PODXL2

PODXL2
Identifiers
Aliases	PODXL2 , EG, PODLX2, podocalyxin like 2
External IDs	OMIM: 616627 MGI: 2442488 HomoloGene: 9254 GeneCards: PODXL2
Gene location (Human)
Chr.	Chromosome 3 (human)
End	127,672,802 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	88,875,044 bp
RNA expression pattern
	Top expressed in
	ganglionic eminence; ; anterior pituitary; ; prefrontal cortex; ; Brodmann area 9; ; nucleus accumbens; ; amygdala; ; caudate nucleus; ; hypothalamus; ; putamen; ; hippocampus proper;
	Top expressed in
	dorsomedial hypothalamic nucleus; ; superior frontal gyrus; ; suprachiasmatic nucleus; ; cerebellar cortex; ; dorsal tegmental nucleus; ; lateral hypothalamus; ; superior colliculus; ; habenula; ; ventromedial nucleus; ; paraventricular nucleus of hypothalamus;
	More reference expression data
	n/a
Gene ontology
Molecular function	glycosaminoglycan binding ; protein binding ;
Cellular component	integral component of membrane ; integral component of plasma membrane ; membrane ; Golgi lumen ;
Biological process	leukocyte tethering or rolling ; cell adhesion ;
	Sources:Amigo / QuickGO
Orthologs
	50512
	319655
	ENSG00000114631
	ENSMUSG00000033152
	Q9NZ53
	Q8CAE9
	NM_015720
	NM_176973 ; NM_001347327 ; NM_001364575
	NP_056535
NP_001334256 ; NP_795947 ; NP_001351504 ; NP_001366146 ; NP_001366147 ;
	NP_001366148 ; NP_001366149 ; NP_001366150 ; NP_001366151 ; NP_001366152 Contents Structure ; Function ; References ; Further reading ;
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 04, 2023

Podocalyxin like 2 is a protein that in humans is encoded by the PODXL2 gene. ^[5]

Structure

This gene is a member of the CD34 family of cell surface transmembrane proteins, which are characterized by an N-terminal extracellular mucin domain, globular and stalk domains, a single pass transmembrane region, and a charged cytoplasmic tail. The encoded protein is a ligand for vascular selectins. [provided by RefSeq, Oct 2012].

Function

Acts as a ligand for vascular selectins. Mediates rapid rolling of leukocytes over vascular surfaces through high affinity divalent cation-dependent interactions with E-, P- and L-selectins

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