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Q9R0M4

- PODXL_MOUSE

UniProt

Q9R0M4 - PODXL_MOUSE

Protein

Podocalyxin

Gene

Podxl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (16 Nov 2001)
      Previous versions | rss
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    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

    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

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB
    2. cell body Source: Ensembl
    3. cytoplasm Source: UniProtKB
    4. filopodium Source: UniProtKB
    5. integral component of membrane Source: UniProtKB-KW
    6. lamellipodium Source: UniProtKB
    7. membrane raft Source: UniProtKB-SubCell
    8. microvillus membrane Source: UniProtKB
    9. plasma membrane Source: UniProtKB
    10. ruffle Source: UniProtKB
    11. slit diaphragm Source: UniProtKB

    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

    ArrayExpressiQ9R0M4.
    BgeeiQ9R0M4.
    CleanExiMM_PODXL.
    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...

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei405 – 42521HelicalSequence AnalysisAdd
    BLAST

    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

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    MPPTTALSAL LLLLLSPASH SHNGNETSTS AIKSSTVQSH QSATTSTEVT    50
    TGHPVASTLA STQPSNPTPF TTSTQSPSMP TSTPNPTSNQ SGGNLTSSVS 100
    EVDKTKTSSP SSTAFTSSSG QTASSGGKSG DSFTTAPTTT LGLINVSSQP 150
    TDLNTTSKLL STPTTDNTTS PQQPVDSSPS TASHPVGQHT PAAVPSSSGS 200
    TPSTDNSTLT WKPTTHKPLG TSEATQPLTS QTPGITTLPV STLQQSMAST 250
    VGTTTEEFTH LISNGTPVAP PGPSTPSPIW AFGNYQLNCE PPIRPDEELL 300
    ILNLTRASLC ERSPLDEKEK LVELLCHSVK ASFKPAEDLC TLHVAPILDN 350
    QAVAVKRIII ETKLSPKAVY ELLKDRWDDL TEAGVSDMKL GKEGPPEVNE 400
    DRFSLPLIIT IVCMASFLLL VAALYGCCHQ RISQRKDQQR LTEELQTVEN 450
    GYHDNPTLEV METPSEMQEK KVVNLNGELG DSWIVPLDNL TKDDLDEEED 500
    THL 503
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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

    ArrayExpressi Q9R0M4.
    Bgeei Q9R0M4.
    CleanExi MM_PODXL.
    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

    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 1, 2014
    This is version 92 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