424,
CC PubMed:17616532). Interaction with CD9, on the contrary, attenuates
CC platelet aggregation and pulmonary metastasis induced by PDPN. Mediates
CC effects on cell migration and adhesion through its different partners.
CC Through MSN or EZR interaction promotes epithelial-mesenchymal
CC transition (EMT) leading to ERZ phosphorylation and triggering RHOA
CC activation leading to cell migration increase and invasiveness.
CC Interaction with CD44 promotes directional cell migration in epithelial
CC and tumor cells (By similarity). In lymph nodes (LNs), controls
CC fibroblastic reticular cells (FRCs) adhesion to the extracellular
CC matrix (ECM) and contraction of the actomyosin by maintaining ERM
CC proteins (EZR; MSN and RDX) and MYL9 activation through association
CC with unknown transmembrane proteins. Engagement of CLEC1B by PDPN
CC promotes FRCs relaxation by blocking lateral membrane interactions
CC leading to reduction of ERM proteins (EZR; MSN and RDX) and MYL9
CC activation (PubMed:25347465). Through binding with LGALS8 may
CC participate in connection of the lymphatic endothelium to the
CC surrounding extracellular matrix (By similarity). In keratinocytes,
CC induces changes in cell morphology showing an elongated shape, numerous
CC membrane protrusions, major reorganization of the actin cytoskeleton,
CC increased motility and decreased cell adhesion (PubMed:10574709).
CC Controls invadopodia stability and maturation leading to efficient
CC degradation of the extracellular matrix (ECM) in tumor cells through
CC modulation of RHOC activity in order to activate ROCK1/ROCK2 and
CC LIMK1/LIMK2 and inactivation of CFL1 (By similarity). Required for
CC normal lung cell proliferation and alveolus formation at birth
CC (PubMed:12654292). Does not function as a water channel or as a
CC regulator of aquaporin-type water channels (By similarity). Does not
CC have any effect on folic acid or amino acid transport
CC (PubMed:12032185). {ECO:0000250|UniProtKB:Q86YL7,
CC ECO:0000269|PubMed:10574709, ECO:0000269|PubMed:12032185,
CC ECO:0000269|PubMed:12654292, ECO:0000269|PubMed:14522983,
CC ECO:0000269|PubMed:15231832, ECO:0000269|PubMed:17616532,
CC ECO:0000269|PubMed:20110424, ECO:0000269|PubMed:25347465}.
CC -!- SUBUNIT: Homodimer. Interacts with CLEC1B; the interaction is
CC independent of CLEC1B glycosylation and activates CLEC1B; the
CC interaction is dependent of sialic acid on O-glycans (PubMed:17616532).
CC Interacts with CD9; this interaction is homophilic and attenuates
CC platelet aggregation and pulmonary metastasis induced by PDPN.
CC Interacts with LGALS8; the interaction is glycosylation-dependent; may
CC participate in connection of the lymphatic endothelium to the
CC surrounding extracellular matrix. Interacts with HSPA9. Interacts (via
CC extracellular domain) with CD44; this interaction is required for PDPN-
CC mediated directional migration and regulation of lamellipodia
CC extension/stabilization during cell spreading and migration. Interacts
CC (via cytoplasmic domain) with MSN and EZR; activates RHOA and promotes
CC epithelial-mesenchymal transition. Interacts with CCL21; relocalized
CC PDPN to the basolateral membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q86YL7, ECO:0000269|PubMed:17616532}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10574709}; Single-
CC pass type I membrane protein {ECO:0000255}. Cell projection,
CC lamellipodium membrane {ECO:0000269|PubMed:10574709}; Single-pass type
CC I membrane protein {ECO:0000269|PubMed:10574709}. Cell projection,
CC filopodium membrane {ECO:0000269|PubMed:10574709}; Single-pass type I
CC membrane protein {ECO:0000255}. Cell projection, microvillus membrane
CC {ECO:0000269|PubMed:10574709}; Single-pass type I membrane protein
CC {ECO:0000255}. Cell projection, ruffle membrane
CC {ECO:0000269|PubMed:10574709}; Single-pass type I membrane protein
CC {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:Q86YL7}. Apical
CC cell membrane {ECO:0000250|UniProtKB:Q86YL7}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q86YL7}. Cell projection, invadopodium
CC {ECO:0000250|UniProtKB:Q86YL7}. Note=Localized to actin-rich microvilli
CC and plasma membrane projections such as filopodia, lamellipodia and
CC ruffles (PubMed:10574709). Association to the lipid rafts is required
CC for PDPN-induced epithelial to mesenchymal transition (EMT).
CC Colocalizes with CD9 in tetraspanin microdomains. Localized at
CC invadopodium adhesion rings in tumor cell. Association to the lipid
CC rafts is essential for PDPN recruitment to invadopodia and ECM
CC degradation (By similarity). {ECO:0000250|UniProtKB:Q86YL7,
CC ECO:0000269|PubMed:10574709}.
CC -!- TISSUE SPECIFICITY: Detected at high levels in lung and brain, at lower
CC levels in kidney, stomach, liver, spleen and esophagus, and not
CC detected in skin and small intestine. Expressed in epithelial cells of
CC choroid plexus, ependyma, glomerulus and alveolus, in mesothelial cells
CC and in endothelia of lymphatic vessels. Also expressed in stromal cells
CC of peripheral lymphoid tissue and thymic epithelial cells. Detected in
CC carcinoma cell lines and cultured fibroblasts. Expressed at higher
CC levels in colon carcinomas than in normal colon tissue.
CC {ECO:0000269|PubMed:10574709, ECO:0000269|PubMed:12032185,
CC ECO:0000269|PubMed:14522983}.
CC -!- DEVELOPMENTAL STAGE: At 12.5 dpc and 13.5 dpc is expressed in the
CC endothelial cells of forming lymph sacs. {ECO:0000269|PubMed:20110424}.
CC -!- INDUCTION: Down-regulated by treatment with puromycin aminonucleoside
CC (PubMed:12032185). Up-regulated during progression to highly aggressive
CC tumors and during epithelial-mesenchymal transition (EMT)
CC (PubMed:20962267). {ECO:0000269|PubMed:12032185,
CC ECO:0000269|PubMed:20962267}.
CC -!- DOMAIN: The cytoplasmic domain controls FRC elongation but is
CC dispensable for contraction (PubMed:25347465). The cytoplasmic domain
CC is essential for recruitment to invadopodia and ECM degradation (By
CC similarity). {ECO:0000250|UniProtKB:Q86YL7,
CC ECO:0000269|PubMed:25347465}.
CC -!- PTM: Extensively O-glycosylated. Contains sialic acid residues. O-
CC glycosylation is necessary for platelet aggregation activity.
CC Disialylated at Thr-52; sialic acid is critical for platelet-
CC aggregating activity and for CLEC1B interaction (By similarity).
CC {ECO:0000250|UniProtKB:Q86YL7, ECO:0000269|PubMed:10574709,
CC ECO:0000269|PubMed:15231832}.
CC -!- PTM: Phosphorylated by PKA; decreases cell migration.
CC {ECO:0000269|PubMed:23530051}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:Q64294}.
CC -!- DISRUPTION PHENOTYPE: Mice die at birth of respiratory failure due to a
CC low number of attenuated type I cells, narrow and irregular air spaces,
CC and defective formation of alveolar saccules (PubMed:12654292).
CC Knockout Pdpn mice neonates are smaller, and approximately 55% died
CC during the first postnatal week. However, approximately 20% survived,
CC had normal weights and life spans, and are fertile (PubMed:20110424).
CC {ECO:0000269|PubMed:12654292, ECO:0000269|PubMed:20110424}.
CC -!- SIMILARITY: Belongs to the podoplanin family. {ECO:0000305}.
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DR EMBL; M73748; AAA39866.1; -; mRNA.
DR EMBL; M96645; AAA37724.1; -; mRNA.
DR EMBL; AJ250246; CAB58997.1; -; mRNA.
DR EMBL; AJ297944; CAC16152.1; -; mRNA.
DR EMBL; AY115493; AAM66761.1; -; Genomic_DNA.
DR EMBL; AK158855; BAE34695.1; -; mRNA.
DR EMBL; AL611982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026551; AAH26551.1; -; mRNA.
DR CCDS; CCDS38943.1; -.
DR PIR; A54560; A54560.
DR RefSeq; NP_001277751.1; NM_001290822.1.
DR RefSeq; NP_034459.2; NM_010329.3.
DR PDB; 3IET; X-ray; 2.20 A; Q/X=76-84.
DR PDB; 6LZ4; X-ray; 2.49 A; C/F=38-51.
DR PDBsum; 3IET; -.
DR PDBsum; 6LZ4; -.
DR AlphaFoldDB; Q62011; -.
DR SMR; Q62011; -.
DR IntAct; Q62011; 1.
DR STRING; 10090.ENSMUSP00000030317; -.
DR GlyGen; Q62011; 19 sites.
DR iPTMnet; Q62011; -.
DR PhosphoSitePlus; Q62011; -.
DR MaxQB; Q62011; -.
DR PaxDb; Q62011; -.
DR PRIDE; Q62011; -.
DR ProteomicsDB; 288024; -.
DR ABCD; Q62011; 17 sequenced antibodies.
DR Antibodypedia; 764; 1284 antibodies from 51 providers.
DR DNASU; 14726; -.
DR Ensembl; ENSMUST00000030317; ENSMUSP00000030317; ENSMUSG00000028583.
DR GeneID; 14726; -.
DR KEGG; mmu:14726; -.
DR UCSC; uc008vqa.2; mouse.
DR CTD; 10630; -.
DR MGI; MGI:103098; Pdpn.
DR VEuPathDB; HostDB:ENSMUSG00000028583; -.
DR eggNOG; ENOG502QRWU; Eukaryota.
DR GeneTree; ENSGT00390000000013; -.
DR InParanoid; Q62011; -.
DR OMA; HTHVPAT; -.
DR OrthoDB; 1303144at2759; -.
DR PhylomeDB; Q62011; -.
DR TreeFam; TF337068; -.
DR Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR BioGRID-ORCS; 14726; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Pdpn; mouse.
DR PRO; PR:Q62011; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q62011; protein.
DR Bgee; ENSMUSG00000028583; Expressed in yolk sac and 84 other tissues.
DR ExpressionAtlas; Q62011; baseline and differential.
DR Genevisible; Q62011; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0031527; C:filopodium membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0031258; C:lamellipodium membrane; ISS:UniProtKB.
DR GO; GO:0061851; C:leading edge of lamellipodium; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0031528; C:microvillus membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0097197; C:tetraspanin-enriched microdomain; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0019956; F:chemokine binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
DR GO; GO:0070252; P:actin-mediated cell contraction; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0048535; P:lymph node development; IMP:UniProtKB.
DR GO; GO:0001946; P:lymphangiogenesis; IMP:MGI.
DR GO; GO:0060838; P:lymphatic endothelial cell fate commitment; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; ISS:UniProtKB.
DR GO; GO:0010572; P:positive regulation of platelet activation; ISO:MGI.
DR GO; GO:1901731; P:positive regulation of platelet aggregation; IDA:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; IMP:MGI.
DR GO; GO:0030155; P:regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:2000392; P:regulation of lamellipodium morphogenesis; ISS:UniProtKB.
DR GO; GO:1904328; P:regulation of myofibroblast contraction; IMP:UniProtKB.
DR GO; GO:1900024; P:regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:0055093; P:response to hyperoxia; IBA:GO_Central.
DR GO; GO:0007266; P:Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IMP:MGI.
DR GO; GO:0035239; P:tube morphogenesis; ISO:MGI.
DR GO; GO:0061032; P:visceral serous pericardium development; TAS:DFLAT.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell membrane; Cell projection; Cell shape;
KW Developmental protein; Direct protein sequencing; Glycoprotein; Membrane;
KW Reference proteome; Sialic acid; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:Q86YL7"
FT CHAIN 23..172
FT /note="Podoplanin"
FT /id="PRO_0000021352"
FT TOPO_DOM 23..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..172
FT /note="Cytoplasmic"
FT REGION 49..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..147
FT /note="Requires for dimerization and lipidd rafts
FT association"
FT /evidence="ECO:0000250|UniProtKB:Q86YL7"
FT REGION 164..165
FT /note="Requires for interaction with MSN and EZR"
FT /evidence="ECO:0000250|UniProtKB:Q86YL7"
FT COMPBIAS 87..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 37
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q86YL7"
FT CARBOHYD 53
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT MUTAGEN 34
FT /note="T->A: Eliminates platelet aggregation activity."
FT /evidence="ECO:0000269|PubMed:14522983"
FT MUTAGEN 167
FT /note="S->A: 50% decrease of cell growth; when associated
FT with A-171. 50% increase of cell migration; when associated
FT with A-171."
FT /evidence="ECO:0000269|PubMed:23530051"
FT MUTAGEN 167
FT /note="S->D: Does not significantly increase cell motility;
FT when associated with D-171. Does not significantly decrease
FT cell growth; when associated with A-171."
FT /evidence="ECO:0000269|PubMed:23530051"
FT MUTAGEN 171
FT /note="S->A: 50% decrease of cell growth; when associated
FT with A-167. 50% increase of cell migration; when associated
FT with A-167."
FT /evidence="ECO:0000269|PubMed:23530051"
FT MUTAGEN 171
FT /note="S->D: Does not significantly increase cell motility;
FT when associated with D-171. Does not significantly decrease
FT cell growth; when associated with A-171."
FT /evidence="ECO:0000269|PubMed:23530051"
FT CONFLICT 29..31
FT /note="EDD -> KNN (in Ref. 2; AAA37724)"
FT /evidence="ECO:0000305"
FT CONFLICT 38..39
FT /note="GD -> EN (in Ref. 2; AAA37724)"
FT /evidence="ECO:0000305"
FT CONFLICT 170..172
FT /note="FSP -> SRPKELNRTGCSPNTSENKRASNLPCSPSSSCGGR (in Ref.
FT 1; AAA39866)"
FT /evidence="ECO:0000305"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3IET"
SQ SEQUENCE 172 AA; 18233 MW; C035ED251918CE6F CRC64;
MWTVPVLFWV LGSVWFWDSA QGGTIGVNED DIVTPGTGDG MVPPGIEDKI TTTGATGGLN
ESTGKAPLVP TQRERGTKPP LEELSTSATS DHDHREHEST TTVKVVTSHS VDKKTSHPNR
DNAGDETQTT DKKDGLPVVT LVGIIVGVLL AIGFVGGIFI VVMKKISGRF SP
