LOCUS       NP_062231                166 aa            linear   ROD 26-APR-2024
DEFINITION  podoplanin isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_062231
VERSION     NP_062231.2
DBSOURCE    REFSEQ: accession NM_019358.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Furusawa,Y., Yamada,S., Itai,S., Nakamura,T., Fukui,M., Harada,H.,
            Kaneko,M.K. and Kato,Y.
  TITLE     Elucidation of Critical Epitope of Anti-Rat Podoplanin Monoclonal
            Antibody PMab-2
  JOURNAL   Monoclon Antib Immunodiagn Immunother 37 (4), 188-193 (2018)
   PUBMED   30088964
  REMARK    GeneRIF: the binding epitope of PMab-2 remains to be determined.
            Herein, we investigated the epitope of PMab-2 using enzyme-linked
            immunosorbent assay, immunohistochemical analysis, and flow
            cytometry. The results revealed that the critical epitope of PMab-2
            is Leu46 and Glu47 of rPDPN.
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Zakhary,I., Alotibi,F., Lewis,J., ElSalanty,M., Wenger,K.,
            Sharawy,M. and Messer,R.L.
  TITLE     Inherent physical characteristics and gene expression differences
            between alveolar and basal bones
  JOURNAL   Oral Surg Oral Med Oral Pathol Oral Radiol 122 (1), 35-42 (2016)
   PUBMED   27039006
  REMARK    GeneRIF: Four genes are expressed significantly higher in basal
            bone than in alveolar bone: SOST, E-11, DMP-1, and MEPE. Three of
            the proteins (SOST, MEPE, and DMP-1) are associated with mature
            osteocytes, indicating that basal bone has more mature osteocyte
            phenotypes because the immature osteocyte converts to a mature
            osteocyte as a result of bone mineralization.
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Martin-Villar,E., Borda-d'Agua,B., Carrasco-Ramirez,P., Renart,J.,
            Parsons,M., Quintanilla,M. and Jones,G.E.
  TITLE     Podoplanin mediates ECM degradation by squamous carcinoma cells
            through control of invadopodia stability
  JOURNAL   Oncogene 34 (34), 4531-4544 (2015)
   PUBMED   25486435
REFERENCE   4  (residues 1 to 166)
  AUTHORS   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. and Turley,S.J.
  TITLE     The CLEC-2-podoplanin axis controls the contractility of
            fibroblastic reticular cells and lymph node microarchitecture
  JOURNAL   Nat Immunol 16 (1), 75-84 (2015)
   PUBMED   25347465
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Hirahara,I., Sato,H., Imai,T., Onishi,A., Morishita,Y., Muto,S.,
            Kusano,E. and Nagata,D.
  TITLE     Methylglyoxal Induced Basophilic Spindle Cells with Podoplanin at
            the Surface of Peritoneum in Rat Peritoneal Dialysis Model
  JOURNAL   Biomed Res Int 2015, 289751 (2015)
   PUBMED   26064894
  REMARK    GeneRIF: In rats treated with MGO, peritoneal fibrous thickening
            with the appearance of basophilic spindle cells with podoplanin,
            cytokeratin, and alpha-smooth muscle actin at the surface of the
            peritoneum was observed
REFERENCE   6  (residues 1 to 166)
  AUTHORS   Breiteneder-Geleff,S., Matsui,K., Soleiman,A., Meraner,P.,
            Poczewski,H., Kalt,R., Schaffner,G. and Kerjaschki,D.
  TITLE     Podoplanin, novel 43-kd membrane protein of glomerular epithelial
            cells, is down-regulated in puromycin nephrosis
  JOURNAL   Am J Pathol 151 (4), 1141-1152 (1997)
   PUBMED   9327748
REFERENCE   7  (residues 1 to 166)
  AUTHORS   Williams,M.C., Cao,Y., Hinds,A., Rishi,A.K. and Wetterwald,A.
  TITLE     T1 alpha protein is developmentally regulated and expressed by
            alveolar type I cells, choroid plexus, and ciliary epithelia of
            adult rats
  JOURNAL   Am J Respir Cell Mol Biol 14 (6), 577-585 (1996)
   PUBMED   8652186
REFERENCE   8  (residues 1 to 166)
  AUTHORS   Wetterwald,A., Hoffstetter,W., Cecchini,M.G., Lanske,B., Wagner,C.,
            Fleisch,H. and Atkinson,M.
  TITLE     Characterization and cloning of the E11 antigen, a marker expressed
            by rat osteoblasts and osteocytes
  JOURNAL   Bone 18 (2), 125-132 (1996)
   PUBMED   8833206
REFERENCE   9  (residues 1 to 166)
  AUTHORS   McElroy,M.C., Pittet,J.F., Hashimoto,S., Allen,L.,
            Wiener-Kronish,J.P. and Dobbs,L.G.
  TITLE     A type I cell-specific protein is a biochemical marker of
            epithelial injury in a rat model of pneumonia
  JOURNAL   Am J Physiol 268 (2 Pt 1), L181-L186 (1995)
   PUBMED   7864138
REFERENCE   10 (residues 1 to 166)
  AUTHORS   Rishi,A.K., Joyce-Brady,M., Fisher,J., Dobbs,L.G., Floros,J.,
            VanderSpek,J., Brody,J.S. and Williams,M.C.
  TITLE     Cloning, characterization, and development expression of a rat lung
            alveolar type I cell gene in embryonic endodermal and neural
            derivatives
  JOURNAL   Dev Biol 167 (1), 294-306 (1995)
   PUBMED   7851650
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Nov 26, 2020 this sequence version replaced NP_062231.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072492.1, U96449.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840115, SAMN16676784
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..166
                     /product="podoplanin isoform 1 precursor"
                     /note="glycoprotein 38; epithelial cell surface
                     transmembrane protein antigen; pulmonary type I alveolar
                     epithelial cell transmembrane differentiation marker; E11
                     antigen epitope; type I cell 40 kDa protein"
                     /calculated_mol_wt=15037
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2550
     mat_peptide     23..166
                     /product="Podoplanin. /id=PRO_0000021353"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64294.1)"
                     /calculated_mol_wt=15037
     Region          28..165
                     /region_name="Podoplanin"
                     /note="pfam05808"
                     /db_xref="CDD:461746"
     Site            34
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64294.1)"
     Site            52
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q86YL7; propagated from
                     UniProtKB/Swiss-Prot (Q64294.1)"
     Region          54..124
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64294.1)"
     Site            55
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64294.1)"
     Site            56
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64294.1)"
     Site            62
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q64294.1)"
     Site            63
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64294.1)"
     Site            71
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64294.1)"
     Site            80
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64294.1)"
     Site            81
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q64294.1)"
     Site            83
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64294.1)"
     Site            84
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q64294.1)"
     Site            94
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64294.1)"
     Site            95
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64294.1)"
     Site            96
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64294.1)"
     Site            101
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64294.1)"
     Site            105
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64294.1)"
     Site            109
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64294.1)"
     Site            110
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64294.1)"
     Site            136..156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64294.1)"
     Region          137..141
                     /region_name="Requires for dimerization and lipid rafts
                     association. /evidence=ECO:0000250|UniProtKB:Q86YL7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64294.1)"
     Region          158..159
                     /region_name="Requires for interaction with MSN and EZR.
                     /evidence=ECO:0000250|UniProtKB:Q86YL7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64294.1)"
     CDS             1..166
                     /gene="Pdpn"
                     /gene_synonym="E11; Gp38; OTS-8; RTI140; RTI40; T1-alpha;
                     T1A"
                     /coded_by="NM_019358.3:202..702"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:54320"
                     /db_xref="RGD:61819"
ORIGIN      
        1 mwtapvllwv lgsvwfwdsa qggaigaled dlvtpgpgdd mvnpgledri ettdttgeld
       61 kstakaplvp tqppieelpt sgtsdhdhke hestttvkav tshstdkktt hsnrdnagge
      121 tqttdkkdgl avvtlvgiii gvllaigfig giiivvmrki sgrfsp
//
