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Podoplanin (Glycoprotein 38) (Gp38) (OTS-8) (PA2.26 antigen) (Transmembrane glycoprotein E11) (E11)

 PDPN_MOUSE              Reviewed;         172 AA.
Q62011; A2A8J3; Q546R8; Q61612;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
22-NOV-2017, entry version 135.
RecName: Full=Podoplanin {ECO:0000250|UniProtKB:Q86YL7};
AltName: Full=Glycoprotein 38 {ECO:0000303|PubMed:1402691};
Short=Gp38 {ECO:0000303|PubMed:1402691};
AltName: Full=OTS-8 {ECO:0000303|PubMed:2088477};
AltName: Full=PA2.26 antigen {ECO:0000303|PubMed:10574709};
AltName: Full=Transmembrane glycoprotein E11 {ECO:0000303|Ref.5};
Short=E11 {ECO:0000303|Ref.5};
Flags: Precursor;
Name=Pdpn {ECO:0000312|MGI:MGI:103098};
Synonyms=Gp38 {ECO:0000303|PubMed:1402691}, Ots8;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2088477;
Nose K., Saito H., Kuroki T.;
"Isolation of a gene sequence induced later by tumor-promoting 12-O-
tetradecanoylphorbol-13-acetate in mouse osteoblastic cells (MC3T3-E1)
and expressed constitutively in ras-transformed cells.";
Cell Growth Differ. 1:511-518(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=1402691; DOI=10.1084/jem.176.5.1477;
Farr A.G., Berry M.L., Kim A., Nelson A.J., Welch M.P., Aruffo A.;
"Characterization and cloning of a novel glycoprotein expressed by
stromal cells in T-dependent areas of peripheral lymphoid tissues.";
J. Exp. Med. 176:1477-1482(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-30 AND 66-73,
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
PubMed=10574709;
Scholl F.G., Gamallo C., Vilaro S., Quintanilla M.;
"Identification of PA2.26 antigen as a novel cell-surface mucin-type
glycoprotein that induces plasma membrane extensions and increased
motility in keratinocytes.";
J. Cell Sci. 112:4601-4613(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
INDUCTION.
TISSUE=Kidney;
PubMed=12032185; DOI=10.1093/ndt/17.6.978;
Boucherot A., Schreiber R., Pavenstaedt H., Kunzelmann K.;
"Cloning and expression of the mouse glomerular podoplanin homologue
gp38P.";
Nephrol. Dial. Transplant. 17:978-984(2002).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
Lu Y., Zhang J., Harris M.A., Harris S.E., Bonewald L., Feng J.;
"Cloning and characterization studies of mouse E11 gene and its
spatial and temporal expression pattern during development.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Visual cortex;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12654292; DOI=10.1016/S0012-1606(02)00098-2;
Ramirez M.I., Millien G., Hinds A., Cao Y., Seldin D.C.,
Williams M.C.;
"T1alpha, a lung type I cell differentiation gene, is required for
normal lung cell proliferation and alveolus formation at birth.";
Dev. Biol. 256:61-72(2003).
[10]
FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF THR-34.
PubMed=14522983; DOI=10.1074/jbc.M309935200;
Kato Y., Fujita N., Kunita A., Sato S., Kaneko M., Osawa M.,
Tsuruo T.;
"Molecular identification of aggrus/T1alpha as a platelet aggregation-
inducing factor expressed in colorectal tumors.";
J. Biol. Chem. 278:51599-51605(2003).
[11]
FUNCTION, AND GLYCOSYLATION.
PubMed=15231832; DOI=10.1074/jbc.M407210200;
Kaneko M., Kato Y., Kunita A., Fujita N., Tsuruo T., Osawa M.;
"Functional sialylated O-glycan to platelet aggregation on Aggrus
(T1alpha/Podoplanin) molecules expressed in Chinese hamster ovary
cells.";
J. Biol. Chem. 279:38838-38843(2004).
[12]
FUNCTION, AND INTERACTION WITH CLEC1B.
PubMed=17616532; DOI=10.1074/jbc.M702327200;
Suzuki-Inoue K., Kato Y., Inoue O., Kaneko M.K., Mishima K.,
Yatomi Y., Yamazaki Y., Narimatsu H., Ozaki Y.;
"Involvement of the snake toxin receptor CLEC-2, in podoplanin-
mediated platelet activation, by cancer cells.";
J. Biol. Chem. 282:25993-26001(2007).
[13]
DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=20110424; DOI=10.1182/blood-2009-04-216069;
Uhrin P., Zaujec J., Breuss J.M., Olcaydu D., Chrenek P.,
Stockinger H., Fuertbauer E., Moser M., Haiko P., Faessler R.,
Alitalo K., Binder B.R., Kerjaschki D.;
"Novel function for blood platelets and podoplanin in developmental
separation of blood and lymphatic circulation.";
Blood 115:3997-4005(2010).
[14]
INDUCTION.
PubMed=20962267; DOI=10.1091/mbc.E10-06-0489;
Martin-Villar E., Fernandez-Munoz B., Parsons M., Yurrita M.M.,
Megias D., Perez-Gomez E., Jones G.E., Quintanilla M.;
"Podoplanin associates with CD44 to promote directional cell
migration.";
Mol. Biol. Cell 21:4387-4399(2010).
[15]
PHOSPHORYLATION, AND MUTAGENESIS OF SER-167 AND SER-171.
PubMed=23530051; DOI=10.1074/jbc.C112.446823;
Krishnan H., Ochoa-Alvarez J.A., Shen Y., Nevel E.,
Lakshminarayanan M., Williams M.C., Ramirez M.I., Miller W.T.,
Goldberg G.S.;
"Serines in the intracellular tail of podoplanin (PDPN) regulate cell
motility.";
J. Biol. Chem. 288:12215-12221(2013).
[16]
FUNCTION, AND DOMAIN.
PubMed=25347465; DOI=10.1038/ni.3035;
Astarita J.L., Cremasco V., Fu J., Darnell M.C., Peck J.R.,
Nieves-Bonilla J.M., Song K., Kondo Y., Woodruff M.C., Gogineni A.,
Onder L., Ludewig B., Weimer R.M., Carroll M.C., Mooney D.J., Xia L.,
Turley S.J.;
"The CLEC-2-podoplanin axis controls the contractility of fibroblastic
reticular cells and lymph node microarchitecture.";
Nat. Immunol. 16:75-84(2015).
[17]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 76-84 IN COMPLEX WITH
IMMUNOGLOBULIN.
PubMed=20479270; DOI=10.1073/pnas.0915176107;
Brooks C.L., Schietinger A., Borisova S.N., Kufer P., Okon M.,
Hirama T., Mackenzie C.R., Wang L.X., Schreiber H., Evans S.V.;
"Antibody recognition of a unique tumor-specific glycopeptide
antigen.";
Proc. Natl. Acad. Sci. U.S.A. 107:10056-10061(2010).
-!- 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:20110424, PubMed:17616532). 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 to 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}.
-!- SUBUNIT: Homodimer. Interacts with CLEC1B; the interaction is
independent of CLEC1B glycosylation and activates CLEC1B; the
interaction is dependent of sialic acid on O-glycans
(PubMed:17616532). 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).
{ECO:0000250|UniProtKB:Q86YL7, ECO:0000269|PubMed:17616532}.
-!- 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}.
-!- TISSUE SPECIFICITY: Detected at high levels in lung and brain, at
lower levels in kidney, stomach, liver, spleen and esophagus, and
not detected in skin and small intestine. Expressed in epithelial
cells of choroid plexus, ependyma, glomerulus and alveolus, in
mesothelial cells and in endothelia of lymphatic vessels. Also
expressed in stromal cells of peripheral lymphoid tissue and
thymic epithelial cells. Detected in carcinoma cell lines and
cultured fibroblasts. Expressed at higher levels in colon
carcinomas than in normal colon tissue.
{ECO:0000269|PubMed:10574709, ECO:0000269|PubMed:12032185,
ECO:0000269|PubMed:14522983}.
-!- DEVELOPMENTAL STAGE: At E12.5 and E13.5 is expressed in the
endothelial cells of forming lymph sacs.
{ECO:0000269|PubMed:20110424}.
-!- INDUCTION: Down-regulated by treatment with puromycin
aminonucleoside (PubMed:12032185). Up-regulated during progression
to highly aggressive tumors and during epithelial-mesenchymal
transition (EMT) (PubMed:20962267). {ECO:0000269|PubMed:12032185,
ECO:0000269|PubMed:20962267}.
-!- DOMAIN: The cytoplasmic domain controls FRC elongation but is
dispensable for contraction (PubMed:25347465). The cytoplasmic
domain is essential for recruitment to invadopodia and ECM
degradation (By similarity). {ECO:0000250|UniProtKB:Q86YL7,
ECO:0000269|PubMed:25347465}.
-!- 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}.
-!- DISRUPTION PHENOTYPE: Mice die at birth of respiratory failure due
to a low number of attenuated type I cells, narrow and irregular
air spaces, and defective formation of alveolar saccules
(PubMed:12654292). Knockout Pdpn mice neonates are smaller, and
approximately 55% died during the first postnatal week. However,
approximately 20% survived, had normal weights and life spans, and
are fertile (PubMed:20110424). {ECO:0000269|PubMed:12654292,
ECO:0000269|PubMed:20110424}.
-!- SIMILARITY: Belongs to the podoplanin family. {ECO:0000305}.
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EMBL; M73748; AAA39866.1; -; mRNA.
EMBL; M96645; AAA37724.1; -; mRNA.
EMBL; AJ250246; CAB58997.1; -; mRNA.
EMBL; AJ297944; CAC16152.1; -; mRNA.
EMBL; AY115493; AAM66761.1; -; Genomic_DNA.
EMBL; AK158855; BAE34695.1; -; mRNA.
EMBL; AL611982; CAM21724.1; -; Genomic_DNA.
EMBL; BC026551; AAH26551.1; -; mRNA.
CCDS; CCDS38943.1; -.
PIR; A54560; A54560.
RefSeq; NP_001277751.1; NM_001290822.1.
RefSeq; NP_034459.2; NM_010329.3.
UniGene; Mm.2976; -.
PDB; 3IET; X-ray; 2.20 A; Q/X=76-84.
PDBsum; 3IET; -.
IntAct; Q62011; 1.
STRING; 10090.ENSMUSP00000030317; -.
iPTMnet; Q62011; -.
PhosphoSitePlus; Q62011; -.
MaxQB; Q62011; -.
PaxDb; Q62011; -.
PRIDE; Q62011; -.
Ensembl; ENSMUST00000030317; ENSMUSP00000030317; ENSMUSG00000028583.
Ensembl; ENSMUST00000181754; ENSMUSP00000137969; ENSMUSG00000096951.
GeneID; 14726; -.
KEGG; mmu:14726; -.
UCSC; uc008vqa.2; mouse.
CTD; 10630; -.
MGI; MGI:103098; Pdpn.
eggNOG; ENOG410J49G; Eukaryota.
eggNOG; ENOG41116TP; LUCA.
GeneTree; ENSGT00390000000013; -.
HOGENOM; HOG000231122; -.
HOVERGEN; HBG080131; -.
InParanoid; Q62011; -.
KO; K16778; -.
OMA; ETTGMEG; -.
OrthoDB; EOG091G0ZYJ; -.
PhylomeDB; Q62011; -.
TreeFam; TF337068; -.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
ChiTaRS; Pdpn; mouse.
PRO; PR:Q62011; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028583; -.
CleanEx; MM_PDPN; -.
ExpressionAtlas; Q62011; baseline and differential.
Genevisible; Q62011; MM.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0042995; C:cell projection; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0030175; C:filopodium; IDA:UniProtKB.
GO; GO:0031527; C:filopodium membrane; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0071437; C:invadopodium; ISS:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0031258; C:lamellipodium membrane; ISS:UniProtKB.
GO; GO:0061851; C:leading edge of lamellipodium; ISS:UniProtKB.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0031528; C:microvillus membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
GO; GO:0097197; C:tetraspanin-enriched microdomain; ISS:UniProtKB.
GO; GO:0051087; F:chaperone binding; ISO:MGI.
GO; GO:0019956; F:chemokine binding; ISO:MGI.
GO; GO:0005102; F:receptor binding; ISS:UniProtKB.
GO; GO:0070252; P:actin-mediated cell contraction; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; ISO:MGI.
GO; GO:0000902; P:cell morphogenesis; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; IMP:MGI.
GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
GO; GO:1905863; P:invadopodium organization; ISS:UniProtKB.
GO; GO:0048286; P:lung alveolus development; IMP:MGI.
GO; GO:0030324; P:lung development; IMP:MGI.
GO; GO:0048535; P:lymph node development; IMP:UniProtKB.
GO; GO:0001946; P:lymphangiogenesis; IMP:MGI.
GO; GO:0060838; P:lymphatic endothelial cell fate commitment; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0051272; P:positive regulation of cellular component movement; IDA:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; ISS:UniProtKB.
GO; GO:1901731; P:positive regulation of platelet aggregation; IDA:UniProtKB.
GO; GO:0006693; P:prostaglandin metabolic process; IMP:MGI.
GO; GO:0030155; P:regulation of cell adhesion; IMP:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IMP:MGI.
GO; GO:2000392; P:regulation of lamellipodium morphogenesis; ISS:UniProtKB.
GO; GO:1904328; P:regulation of myofibroblast contraction; IMP:UniProtKB.
GO; GO:1900024; P:regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
GO; GO:0007266; P:Rho protein signal transduction; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; IMP:MGI.
GO; GO:0035239; P:tube morphogenesis; ISO:MGI.
GO; GO:0061032; P:visceral serous pericardium development; TAS:DFLAT.
GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB.
InterPro; IPR008783; Podoplanin.
Pfam; PF05808; Podoplanin; 1.
1: Evidence at protein level;
3D-structure; Cell junction; Cell membrane; Cell projection;
Cell shape; Complete proteome; Developmental protein;
Direct protein sequencing; Glycoprotein; Membrane; Reference proteome;
Sialic acid; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 22 {ECO:0000250|UniProtKB:Q86YL7}.
CHAIN 23 172 Podoplanin.
/FTId=PRO_0000021352.
TOPO_DOM 23 141 Extracellular. {ECO:0000255}.
TRANSMEM 142 162 Helical. {ECO:0000255}.
TOPO_DOM 163 172 Cytoplasmic.
REGION 143 147 Requires for dimerization and lipidd
rafts association.
{ECO:0000250|UniProtKB:Q86YL7}.
REGION 164 165 Requires for interaction with MSN and
EZR. {ECO:0000250|UniProtKB:Q86YL7}.
CARBOHYD 37 37 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 51 51 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 52 52 O-linked (GalNAc...) threonine.
{ECO:0000250|UniProtKB:Q86YL7}.
CARBOHYD 53 53 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 56 56 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 60 60 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 63 63 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 71 71 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 77 77 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 85 85 O-linked (GalNAc...) serine.
{ECO:0000255}.
CARBOHYD 86 86 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 87 87 O-linked (GalNAc...) serine.
{ECO:0000255}.
CARBOHYD 89 89 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 90 90 O-linked (GalNAc...) serine.
{ECO:0000255}.
CARBOHYD 100 100 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 101 101 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 102 102 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 107 107 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 115 115 O-linked (GalNAc...) threonine.
{ECO:0000255}.
MUTAGEN 34 34 T->A: Eliminates platelet aggregation
activity. {ECO:0000269|PubMed:14522983}.
MUTAGEN 167 167 S->A: 50% decrease of cell growth; when
associated with A-171. 50% increase of
cell migration; when associated with A-
171. {ECO:0000269|PubMed:23530051}.
MUTAGEN 167 167 S->D: Does not significantly increase
cell motility; when associated with D-
171. Does not significantly decrease cell
growth; when associated with A-171.
{ECO:0000269|PubMed:23530051}.
MUTAGEN 171 171 S->A: 50% decrease of cell growth; when
associated with A-167. 50% increase of
cell migration; when associated with A-
167. {ECO:0000269|PubMed:23530051}.
MUTAGEN 171 171 S->D: Does not significantly increase
cell motility; when associated with D-
171. Does not significantly decrease cell
growth; when associated with A-171.
{ECO:0000269|PubMed:23530051}.
CONFLICT 29 31 EDD -> KNN (in Ref. 2; AAA37724).
{ECO:0000305}.
CONFLICT 38 39 GD -> EN (in Ref. 2; AAA37724).
{ECO:0000305}.
CONFLICT 170 172 FSP -> SRPKELNRTGCSPNTSENKRASNLPCSPSSSCGG
R (in Ref. 1; AAA39866). {ECO:0000305}.
HELIX 81 83 {ECO:0000244|PDB:3IET}.
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


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