Q62011 (PDPN_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 89.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Podoplanin Alternative name(s): Aggrus Glycoprotein 38 Short name=Gp38 OTS-8 PA2.26 antigen T1-alpha Short name=T1A Transmembrane glycoprotein E11 | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 172 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | May be involved in cell migration and/or actin cytoskeleton organization. When expressed in keratinocytes, induces changes in cell morphology with transfected cells showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion. Required for normal lung cell proliferation and alveolus formation at birth. Induces platelet aggregation. Does not have any effect on folic acid or amino acid transport. Does not function as a water channel or as a regulator of aquaporin-type water channels. Ref.3 Ref.4 Ref.9 Ref.10 Ref.11 |
| Subcellular location | Membrane; Single-pass type I membrane protein. Cell projection › lamellipodium membrane; Single-pass type I membrane protein. Cell projection › filopodium membrane; Single-pass type I membrane protein. Cell projection › microvillus membrane; Single-pass type I membrane protein. Cell projection › ruffle membrane; Single-pass type I membrane protein. Note: Localized to actin-rich microvilli and plasma membrane projections such as filopodia, lamellipodia and ruffles. Ref.3 |
| 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. Ref.3 Ref.4 Ref.10 |
| Induction | Down-regulated by treatment with puromycin aminonucleoside. Ref.4 |
| Post-translational modification | Extensively O-glycosylated. Contains sialic acid residues. O-glycosylation is necessary for platelet aggregation activity. Ref.3 Ref.11 The N-terminus is blocked By similarity. |
| 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. Ref.9 |
| Sequence similarities | Belongs to the podoplanin family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | Potential | ||||||
| Chain | 23 – 172 | 150 | Podoplanin | PRO_0000021352 | |||||
Regions | |||||||||
| Topological domain | 23 – 141 | 119 | Extracellular Potential | ||||||
| Transmembrane | 142 – 162 | 21 | Helical; Potential | ||||||
| Topological domain | 163 – 172 | 10 | Cytoplasmic | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 37 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 51 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 52 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 53 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 56 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 60 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 63 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 71 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 77 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 85 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 86 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 87 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 89 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 90 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 100 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 101 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 102 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 107 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 115 | 1 | O-linked (GalNAc...) Potential | ||||||
Experimental info | |||||||||
| Mutagenesis | 34 | 1 | T → A: Eliminates platelet aggregation activity. Ref.10 | ||||||
| Sequence conflict | 29 – 31 | 3 | EDD → KNN in AAA37724. Ref.2 | ||||||
| Sequence conflict | 38 – 39 | 2 | GD → EN in AAA37724. Ref.2 | ||||||
| Sequence conflict | 170 – 172 | 3 | FSP → SRPKELNRTGCSPNTSENKR ASNLPCSPSSSCGGR in AAA39866. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "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." Nose K., Saito H., Kuroki T. Cell Growth Differ. 1:511-518(1990) [PubMed: 2088477] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Characterization and cloning of a novel glycoprotein expressed by stromal cells in T-dependent areas of peripheral lymphoid tissues." Farr A.G., Berry M.L., Kim A., Nelson A.J., Welch M.P., Aruffo A. J. Exp. Med. 176:1477-1482(1992) [PubMed: 1402691] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. |
| [3] | "Identification of PA2.26 antigen as a novel cell-surface mucin-type glycoprotein that induces plasma membrane extensions and increased motility in keratinocytes." Scholl F.G., Gamallo C., Vilaro S., Quintanilla M. J. Cell Sci. 112:4601-4613(1999) [PubMed: 10574709] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-30 AND 66-73, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION. |
| [4] | "Cloning and expression of the mouse glomerular podoplanin homologue gp38P." Boucherot A., Schreiber R., Pavenstaedt H., Kunzelmann K. Nephrol. Dial. Transplant. 17:978-984(2002) [PubMed: 12032185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION. Tissue: Kidney. |
| [5] | "Cloning and characterization studies of mouse E11 gene and its spatial and temporal expression pattern during development." Lu Y., Zhang J., Harris M.A., Harris S.E., Bonewald L., Feng J. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/Sv. |
| [6] | "The transcriptional landscape of the mammalian genome." 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. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Visual cortex. |
| [7] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." 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. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6. |
| [8] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Colon. |
| [9] | "T1alpha, a lung type I cell differentiation gene, is required for normal lung cell proliferation and alveolus formation at birth." Ramirez M.I., Millien G., Hinds A., Cao Y., Seldin D.C., Williams M.C. Dev. Biol. 256:61-72(2003) [PubMed: 12654292] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE. |
| [10] | "Molecular identification of aggrus/T1alpha as a platelet aggregation-inducing factor expressed in colorectal tumors." Kato Y., Fujita N., Kunita A., Sato S., Kaneko M., Osawa M., Tsuruo T. J. Biol. Chem. 278:51599-51605(2003) [PubMed: 14522983] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF THR-34. |
| [11] | "Functional sialylated O-glycan to platelet aggregation on Aggrus (T1alpha/Podoplanin) molecules expressed in Chinese hamster ovary cells." Kaneko M., Kato Y., Kunita A., Fujita N., Tsuruo T., Osawa M. J. Biol. Chem. 279:38838-38843(2004) [PubMed: 15231832] [Abstract] Cited for: FUNCTION, GLYCOSYLATION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M73748 mRNA. Translation: AAA39866.1. M96645 mRNA. Translation: AAA37724.1. AJ250246 mRNA. Translation: CAB58997.1. AJ297944 mRNA. Translation: CAC16152.1. AY115493 Genomic DNA. Translation: AAM66761.1. AK158855 mRNA. Translation: BAE34695.1. AL611982 Genomic DNA. Translation: CAM21724.1. BC026551 mRNA. Translation: AAH26551.1. | ||||||||||||
| IPI | IPI00230205. | ||||||||||||
| PIR | A54560. | ||||||||||||
| RefSeq | NP_034459.2. NM_010329.2. | ||||||||||||
| UniGene | Mm.2976. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | Q62011. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | Q62011. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSMUST00000030317; ENSMUSP00000030317; ENSMUSG00000028583. | ||||||||||||
| GeneID | 14726. | ||||||||||||
| KEGG | mmu:14726. | ||||||||||||
| UCSC | uc008vqa.1. mouse. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 10630. | ||||||||||||
| MGI | MGI:103098. Pdpn. | ||||||||||||
Phylogenomic databases | |||||||||||||
| GeneTree | ENSGT00390000000013. | ||||||||||||
| HOGENOM | HBG283047. | ||||||||||||
| HOVERGEN | HBG080131. | ||||||||||||
| InParanoid | Q62011. | ||||||||||||
| OMA | VDGDTQT. | ||||||||||||
| OrthoDB | EOG47PX73. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q62011. | ||||||||||||
| Bgee | Q62011. | ||||||||||||
| CleanEx | MM_PDPN. | ||||||||||||
| Genevestigator | Q62011. | ||||||||||||
| GermOnline | ENSMUSG00000028583. Mus musculus. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR008783. Podoplanin. [Graphical view] | ||||||||||||
| PANTHER | PTHR16861. Podoplanin. 1 hit. | ||||||||||||
| Pfam | PF05808. Podoplanin. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| NextBio | 286753. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | PDPN_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q62011 Secondary accession number(s): A2A8J3, Q546R8, Q61612 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with