UniProt functional annotation for Q5CZR5



	UniProt functional annotation for Q5CZR5

UniProt code: Q5CZR5.

Organism: Danio rerio (Zebrafish) (Brachydanio rerio).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; Danionidae; Danioninae; Danio.

Function: Pore-forming protein which might play a role in host defense. Exists as an antiparallel dimer in solution. Can also assemble into an octameric pore-like structure spanning the cell membrane. Oligomerization may be triggered by binding of the jacalin-type lectin domain to high-mannose cell-surface proteoglycans, and also requires a low pH environment. In vitro, shows high binding affinity for S.cerevisiae mannan and human HIV virus glycoprotein gp120. {ECO:0000269|PubMed:26711430}.

Subunit: Homodimer in soluble form. Forms an octameric pore-like structure in the membrane. {ECO:0000269|PubMed:26711430}.

Subcellular location: Cell membrane {ECO:0000305|PubMed:26711430}.

Induction: Up-regulated in the presence of organophosphate pesticides and zinc. {ECO:0000269|PubMed:27514782}.

Domain: The jacalin-type lectin domain has strong affinity for high- mannose glycans with terminal non-reducing ends of Man(alpha-1,2)Man or Man(alpha-1,3)Man. {ECO:0000269|PubMed:26711430}.

Annotations taken from UniProtKB at the EBI.


Organism:		Danio rerio (Zebrafish) (Brachydanio rerio).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; Danionidae; Danioninae; Danio.



Function:		Pore-forming protein which might play a role in host defense. Exists as an antiparallel dimer in solution. Can also assemble into an octameric pore-like structure spanning the cell membrane. Oligomerization may be triggered by binding of the jacalin-type lectin domain to high-mannose cell-surface proteoglycans, and also requires a low pH environment. In vitro, shows high binding affinity for S.cerevisiae mannan and human HIV virus glycoprotein gp120. {ECO:0000269\|PubMed:26711430}.


Subunit:		Homodimer in soluble form. Forms an octameric pore-like structure in the membrane. {ECO:0000269\|PubMed:26711430}.
Subcellular location:		Cell membrane {ECO:0000305\|PubMed:26711430}.
Induction:		Up-regulated in the presence of organophosphate pesticides and zinc. {ECO:0000269\|PubMed:27514782}.
Domain:		The jacalin-type lectin domain has strong affinity for high- mannose glycans with terminal non-reducing ends of Man(alpha-1,2)Man or Man(alpha-1,3)Man. {ECO:0000269\|PubMed:26711430}.