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Q9R0M4

- PODXL_MOUSE

UniProt

Q9R0M4 - PODXL_MOUSE

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Protein

Podocalyxin

Gene

Podxl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. cell migration Source: UniProtKB
  3. epithelial tube formation Source: UniProtKB
  4. glomerular visceral epithelial cell development Source: UniProtKB
  5. leukocyte migration Source: MGI
  6. negative regulation of cell adhesion Source: UniProtKB
  7. negative regulation of cell-cell adhesion Source: UniProtKB
  8. positive regulation of cell-cell adhesion mediated by integrin Source: UniProtKB
  9. positive regulation of cell migration Source: UniProtKB
  10. regulation of microvillus assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Podocalyxin
Alternative name(s):
Podocalyxin-like protein 1
Short name:
PC
Short name:
PCLP-1
Gene namesi
Name:Podxl
Synonyms:Pclp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1351317. Podxl.

Subcellular locationi

Apical cell membrane 1 Publication. Cell projectionmicrovillus 1 Publication. Membrane raft By similarity. Cell projectionlamellipodium By similarity. Cell projectionfilopodium By similarity. Cell projectionruffle By similarity. Membrane Curated; Single-pass type I membrane protein Curated
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).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 404383ExtracellularSequence AnalysisAdd
BLAST
Transmembranei405 – 42521HelicalSequence AnalysisAdd
BLAST
Topological domaini426 – 50378CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. cell body Source: Ensembl
  3. cytoplasm Source: UniProtKB
  4. extracellular space Source: Ensembl
  5. extracellular vesicular exosome Source: Ensembl
  6. filopodium Source: UniProtKB
  7. integral component of membrane Source: UniProtKB-KW
  8. lamellipodium Source: UniProtKB
  9. microvillus membrane Source: UniProtKB
  10. plasma membrane Source: UniProtKB
  11. ruffle Source: UniProtKB
  12. slit diaphragm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 503482PodocalyxinPRO_0000024755Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi25 – 251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi167 – 1671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
Modified residuei482 – 4821PhosphoserineBy similarity
Modified residuei501 – 5011PhosphothreonineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9R0M4.
PaxDbiQ9R0M4.
PRIDEiQ9R0M4.

PTM databases

PhosphoSiteiQ9R0M4.

Expressioni

Tissue specificityi

Expressed in liver cells and hematopoietic cells (at protein level). Glomerular epithelium cell (podocyte).1 Publication

Gene expression databases

BgeeiQ9R0M4.
CleanExiMM_PODXL.
ExpressionAtlasiQ9R0M4. baseline and differential.
GenevestigatoriQ9R0M4.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

IntActiQ9R0M4. 3 interactions.
MINTiMINT-4108172.
STRINGi10090.ENSMUSP00000026698.

Structurei

3D structure databases

ProteinModelPortaliQ9R0M4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi27 – 259233Ser/Thr-richAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the podocalyxin family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG47672.
GeneTreeiENSGT00730000111314.
HOGENOMiHOG000115601.
HOVERGENiHBG053629.
InParanoidiQ9R0M4.
KOiK06817.
OMAiRASLCER.
OrthoDBiEOG7CVQ0P.
PhylomeDBiQ9R0M4.
TreeFamiTF333564.

Family and domain databases

InterProiIPR013836. CD34/Podocalyxin.
IPR017403. Podocalyxin-like_p1.
[Graphical view]
PfamiPF06365. CD34_antigen. 1 hit.
[Graphical view]
PIRSFiPIRSF038143. Podocalyxin-like_p1. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R0M4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPPTTALSAL LLLLLSPASH SHNGNETSTS AIKSSTVQSH QSATTSTEVT
60 70 80 90 100
TGHPVASTLA STQPSNPTPF TTSTQSPSMP TSTPNPTSNQ SGGNLTSSVS
110 120 130 140 150
EVDKTKTSSP SSTAFTSSSG QTASSGGKSG DSFTTAPTTT LGLINVSSQP
160 170 180 190 200
TDLNTTSKLL STPTTDNTTS PQQPVDSSPS TASHPVGQHT PAAVPSSSGS
210 220 230 240 250
TPSTDNSTLT WKPTTHKPLG TSEATQPLTS QTPGITTLPV STLQQSMAST
260 270 280 290 300
VGTTTEEFTH LISNGTPVAP PGPSTPSPIW AFGNYQLNCE PPIRPDEELL
310 320 330 340 350
ILNLTRASLC ERSPLDEKEK LVELLCHSVK ASFKPAEDLC TLHVAPILDN
360 370 380 390 400
QAVAVKRIII ETKLSPKAVY ELLKDRWDDL TEAGVSDMKL GKEGPPEVNE
410 420 430 440 450
DRFSLPLIIT IVCMASFLLL VAALYGCCHQ RISQRKDQQR LTEELQTVEN
460 470 480 490 500
GYHDNPTLEV METPSEMQEK KVVNLNGELG DSWIVPLDNL TKDDLDEEED

THL
Length:503
Mass (Da):53,389
Last modified:November 16, 2001 - v2
Checksum:i786A1ECF65484D1F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti78 – 781S → F.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028048 mRNA. Translation: BAA86912.1.
AF290209 mRNA. Translation: AAG02458.1.
BC052442 mRNA. Translation: AAH52442.1.
BC054530 mRNA. Translation: AAH54530.1.
CCDSiCCDS19983.1.
RefSeqiNP_038751.2. NM_013723.3.
UniGeneiMm.89918.

Genome annotation databases

EnsembliENSMUST00000026698; ENSMUSP00000026698; ENSMUSG00000025608.
GeneIDi27205.
KEGGimmu:27205.
UCSCiuc009bgh.2. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028048 mRNA. Translation: BAA86912.1 .
AF290209 mRNA. Translation: AAG02458.1 .
BC052442 mRNA. Translation: AAH52442.1 .
BC054530 mRNA. Translation: AAH54530.1 .
CCDSi CCDS19983.1.
RefSeqi NP_038751.2. NM_013723.3.
UniGenei Mm.89918.

3D structure databases

ProteinModelPortali Q9R0M4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9R0M4. 3 interactions.
MINTi MINT-4108172.
STRINGi 10090.ENSMUSP00000026698.

PTM databases

PhosphoSitei Q9R0M4.

Proteomic databases

MaxQBi Q9R0M4.
PaxDbi Q9R0M4.
PRIDEi Q9R0M4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000026698 ; ENSMUSP00000026698 ; ENSMUSG00000025608 .
GeneIDi 27205.
KEGGi mmu:27205.
UCSCi uc009bgh.2. mouse.

Organism-specific databases

CTDi 5420.
MGIi MGI:1351317. Podxl.

Phylogenomic databases

eggNOGi NOG47672.
GeneTreei ENSGT00730000111314.
HOGENOMi HOG000115601.
HOVERGENi HBG053629.
InParanoidi Q9R0M4.
KOi K06817.
OMAi RASLCER.
OrthoDBi EOG7CVQ0P.
PhylomeDBi Q9R0M4.
TreeFami TF333564.

Miscellaneous databases

NextBioi 305071.
PROi Q9R0M4.
SOURCEi Search...

Gene expression databases

Bgeei Q9R0M4.
CleanExi MM_PODXL.
ExpressionAtlasi Q9R0M4. baseline and differential.
Genevestigatori Q9R0M4.

Family and domain databases

InterProi IPR013836. CD34/Podocalyxin.
IPR017403. Podocalyxin-like_p1.
[Graphical view ]
Pfami PF06365. CD34_antigen. 1 hit.
[Graphical view ]
PIRSFi PIRSF038143. Podocalyxin-like_p1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiPODXL_MOUSE
AccessioniPrimary (citable) accession number: Q9R0M4
Secondary accession number(s): Q9ESZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 16, 2001
Last modified: October 29, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3