The domain within your query sequence starts at position 23 and ends at position 268; the E-value for the SelP_N domain shown below is 9.3e-108.



PFAM accession number:PF04592
Interpro abstract (IPR007671):

SelP is the only known eukaryotic selenoprotein that contains multiple selenocysteine (Sec) residues, and accounts for more than 50% of the selenium content of rat and human plasma [ (PUBMED:10775431) ]. It is thought to be glycosylated [ (PUBMED:11168591) ]. SelP may have antioxidant properties. It can attach to epithelial cells, and may protect vascular endothelial cells against peroxynitrite toxicity [ (PUBMED:10775431) ]. The high selenium content of SelP suggests that it may be involved in selenium intercellular transport or storage [ (PUBMED:11168591) ]. The promoter structure of bovine SelP suggests that it may be involved in countering heavy metal intoxication, and may also have a developmental function [ (PUBMED:9358058) ]. The N-terminal region of SelP can exist independently of the C-terminal region. Zebrafish selenoprotein Pb ( Q98SV0 ) lacks the C-terminal Sec-rich region, and a protein encoded by the rat SelP gene and lacking this region has also been reported [ (PUBMED:11168591) ]. The N-terminal region contains a conserved SecxxCys motif, which is similar to the CysxxCys found in thioredoxins. It is speculated that the N-terminal region may adopt a thioredoxin fold and catalyse redox reactions [ (PUBMED:11168591) ]. The N-terminal region also contains a His-rich region, which is thought to mediate heparin binding. Binding to heparan proteoglycans could account for the membrane binding properties of SelP [ (PUBMED:10775431) ].

The function of the bacterial members of this family is uncharacterised.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry SelP_N