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Protein

Podocalyxin

Gene

PODXL

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

Keywordsi

Biological processCell 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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 452ExtracellularSequence analysisAdd BLAST431
Transmembranei453 – 473HelicalSequence analysisAdd BLAST21
Topological domaini474 – 551CytoplasmicSequence analysisAdd BLAST78

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000002475622 – 551PodocalyxinAdd BLAST530

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi145N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi180N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi333N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei511PhosphothreonineBy similarity1
Modified residuei530PhosphoserineBy similarity1
Modified residuei549PhosphothreonineBy similarity1

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 interactor
MINTiQ28645
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

InterProiView protein in InterPro
IPR013836 CD34/Podocalyxin
IPR017403 PODXL
PANTHERiPTHR12067 PTHR12067, 1 hit
PfamiView protein in Pfam
PF06365 CD34_antigen, 1 hit
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

Similar proteinsi

Entry informationi

Entry nameiPODXL_RABIT
AccessioniPrimary (citable) accession number: Q28645
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 1, 1996
Last modified: March 28, 2018
This is version 80 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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