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0  structures 77  species 0  interactions 116  sequences 3  architectures

Family: SelP_N (PF04592)

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 uncharacterised.

Literature references

  1. Mostert V; , Arch Biochem Biophys 2000;376:433-438.: Selenoprotein P: properties, functions, and regulation. PUBMED:10775431 EPMC:10775431

  2. 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

  3. 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


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.

Domain organisation

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Pfam Clan

This family is a member of clan Thioredoxin (CL0172), which has the following description:

This clan contains families related to the thioredoxin family. Thioredoxins are small enzymes that are involved in redox reactions via the reversible oxidation of an active centre disulfide bond. The thioredoxin fold consists of a 3 layer alpha/beta/alpha sandwich and a central beta sheet.

The clan contains the following 57 members:

2Fe-2S_thioredx AhpC-TSA AhpC-TSA_2 Aminopep ArsC ArsD Calsequestrin DIM1 DSBA DUF1223 DUF1462 DUF1525 DUF1687 DUF2703 DUF2847 DUF4174 DUF836 DUF899 DUF953 ERp29_N GILT Glutaredoxin GSHPx GST_N GST_N_2 GST_N_3 GST_N_4 HyaE KaiB L51_S25_CI-B8 Metallopep MRP-S23 MRP-S25 OST3_OST6 Peptidase_M76 Phosducin Rdx Redoxin SCO1-SenC SelP_N Sep15_SelM 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_HI0045 Zincin_1

Alignments

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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
(11)
Full
(116)
Representative proteomes UniProt
(238)
NCBI
(522)
Meta
(0)
RP15
(31)
RP35
(59)
RP55
(96)
RP75
(110)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(11)
Full
(116)
Representative proteomes UniProt
(238)
NCBI
(522)
Meta
(0)
RP15
(31)
RP35
(59)
RP55
(96)
RP75
(110)
Alignment:
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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
(11)
Full
(116)
Representative proteomes UniProt
(238)
NCBI
(522)
Meta
(0)
RP15
(31)
RP35
(59)
RP55
(96)
RP75
(110)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download    
Gzipped Download   Download   Download   Download   Download   Download   Download   Download    

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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'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.

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Curation and family details

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Curation View help on the curation process

Seed source: DOMO:DM04433;
Previous IDs: none
Type: Family
Author: Kerrison ND
Number in seed: 11
Number in full: 116
Average length of the domain: 173.70 aa
Average identity of full alignment: 28 %
Average coverage of the sequence by the domain: 57.39 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 17690987 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.2 23.2
Trusted cut-off 23.8 24.4
Noise cut-off 23.1 23.1
Model length: 233
Family (HMM) version: 12
Download: download the raw HMM for this family

Species distribution

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