Summary: Selenoprotein P, N terminal region
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Selenoprotein P Edit Wikipedia article
| SelP, N terminus | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | SelP_N | ||||||||
| Pfam | PF04592 | ||||||||
| Pfam clan | CL0172 | ||||||||
| InterPro | IPR007671 | ||||||||
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| SelP, C terminus | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | SelP_C | ||||||||
| Pfam | PF04593 | ||||||||
| InterPro | IPR007672 | ||||||||
| |||||||||
In molecular biology, the protein domain selenoprotein P (SelP) is the only known eukaryotic selenoprotein that contains multiple selenocysteine (Sec) residues. It is a secreted glycoprotein, often found in the plasma. Its precise function remains to be elucidated; however, it is thought to have antioxidant properties.[1] This particular protein contains two domains: the C terminal and N terminal domain. The N-terminal domain is larger than the C terminal[2] and the N-terminal is thought to be glycosylated.[3]
Contents
Function
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.[3] The promoter structure of bovine SelP suggests that it may be involved in countering heavy metal intoxication, and may also have a developmental function.[4]
Structure
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.[3] 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.[3]
N terminal domain
Function
N-terminal domain allows conservation of whole body selenium and appears to supply selenium to the kidney[5]
Structure
The structure of the N-terminal domain is larger and contains less Selenium. However it is thought to be heavily glycosylated[5]
C terminal domain
Function
The function of the C-terminal domain is known to be vital for maintaining levels of selenium in brain and testis but not for the maintenance of whole body selenium. Brain and testis tissue.[5]
Structure
The C-terminal domain is smaller in size but far more rich in selenium.[5]
Protein interactions
Binds to heparin in a pH-dependent manner[2]
References
- ^ a b Mostert V (April 2000). "Selenoprotein P: properties, functions, and regulation". Arch. Biochem. Biophys. 376 (2): 433–8. doi:10.1006/abbi.2000.1735. PMID 10775431.
- ^ a b Burk RF; Hill KE (2009). "Selenoprotein P-expression, functions, and roles in mammals". Biochim Biophys Acta. 1790 (11): 1441–7. doi:10.1016/j.bbagen.2009.03.026. PMC 2763998. PMID 19345254.
- ^ a b c d Kryukov GV; Gladyshev VN (December 2000). "Selenium metabolism in zebrafish: multiplicity of selenoprotein genes and expression of a protein containing 17 selenocysteine residues". Genes Cells. 5 (12): 1049–60. doi:10.1046/j.1365-2443.2000.00392.x. PMID 11168591.
- ^ Fujii M; Saijoh K; Kobayashi T; Fujii S; Lee MJ; Sumino K (October 1997). "Analysis of bovine selenoprotein P-like protein gene and availability of metal responsive element (MRE) located in its promoter". Gene. 199 (1–2): 211–7. doi:10.1016/S0378-1119(97)00369-7. PMID 9358058.
- ^ a b c d Hill KE, Zhou J, Austin LM, Motley AK, Ham AJ, Olson GE, et al. (2007). "The selenium-rich C-terminal domain of mouse selenoprotein P is necessary for the supply of selenium to brain and testis but not for the maintenance of whole body selenium". J Biol Chem. 282 (15): 10972–80. doi:10.1074/jbc.M700436200. PMID 17311913.
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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
-
Mostert V; , Arch Biochem Biophys 2000;376:433-438.: Selenoprotein P: properties, functions, and regulation. PUBMED:10775431 EPMC:10775431
-
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
-
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
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 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 62 members:
2Fe-2S_thioredx AhpC-TSA AhpC-TSA_2 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 GST_N_5 HyaE KaiB L51_S25_CI-B8 MRP-S23 MRP-S25 OST3_OST6 Phe_hydrox_dim Phosducin QSOX_Trx1 Rdx Redoxin SCO1-SenC SelP_N Sep15_SelM SH3BGR T4_deiodinase Thioredox_DsbH Thioredoxin Thioredoxin_11 Thioredoxin_12 Thioredoxin_13 Thioredoxin_14 Thioredoxin_15 Thioredoxin_16 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 (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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| Seed (10) |
Full (362) |
Representative proteomes | UniProt (627) |
NCBI (991) |
Meta (0) |
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| RP15 (47) |
RP35 (107) |
RP55 (250) |
RP75 (361) |
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| PP/heatmap | 1 | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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| Seed (10) |
Full (362) |
Representative proteomes | UniProt (627) |
NCBI (991) |
Meta (0) |
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|---|---|---|---|---|---|---|---|---|---|
| RP15 (47) |
RP35 (107) |
RP55 (250) |
RP75 (361) |
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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.
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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
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 |
| Sequence Ontology: | SO:0100021 |
| Author: |
Kerrison ND 
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| Number in seed: | 10 |
| Number in full: | 362 |
| Average length of the domain: | 166.50 aa |
| Average identity of full alignment: | 29 % |
| Average coverage of the sequence by the domain: | 55.30 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 233 | ||||||||||||
| Family (HMM) version: | 15 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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