PODXL_CHICK
ID PODXL_CHICK Reviewed; 571 AA.
AC O57604;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Podocalyxin;
DE AltName: Full=Podocalyxin-like protein 1;
DE Short=PC;
DE Short=PCLP-1;
DE AltName: Full=Thrombomucin;
DE Flags: Precursor;
GN Name=PODXL; Synonyms=MEP21, PCLP, PCLP1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 389-402 AND 425-447, AND
RP TISSUE SPECIFICITY.
RX PubMed=9298993; DOI=10.1083/jcb.138.6.1395;
RA McNagny K.M., Pettersson I., Rossi F., Flamme I., Shevchenko A., Mann M.,
RA Graf T.;
RT "Thrombomucin, a novel cell surface protein that defines thrombocytes and
RT multipotent hematopoietic progenitors.";
RL J. Cell Biol. 138:1395-1407(1997).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17311105; DOI=10.1371/journal.pone.0000237;
RA Nielsen J.S., Graves M.L., Chelliah S., Vogl A.W., Roskelley C.D.,
RA McNagny K.M.;
RT "The CD34-related molecule podocalyxin is a potent inducer of microvillus
RT formation.";
RL PLoS ONE 2:E237-E237(2007).
CC -!- FUNCTION: Involved in the regulation of both adhesion and cell
CC morphology and cancer progression. Functions as an anti-adhesive
CC molecule that maintains an open filtration pathway between neighboring
CC foot processes in the podocyte by charge repulsion. Acts as a pro-
CC adhesive molecule, enhancing the adherence of cells to immobilized
CC ligands, increasing the rate of migration and cell-cell contacts in an
CC integrin-dependent manner. Involved in the formation of a preapical
CC plasma membrane subdomain to set up initial epithelial polarization and
CC the apical lumen formation during renal tubulogenesis. Plays a role in
CC cancer development and aggressiveness by inducing cell migration and
CC invasion through its interaction with the actin-binding protein EZR.
CC Affects EZR-dependent signaling events, leading to increased activities
CC of the MAPK and PI3K pathways in cancer cells (By similarity). Induces
CC the formation of apical actin-dependent microvilli. {ECO:0000250,
CC ECO:0000269|PubMed:17311105}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:17311105}. Cell projection, microvillus
CC {ECO:0000250}. Membrane raft {ECO:0000250}. Cell projection,
CC lamellipodium {ECO:0000250}. Cell projection, filopodium {ECO:0000250}.
CC Cell projection, ruffle {ECO:0000250}. Membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}. Note=In single attached
CC epithelial cells is restricted to a preapical pole on the free plasma
CC membrane whereas other apical and basolateral proteins are not yet
CC polarized. Colocalizes with SLC9A3R2 at the apical plasma membrane
CC during epithelial polarization. Colocalizes with SLC9A3R1 at the trans-
CC Golgi network (transiently). Its association with the membrane raft is
CC transient. Forms granular, punctuated pattern, forming patches,
CC preferentially adopting a polar distribution, located on the migrating
CC poles of the cell or forming clusters along the terminal ends of
CC filipodia establishing contact with the endothelial cells. Colocalizes
CC with the submembrane actin of lamellipodia, particularly associated
CC with ruffles. Colocalizes with vinculin at protrusions of cells.
CC Colocalizes with ITGB1. Colocalizes with actin filaments, ezrin and
CC SLC9A3R1 in a punctate pattern at the apical cell surface where
CC microvilli form. Colocalizes with EZR and SLC9A3R2 at the apical cell
CC membrane of glomerular epithelium cells (By similarity). Colocalizes
CC with SLC9A3R1 at the apical cell membrane. Colocalizes with PARD3,
CC PRKCI, EXOC5, OCLN, RAB11A and RAB8A in apical membrane initiation
CC sites (AMIS) during the generation of apical surface and luminogenesis
CC (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in thrombocytes, kidney podocytes,
CC vascular endothelia and mono- and multipotent progenitors from the bone
CC marrow (at protein level). {ECO:0000269|PubMed:9298993}.
CC -!- DEVELOPMENTAL STAGE: Expressed on the surface of extra- and
CC intraembryonic hematopoietic cells, neural tube, aorta, glomerulus,
CC liver, heart and coelomic cavity in 4 day old embryo; in each of these
CC tissues, detection is restricted to cells comprising the lumenal
CC surfaces of tissues or boundary elements between tissues such as in the
CC liver capsule, aorta, mesonephros, coelomic cavity and the central
CC canal of the neural tube. Expressed in multipotent progenitors of day
CC three yolk sac (at protein level).
CC -!- DOMAIN: Both the O-glycan-rich domain of the extracellular domain and
CC the C-terminus PDZ-binding motif (DTHL) in the cytoplasmic tail harbor
CC an apical sorting signal. The cytoplasmic domain is necessary for the
CC apical membrane targeting and renal tubulogenesis. The large highly
CC anionic extracellular domain allows to maintain open filtration
CC pathways between neighboring podocyte foot processes (By similarity).
CC The cytoplasmic C-terminus PDZ-binding motif (DTHL) is essential for
CC interaction with SLC9A3R1 and for targeting SLC9A3R1 to the apical cell
CC membrane. The extracellular domain is necessary for microvillus
CC formation. {ECO:0000250}.
CC -!- PTM: N- and O-linked glycosylated. Sialoglycoprotein (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the podocalyxin family. {ECO:0000305}.
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DR EMBL; Y13978; CAA74311.1; -; mRNA.
DR RefSeq; NP_001258823.1; NM_001271894.1.
DR AlphaFoldDB; O57604; -.
DR STRING; 9031.ENSGALP00000039359; -.
DR PaxDb; O57604; -.
DR GeneID; 395755; -.
DR KEGG; gga:395755; -.
DR CTD; 5420; -.
DR VEuPathDB; HostDB:geneid_395755; -.
DR eggNOG; ENOG502S2JU; Eukaryota.
DR InParanoid; O57604; -.
DR OrthoDB; 1404598at2759; -.
DR PRO; PR:O57604; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0031528; C:microvillus membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0072175; P:epithelial tube formation; ISS:UniProtKB.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0032534; P:regulation of microvillus assembly; IDA:UniProtKB.
DR InterPro; IPR013836; CD34/Podocalyxin.
DR InterPro; IPR017403; PODXL.
DR PANTHER; PTHR12067; PTHR12067; 1.
DR Pfam; PF06365; CD34_antigen; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Cell projection; Direct protein sequencing;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..571
FT /note="Podocalyxin"
FT /id="PRO_0000394750"
FT TOPO_DOM 20..476
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..571
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 70..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 571 AA; 61015 MW; 9C5FD102759D7731 CRC64;
MRAPLLLPLL PLLLFGVSSG NNDKTTHSTT VSPETTKQIT TITVTTSQVQ GSISASKPSS
TAPTAVMSFT KAQEAATSSK QHDSSTSSIP PPSTSITPSI ITTSPQGKTP STPALTHTPD
QNTKTTGRQD DTSHVSVAST SASQQVSSSA SAAVPTTTSA VTSSATQQKV SPTDSSEILL
KPSASPNSTQ VTSPSRTPKG FLSTVTTSPH IADNGSTALN QLKSTVSSSE VPVSSFLDKD
HSVSSSTSAT NQHLSLSSHR PTSPVPKFEC STPHSGSVPS TSSKTSLSSP SSSTKNATVT
TTMTTAKAAY TSQGDGSVTH KSGVTAQSPT SAPLPTPTLK DHMKSKSPDQ THSNVSPPNE
VICEDQIGEV RPILNLKEEK TCDDWKKASN EAFFEVFCSG RRHAFNSTRD RCTVKLASSN
HRRWAVHVIV HRVLDPAAVF EELKEKRNEL EKLGITNVTY LNQEMEEEIK DQSSTPLIIT
IVTLAGSLLL IAAIYGCCHQ RFSQKKSQQR LTEELQTMEN GYHDNPTLEV METGSEMQEK
KVNLNGELGD SWIVPLDTIM KEDLEEEDTH L
