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Q9R0M4 (PODXL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Podocalyxin
Alternative name(s):
Podocalyxin-like protein 1
Short name=PC
Short name=PCLP-1
Gene names
Name:Podxl
Synonyms:Pclp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the regulation of both adhesion and cell morphology and cancer progression. Function as an anti-adhesive molecule that maintains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Acts as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner. Induces the formation of apical actin-dependent microvilli. Involved in the formation of a preapical plasma membrane subdomain to set up inital epithelial polarization and the apical lumen formation during renal tubulogenesis. Plays a role in cancer development and aggressiveness by inducing cell migration and invasion through its interaction with the actin-binding protein EZR. Affects EZR-dependent signaling events, leading to increased activities of the MAPK and PI3K pathways in cancer cells. Ref.4 Ref.5

Subunit structure

Monomer; when associated with the membrane raft. Oligomer; when integrated in the apical membrane. Found in a complex with EZR, PODXL and SLC9A3R2. Associates with the actin cytoskeleton through complex formation with EZR and SLC9A3R2. Interacts (via the C-terminal PDZ-binding motif DTHL) with SLC9A3R1 (via the PDZ domains); interaction is not detected in glomerular epithelium cells, take place early in the secretory pathway and is necessary for its apical membrane sorting. Interacts (via the C-terminal PDZ-binding motif DTHL) with SLC9A3R2 (via the PDZ 1 domain); interaction is detected in glomerular epithelium cells. Interacts with EZR By similarity.

Subcellular location

Apical cell membrane. Cell projectionmicrovillus. Membrane raft By similarity. Cell projectionlamellipodium By similarity. Cell projectionfilopodium By similarity. Cell projectionruffle By similarity. Membrane; Single-pass type I membrane protein Potential. Note: In single attached epithelial cells is restricted to a preapical pole on the free plasma membrane whereas other apical and basolateral proteins are not yet polarized. Colocalizes with SLC9A3R2 at the apical plasma membrane during epithelial polarization. Colocalizes with SLC9A3R1 at the trans-Golgi network (transiently) and at the apical plasma membrane. Its association with the membrane raft is transient. Forms granular, punctuated pattern, forming patches, preferentially adopting a polar distribution, located on the migrating poles of the cell or forming clusters along the terminal ends of filipodia establishing contact with the endothelial cells. Colocalizes with the submembrane actin of lamellipodia, particularly associated with ruffles. Colocalizes with vinculin at protrusions of cells. Colocalizes with ITGB1. Colocalizes with EZR and SLC9A3R2 at the apical cell membrane of glomerular epithelium cells By similarity. Colocalizes with actin filaments, EZR and SLC9A3R1 in a punctate pattern at the apical cell surface where microvilli form. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, RAB11A and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and luminogenesis By similarity. Ref.5

Tissue specificity

Expressed in liver cells and hematopoietic cells (at protein level). Glomerular epithelium cell (podocyte). Ref.4

Domain

Both the O-glycan-rich domain of the extracellular domain and the C-terminus PDZ-binding motif (DTHL) in the cytoplasmic tail harbor an apical sorting signal. The cytoplasmic domain is necessary for the apical membrane targeting and renal tubulogenesis. The large highly anionic extracellular domain allows to maintain open filtration pathways between neighboring podocyte foot processes. The cytoplasmic C-terminus PDZ-binding motif (DTHL) is essential for interaction with SLC9A3R1 and for targeting SLC9A3R1 to the apical cell membrane. The extracellular domain is necessary for microvillus formation By similarity.

Post-translational modification

N- and O-linked glycosylated. Sialoglycoprotein By similarity.

Disruption phenotype

Die within the first 24 h of postnatal life from profound defects in kidney and/or gut formation. They are anuric (no measurable urine in the bladder), and fail to generate the extensive interdigitated foot process and instead retain cell junctions between immature podocytes. Ref.4

Sequence similarities

Belongs to the podocalyxin family.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Cell projection
Membrane
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Inferred from mutant phenotype PubMed 20395446. Source: UniProtKB

epithelial tube formation

Inferred from sequence or structural similarity. Source: UniProtKB

glomerular visceral epithelial cell development

Inferred from sequence or structural similarity. Source: UniProtKB

leukocyte migration

Inferred from mutant phenotype PubMed 15701716. Source: MGI

negative regulation of cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell-cell adhesion

Inferred from mutant phenotype PubMed 20395446. Source: UniProtKB

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell-cell adhesion mediated by integrin

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of microvillus assembly

Inferred from direct assay Ref.5. Source: UniProtKB

   Cellular_componentapical plasma membrane

Inferred from direct assay Ref.5. Source: UniProtKB

cell body

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

filopodium

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

membrane raft

Inferred from electronic annotation. Source: UniProtKB-SubCell

microvillus membrane

Inferred from direct assay Ref.5. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

ruffle

Inferred from sequence or structural similarity. Source: UniProtKB

slit diaphragm

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 503482Podocalyxin
PRO_0000024755

Regions

Topological domain22 – 404383Extracellular Potential
Transmembrane405 – 42521Helical; Potential
Topological domain426 – 50378Cytoplasmic Potential
Compositional bias27 – 259233Ser/Thr-rich

Amino acid modifications

Modified residue4821Phosphoserine By similarity
Modified residue5011Phosphothreonine By similarity
Glycosylation251N-linked (GlcNAc...) Potential
Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation1451N-linked (GlcNAc...) Potential
Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation1671N-linked (GlcNAc...) Potential
Glycosylation2061N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Potential

Natural variations

Natural variant781S → F.

Sequences

Sequence LengthMass (Da)Tools
Q9R0M4 [UniParc].

Last modified November 16, 2001. Version 2.
Checksum: 786A1ECF65484D1F

FASTA50353,389
        10         20         30         40         50         60 
MPPTTALSAL LLLLLSPASH SHNGNETSTS AIKSSTVQSH QSATTSTEVT TGHPVASTLA 

        70         80         90        100        110        120 
STQPSNPTPF TTSTQSPSMP TSTPNPTSNQ SGGNLTSSVS EVDKTKTSSP SSTAFTSSSG 

       130        140        150        160        170        180 
QTASSGGKSG DSFTTAPTTT LGLINVSSQP TDLNTTSKLL STPTTDNTTS PQQPVDSSPS 

       190        200        210        220        230        240 
TASHPVGQHT PAAVPSSSGS TPSTDNSTLT WKPTTHKPLG TSEATQPLTS QTPGITTLPV 

       250        260        270        280        290        300 
STLQQSMAST VGTTTEEFTH LISNGTPVAP PGPSTPSPIW AFGNYQLNCE PPIRPDEELL 

       310        320        330        340        350        360 
ILNLTRASLC ERSPLDEKEK LVELLCHSVK ASFKPAEDLC TLHVAPILDN QAVAVKRIII 

       370        380        390        400        410        420 
ETKLSPKAVY ELLKDRWDDL TEAGVSDMKL GKEGPPEVNE DRFSLPLIIT IVCMASFLLL 

       430        440        450        460        470        480 
VAALYGCCHQ RISQRKDQQR LTEELQTVEN GYHDNPTLEV METPSEMQEK KVVNLNGELG 

       490        500 
DSWIVPLDNL TKDDLDEEED THL 

« Hide

References

« Hide 'large scale' references
[1]"Identification of podocalyxin-like protein 1 as a novel cell surface marker for hemangioblasts in the murine aorta-gonad-mesonephros region."
Hara T., Nakano Y., Tanaka M., Tamura K., Sekiguchi T., Minehata K., Copeland N.G., Jenkins N.A., Okabe M., Kogo H., Mukouyama Y., Miyajima A.
Immunity 11:567-578(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Gene structure of mouse podocalyxin."
Kershaw D.B., Li J.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[4]"Anuria, omphalocele, and perinatal lethality in mice lacking the CD34-related protein podocalyxin."
Doyonnas R., Kershaw D.B., Duhme C., Merkens H., Chelliah S., Graf T., McNagny K.M.
J. Exp. Med. 194:13-27(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[5]"The CD34-related molecule podocalyxin is a potent inducer of microvillus formation."
Nielsen J.S., Graves M.L., Chelliah S., Vogl A.W., Roskelley C.D., McNagny K.M.
PLoS ONE 2:E237-E237(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB028048 mRNA. Translation: BAA86912.1.
AF290209 mRNA. Translation: AAG02458.1.
BC052442 mRNA. Translation: AAH52442.1.
BC054530 mRNA. Translation: AAH54530.1.
CCDSCCDS19983.1.
RefSeqNP_038751.2. NM_013723.3.
UniGeneMm.89918.

3D structure databases

ProteinModelPortalQ9R0M4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9R0M4. 3 interactions.
MINTMINT-4108172.
STRING10090.ENSMUSP00000026698.

PTM databases

PhosphoSiteQ9R0M4.

Proteomic databases

MaxQBQ9R0M4.
PaxDbQ9R0M4.
PRIDEQ9R0M4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026698; ENSMUSP00000026698; ENSMUSG00000025608.
GeneID27205.
KEGGmmu:27205.
UCSCuc009bgh.2. mouse.

Organism-specific databases

CTD5420.
MGIMGI:1351317. Podxl.

Phylogenomic databases

eggNOGNOG47672.
GeneTreeENSGT00730000111314.
HOGENOMHOG000115601.
HOVERGENHBG053629.
InParanoidQ9R0M4.
KOK06817.
OMARASLCER.
OrthoDBEOG7CVQ0P.
PhylomeDBQ9R0M4.
TreeFamTF333564.

Gene expression databases

ArrayExpressQ9R0M4.
BgeeQ9R0M4.
CleanExMM_PODXL.
GenevestigatorQ9R0M4.

Family and domain databases

InterProIPR013836. CD34/Podocalyxin.
IPR017403. Podocalyxin-like_p1.
[Graphical view]
PfamPF06365. CD34_antigen. 1 hit.
[Graphical view]
PIRSFPIRSF038143. Podocalyxin-like_p1. 1 hit.
ProtoNetSearch...

Other

NextBio305071.
PROQ9R0M4.
SOURCESearch...

Entry information

Entry namePODXL_MOUSE
AccessionPrimary (citable) accession number: Q9R0M4
Secondary accession number(s): Q9ESZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 16, 2001
Last modified: July 9, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot