Summary
Selenoprotein P, N terminal region
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 [1]. It is thought to be glycosylated [2]. SelP may have antioxidant properties. It can attach to epithelial cells, and may protect vascular endothelial cells against peroxynitrite toxicity [1]. The high selenium content of SelP suggests that it may be involved in selenium intercellular transport or storage [2]. The promoter structure of bovine SelP suggest that it may be involved in countering heavy metal intoxication, and may also have a developmental function [3]. 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 [2]. 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 [2]. 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 [1].
Literature references
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Mostert V; , Arch Biochem Biophys 2000;376:433-438.: Selenoprotein P: properties, functions, and regulation. PUBMED:10775431
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Kryukov GV, Gladyshev VN; , Genes Cells 2000;5:1049-1060.: Selenium metabolism in zebrafish: multiplicity of selenoprotein genes and expression of a protein containing 17 selenocysteine residues. PUBMED:11168591
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Fujii M, Saijoh K, Kobayashi T, Fujii S, Lee MJ, Sumino K; , Gene 1997;199:211-217.: Analysis of bovine selenoprotein P-like protein gene and availability of metal responsive element (MRE) located in its promoter. PUBMED:9358058
InterPro entry 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 () 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.Clan
This family is a member of clan Thioredoxin-like (CL0172), which contains the following 27 members:
AhpC-TSA ArsC Calsequestrin DIM1 DSBA DUF1525 DUF1687 DUF255 DUF836 DUF899 DUF953 ERp29_N Glutaredoxin GSHPx GST_N HyaE KaiB OST3_OST6 Phosducin Redoxin SCO1-SenC SelP_N SH3BGR T4_deiodinase Thioredoxin Tom37 YtfJ_HI0045Gene Ontology
| Molecular function | selenium binding (GO:0008430) |
External database links
| PANDIT: | PF04592 |
| SYSTERS: | SelP_N |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | DOMO:DM04433; |
| Previous IDs: | none |
| Type: | Family |
| Author: | Kerrison ND |
| Number in seed: | 6 |
| Number in full: | 29 |
| Average length of the domain: | 181.40 aa |
| Average identity of full alignment: | 33 % |
| Average coverage of the sequence by the domain: | 64.04 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 238 | ||||||||||||
| Family (HMM) version: | 7 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
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