Summary: Selenoprotein P, N terminal region
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Selenoprotein P, N terminal region Provide feedback
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]. The function of the bacterial members of this family is uncharcterised.
Literature references
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Mostert V; , Arch Biochem Biophys 2000;376:433-438.: Selenoprotein P: properties, functions, and regulation. PUBMED:10775431 EPMC: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 EPMC: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 EPMC:9358058
External database links
| PANDIT: | PF04592 |
| Pseudofam: | PF04592 |
| SYSTERS: | SelP_N |
This tab holds annotation information from the InterPro database.
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 (SWISSPROT) 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.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | selenium binding (GO:0008430) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan Thioredoxin (CL0172), which contains the following 45 members:
2Fe-2S_thioredx AhpC-TSA AhpC-TSA_2 ArsC ArsD Calsequestrin DIM1 DSBA DUF1525 DUF1687 DUF2703 DUF4174 DUF836 DUF899 DUF953 ERp29_N Glutaredoxin GSHPx GST_N GST_N_2 GST_N_3 HyaE KaiB MRP-S23 MRP-S25 OST3_OST6 Phosducin Redoxin SCO1-SenC SelP_N SH3BGR T4_deiodinase Thioredox_DsbH Thioredoxin Thioredoxin_2 Thioredoxin_3 Thioredoxin_4 Thioredoxin_5 Thioredoxin_6 Thioredoxin_7 Thioredoxin_8 Thioredoxin_9 Tom37 TraF YtfJ_HI0045Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (6) |
Full (83) |
Representative proteomes | NCBI (89) |
Meta (1) |
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| RP15 (10) |
RP35 (14) |
RP55 (34) |
RP75 (49) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (6) |
Full (83) |
Representative proteomes | NCBI (89) |
Meta (1) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (10) |
RP35 (14) |
RP55 (34) |
RP75 (49) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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 HMMER3.
HMM logo
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Trees
This page displays the phylogenetic tree for this family's seed alignment. 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 alignment.
Note: You can also download the data file for the tree.
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: | 83 |
| Average length of the domain: | 177.60 aa |
| Average identity of full alignment: | 34 % |
| Average coverage of the sequence by the domain: | 63.13 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 238 | ||||||||||||
| Family (HMM) version: | 9 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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