ID F1SNF3_PIG Unreviewed; 516 AA.
AC F1SNF3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Podocalyxin {ECO:0000256|ARBA:ARBA00017371, ECO:0000256|PIRNR:PIRNR038143};
DE AltName: Full=Podocalyxin-like protein 1 {ECO:0000256|ARBA:ARBA00031141, ECO:0000256|PIRNR:PIRNR038143};
GN Name=PODXL {ECO:0000313|Ensembl:ENSSSCP00000017534.4,
GN ECO:0000313|VGNC:VGNC:110306};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000017534.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000017534.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000017534.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000017534.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. Induces the formation of apical actin-
CC dependent microvilli. Involved in the formation of a preapical plasma
CC membrane subdomain to set up initial epithelial polarization and the
CC 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.
CC {ECO:0000256|ARBA:ARBA00003167}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004221, ECO:0000256|PIRNR:PIRNR038143}. Cell
CC membrane {ECO:0000256|ARBA:ARBA00004236}. Cell projection, filopodium
CC {ECO:0000256|ARBA:ARBA00004486}. Cell projection, microvillus
CC {ECO:0000256|ARBA:ARBA00004105, ECO:0000256|PIRNR:PIRNR038143}. Cell
CC projection, ruffle {ECO:0000256|ARBA:ARBA00004466}. Membrane raft
CC {ECO:0000256|PIRNR:PIRNR038143}. Cell projection, lamellipodium
CC {ECO:0000256|PIRNR:PIRNR038143}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the podocalyxin family.
CC {ECO:0000256|ARBA:ARBA00007029, ECO:0000256|PIRNR:PIRNR038143}.
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DR RefSeq; XP_003134717.3; XM_003134669.4.
DR AlphaFoldDB; F1SNF3; -.
DR STRING; 9823.ENSSSCP00000017534; -.
DR PeptideAtlas; F1SNF3; -.
DR Ensembl; ENSSSCT00000018018.5; ENSSSCP00000017534.4; ENSSSCG00000016548.5.
DR GeneID; 100512201; -.
DR KEGG; ssc:100512201; -.
DR CTD; 5420; -.
DR VGNC; VGNC:110306; PODXL.
DR GeneTree; ENSGT00730000111314; -.
DR HOGENOM; CLU_032485_0_0_1; -.
DR InParanoid; F1SNF3; -.
DR OrthoDB; 4265119at2759; -.
DR Proteomes; UP000008227; Chromosome 18.
DR Bgee; ENSSSCG00000016548; Expressed in endocardial endothelium and 43 other cell types or tissues.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0031528; C:microvillus membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0032534; P:regulation of microvillus assembly; IBA:GO_Central.
DR InterPro; IPR013836; CD34/Podocalyxin.
DR InterPro; IPR017403; PODXL.
DR PANTHER; PTHR12067; PODOCALYXIN; 1.
DR PANTHER; PTHR12067:SF5; PODOCALYXIN; 1.
DR Pfam; PF06365; CD34_antigen; 1.
DR PIRSF; PIRSF038143; Podocalyxin-like_p1; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|PIRNR:PIRNR038143};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR038143};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273,
KW ECO:0000256|PIRNR:PIRNR038143};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR038143};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..516
FT /note="Podocalyxin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023833945"
FT TRANSMEM 416..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 53..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 54163 MW; CEA22AF0C69A1BF9 CRC64;
MRSVLVLSGL LLLLSPSFFL DAANTTANTI ASTTVSAVSN TFSTASIQTM SLNSTSITTS
RSSLQSSTEP KGSMPTSSSA SGVTSAQQNT SPAASTKTEK PTSGSSPTVG SEDLKSTALT
VSTKPEITSG QSEITKVTAS VVSTEGHQTT TSPINLNNTS KTSPASTPVP ALASISQPGT
VPGTPPVPVT LVPMTPEPPG SSSQGSNRNI ATTSVSTPAT FTTQEMLITI TPPVTSRGTQ
RIPSEPPVLP DTPTAPQPTG SASGPRTAPP ARGPTRSSPR LVSAASPTAS LPPPASASGV
EIQCSAPERL SEETFVLNFS KADLCKSSPV GAKLYTLLCQ AAKATFNPSQ DQCNIQLAPV
PEIQSVAVKS ITIHTKLCPK DTFELLKNKW ADLKEVGVTN MQLGDQGPPE ETEDRFSMPL
IITIVCMASF LLLVAALYGC CHQRLSQRKD QQRLTEELQT VENGYHDNPT LEVMETSSEM
QEKKVANLNG ELGDSWIVPL DNLTKDDLEE EEDTHL
//
