The domain within your query sequence starts at position 249 and ends at position 380; the E-value for the SelP_C domain shown below is 2.6e-78.
GQHRQGHLESUDTTASEGLHLSLAQRKLURRGCINQLLCKLSKESEAAPSSCCCHCRHLI FEKSGSAIAUQCAENLPSLCSUQGLFAEEKVTESCQCRSPPAAUQNQPMNPMEANPNUSU DNQTRKUKUHSN
SelP_C |
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PFAM accession number: | PF04593 |
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Interpro abstract (IPR007672): | 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 always contains one Sec residue, and this is separated from the C-terminal region (9-16 sec residues) by a histidine-rich sequence [ (PUBMED:11168591) ]. The large number of Sec residues in the C-terminal portion of SelP suggests that it may be involved in selenium transport or storage. However, it is also possible that this region has a redox function [ (PUBMED:11168591) ]. |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry SelP_C