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Protein

Podocalyxin

Gene

PODXL

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: 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.

GO - Biological processi

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

  • Apical cell membrane By similarity
  • Cell projectionmicrovillus By similarity
  • 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. Colocalizes with actin filaments, EZR and SLC9A3R1 in a punctate pattern at the apical cell surface where microvilli form (By similarity). Colocalizes with PARD3, PRKCI, EXOC5, OCLN, RAB11A and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and luminogenesis.By similarity1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 452431ExtracellularSequence analysisAdd
BLAST
Transmembranei453 – 47321HelicalSequence analysisAdd
BLAST
Topological domaini474 – 55178CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 551530PodocalyxinPRO_0000024756Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence analysis
Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence analysis
Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence analysis
Modified residuei511 – 5111PhosphothreonineBy similarity
Modified residuei530 – 5301PhosphoserineBy similarity
Modified residuei549 – 5491PhosphothreonineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiQ28645.

Expressioni

Tissue specificityi

Glomerular epithelium cell (podocyte) and endothelial cells.1 Publication

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

Binary interactionsi

WithEntry#Exp.IntActNotes
SLC9A3R2Q8SQG97EBI-8375591,EBI-1174758

Protein-protein interaction databases

IntActiQ28645. 1 interaction.
MINTiMINT-1773380.
STRINGi9986.ENSOCUP00000021702.

Family & Domainsi

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

eggNOGiENOG410IFKB. Eukaryota.
ENOG410YCG4. LUCA.
HOGENOMiHOG000115601.
HOVERGENiHBG053629.
InParanoidiQ28645.
KOiK06817.

Family and domain databases

InterProiIPR013836. CD34/Podocalyxin.
IPR017403. PODXL.
[Graphical view]
PANTHERiPTHR12067. PTHR12067. 2 hits.
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.

Q28645-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSALALAAL LLLLLSPPSL SQEKSPQPGP TPMATSTSTR PAPASAPAPK
60 70 80 90 100
SSVAASVPAE QNTTPMTTKA PATQSPSASP GSSVENSAPA QGSTTTQQSL
110 120 130 140 150
SVTTKAEAKD AGGVPTAHVT GSARPVTSGS QVAAQDPAAS KAPSNHSITT
160 170 180 190 200
KPLATEATSQ APRQTTDVGT PGPTAPPVTN STSPDLLGHA TPKPSEGPQL
210 220 230 240 250
SFPTAAGSLG PVTGSGTGSG TLSTPQGKPA TLTPVASSAE TQGMPSPMPP
260 270 280 290 300
SPASPSSSPF PSSPSPSPAL QPSGPSAAGT EDTTGRGPTS SSTELASTAL
310 320 330 340 350
HGPSTLSPTS AVRDQRVSCG PPERPTEQLL ILNLTRSSPC IHVFQRQSQG
360 370 380 390 400
EGETEISMHS TDSLPEDKLV TLLCRAAKPT FNPAQDQCHV LLAPMLGSHA
410 420 430 440 450
VVVKEITIKT NLLPTAVFEL LKDRWDDLRE EGVSDMQLGD QGPPEETEDR
460 470 480 490 500
FSLPLIITIV CMASFLLLVA ALYGCCHQRL SHRKDQQRLT EELQTVENGY
510 520 530 540 550
HDNPTLEVME TSAEMQEKKV VNLNGELGDS WIVPLDNLTK DDLDEEEDTH

L
Length:551
Mass (Da):57,041
Last modified:November 1, 1996 - v1
Checksum:iE9B8AE168CDFB8C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35239 mRNA. Translation: AAC48489.1.
RefSeqiNP_001076235.1. NM_001082766.1.
UniGeneiOcu.2283.

Genome annotation databases

GeneIDi100009552.
KEGGiocu:100009552.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35239 mRNA. Translation: AAC48489.1.
RefSeqiNP_001076235.1. NM_001082766.1.
UniGeneiOcu.2283.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ28645. 1 interaction.
MINTiMINT-1773380.
STRINGi9986.ENSOCUP00000021702.

Proteomic databases

PRIDEiQ28645.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009552.
KEGGiocu:100009552.

Organism-specific databases

CTDi5420.

Phylogenomic databases

eggNOGiENOG410IFKB. Eukaryota.
ENOG410YCG4. LUCA.
HOGENOMiHOG000115601.
HOVERGENiHBG053629.
InParanoidiQ28645.
KOiK06817.

Family and domain databases

InterProiIPR013836. CD34/Podocalyxin.
IPR017403. PODXL.
[Graphical view]
PANTHERiPTHR12067. PTHR12067. 2 hits.
PfamiPF06365. CD34_antigen. 1 hit.
[Graphical view]
PIRSFiPIRSF038143. Podocalyxin-like_p1. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning, expression, and characterization of podocalyxin-like protein 1 from rabbit as a transmembrane protein of glomerular podocytes and vascular endothelium."
    Kershaw D.B., Thomas P.E., Wharram B.L., Goyal M., Wiggins J.E., Whiteside C.I., Wiggins R.C.
    J. Biol. Chem. 270:29439-29446(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: New Zealand white.
  2. "A molecular network for de novo generation of the apical surface and lumen."
    Bryant D.M., Datta A., Rodriguez-Fraticelli A.E., Peraenen J., Martin-Belmonte F., Mostov K.E.
    Nat. Cell Biol. 12:1035-1045(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPODXL_RABIT
AccessioniPrimary (citable) accession number: Q28645
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 1, 1996
Last modified: November 11, 2015
This is version 76 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.