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Podocalyxin (Gp135) (Podocalyxin-like protein 1) (PC) (PC-like protein 1) (PCLP-1) (cPCLP1)

 PODXL_CANLF             Reviewed;         571 AA.
Q52S86;
15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
25-OCT-2017, entry version 60.
RecName: Full=Podocalyxin;
AltName: Full=Gp135;
AltName: Full=Podocalyxin-like protein 1;
Short=PC;
Short=PC-like protein 1;
Short=PCLP-1;
Short=cPCLP1;
Flags: Precursor;
Name=PODXL; Synonyms=PCLP, PCLP1;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 398-406; 448-466 AND
525-538, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-199;
ASN-373 AND ASN-383, MUTAGENESIS OF ASN-123; ASN-199; ASN-373 AND
ASN-383, AND TISSUE SPECIFICITY.
PubMed=15814834; DOI=10.1681/ASN.2004121145;
Cheng H.Y., Lin Y.Y., Yu C.Y., Chen J.Y., Shen K.F., Lin W.L.,
Liao H.K., Chen Y.J., Liu C.H., Pang V.F., Jou T.S.;
"Molecular identification of canine podocalyxin-like protein 1 as a
renal tubulogenic regulator.";
J. Am. Soc. Nephrol. 16:1612-1622(2005).
[2]
FUNCTION, INTERACTION WITH SLC9A3R2, AND SUBCELLULAR LOCATION.
PubMed=15642748; DOI=10.1083/jcb.200407072;
Meder D., Shevchenko A., Simons K., Fuellekrug J.;
"Gp135/podocalyxin and NHERF-2 participate in the formation of a
preapical domain during polarization of MDCK cells.";
J. Cell Biol. 168:303-313(2005).
[3]
SUBUNIT, INTERACTION WITH SLC9A3R1, GLYCOSYLATION AT ASN-199; ASN-373
AND ASN-383, AND MUTAGENESIS OF ASN-199; ASN-373 AND ASN-383.
PubMed=17332505; DOI=10.1091/mbc.E06-07-0629;
Yu C.Y., Chen J.Y., Lin Y.Y., Shen K.F., Lin W.L., Chien C.L.,
ter Beest M.B., Jou T.S.;
"A bipartite signal regulates the faithful delivery of apical domain
marker podocalyxin/Gp135.";
Mol. Biol. Cell 18:1710-1722(2007).
-!- 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.
{ECO:0000269|PubMed:15642748, ECO:0000269|PubMed:15814834}.
-!- SUBUNIT: 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. 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). Monomer; when associated with
the membrane raft. Oligomer; when integrated in the apical
membrane. Interacts with SLC9A3R2. Interacts (via the C-terminal
PDZ-binding motif DTHL) with SLC9A3R1 (via the PDZ domains); the
interaction take place early in the secretory pathway and is
necessary for its apical membrane sorting. {ECO:0000250,
ECO:0000269|PubMed:15642748, ECO:0000269|PubMed:17332505}.
-!- SUBCELLULAR LOCATION: Apical cell membrane. Membrane raft. Cell
projection, lamellipodium {ECO:0000250}. Cell projection,
filopodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}.
Cell projection, microvillus {ECO:0000250}. Membrane
{ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Note=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
actin filaments, ezrin and SLC9A3R1 in a punctate pattern at the
apical cell surface where microvilli form. Colocalizes with EZR
and SLC9A3R2 at the apical cell membrane of glomerular epithelium
cells (By similarity). 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. 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). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in glomerular and tubular epithelial
cells and peritubular capillaries of the kidney (at protein
level). Expressed in heart, lung, renal cortex and medulla, kidney
and muscle. {ECO:0000269|PubMed:15814834}.
-!- DOMAIN: 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).
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.
{ECO:0000250}.
-!- PTM: N- and O-linked glycosylated. Sialoglycoprotein.
{ECO:0000269|PubMed:15814834, ECO:0000269|PubMed:17332505}.
-!- SIMILARITY: Belongs to the podocalyxin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY970669; AAX93749.1; -; mRNA.
RefSeq; NP_001018645.1; NM_001020809.1.
UniGene; Cfa.23488; -.
SMR; Q52S86; -.
STRING; 9615.ENSCAFP00000041563; -.
iPTMnet; Q52S86; -.
PaxDb; Q52S86; -.
GeneID; 482252; -.
KEGG; cfa:482252; -.
CTD; 5420; -.
eggNOG; ENOG410IFKB; Eukaryota.
eggNOG; ENOG410YCG4; LUCA.
HOGENOM; HOG000115601; -.
HOVERGEN; HBG053629; -.
InParanoid; Q52S86; -.
KO; K06817; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030175; C:filopodium; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0031528; C:microvillus membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0001726; C:ruffle; ISS:UniProtKB.
GO; GO:0036057; C:slit diaphragm; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0072175; P:epithelial tube formation; IDA:UniProtKB.
GO; GO:0072015; P:glomerular visceral epithelial cell development; ISS:UniProtKB.
GO; GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0032534; P:regulation of microvillus assembly; ISS:UniProtKB.
InterPro; IPR013836; CD34/Podocalyxin.
InterPro; IPR017403; PODXL.
PANTHER; PTHR12067; PTHR12067; 1.
Pfam; PF06365; CD34_antigen; 1.
PIRSF; PIRSF038143; Podocalyxin-like_p1; 1.
1: Evidence at protein level;
Cell adhesion; Cell membrane; Cell projection; Complete proteome;
Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 571 Podocalyxin.
/FTId=PRO_5000095844.
TOPO_DOM 23 474 Extracellular. {ECO:0000255}.
TRANSMEM 475 495 Helical. {ECO:0000255}.
TOPO_DOM 496 571 Cytoplasmic. {ECO:0000255}.
COMPBIAS 257 348 Pro-rich.
MOD_RES 531 531 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9R0M4}.
MOD_RES 550 550 Phosphoserine.
{ECO:0000250|UniProtKB:O00592}.
MOD_RES 569 569 Phosphothreonine.
{ECO:0000250|UniProtKB:O00592}.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15814834,
ECO:0000269|PubMed:17332505}.
CARBOHYD 373 373 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15814834,
ECO:0000269|PubMed:17332505}.
CARBOHYD 383 383 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15814834,
ECO:0000269|PubMed:17332505}.
MUTAGEN 123 123 N->Q: Does not reduce N-glycosylation.
{ECO:0000269|PubMed:15814834}.
MUTAGEN 199 199 N->Q: Reduces N-glycosylation but not
apical targeting. Reduces strongly N-
glycosylation but not apical targeting;
when associated with Q-373 and Q-383.
{ECO:0000269|PubMed:15814834,
ECO:0000269|PubMed:17332505}.
MUTAGEN 373 373 N->Q: Reduces N-glycosylation but not
apical targeting. Reduces strongly N-
glycosylation but not apical targeting;
when associated with Q-199 and Q-383.
{ECO:0000269|PubMed:15814834,
ECO:0000269|PubMed:17332505}.
MUTAGEN 383 383 N->Q: Reduces N-glycosylation but not
apical targeting. Reduces strongly N-
glycosylation but not apical targeting;
when associated with Q-199 and Q-373.
{ECO:0000269|PubMed:15814834,
ECO:0000269|PubMed:17332505}.
SEQUENCE 571 AA; 59906 MW; EA23F38263093539 CRC64;
MRPAPPPPLL LLLLLLPPPS LSHDGTIIAA TSPTSGQPST ELPGGKGLIT TAKTIQNTDL
AITGEKVMSA TVSKGPLPGS SNSVSMTLAP TQKNTVIAPD QDEKVSTNPT IATSDSKGIP
DLNKSILPSA TNSMKPDTPV TQTAGPGAQG NPGTTVSHMT SENTEQTTSQ PPPQVKPSSI
TPALTSIITP TSPRQPSANS TTLKPPESSS ESPDKSHTAS SSLGTKVVPS SSLYGTSPTR
TSSVTFWGGP QSSSGTPPVP APTPRPAATS SSTPGISSVP GTTSLPSETE SLESPSSESP
SQPPKLRPTG PPSSGSSGPA ASLPDEGPRS SSTQRAATAP RAPSVPSPTS AQGDDRIKCE
SPGRLTDKML LLNLTRSGLC AGNNSDDKLI TLLCRAAKAT FNPAQDQCHI RLVPIQDTQA
VAIKEITVQT NLLPRDVYEL LKDKWDELKE VGVSNMKLGD QGPPEETEDR FSMPLIITIV
CMASFLLLVA ALYGCCHQRL SQRKDQQRLT EELQTVENGY HDNPTLEVME TSSEMQEKKV
VNLNGELGDS WIVPLDNLAK DDLDEEEDTH L


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