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0  structures 48  species 0  interactions 83  sequences 4  architectures

Family: SelP_N (PF04592)

Summary: Selenoprotein P, N terminal region

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This is the Wikipedia entry entitled "Selenoprotein P". More...

Selenoprotein P Edit Wikipedia article

SelP, N terminus
Identifiers
Symbol SelP_N
Pfam PF04592
Pfam clan CL0172
InterPro IPR007671
SelP, C terminus
Identifiers
Symbol SelP_C
Pfam PF04593
InterPro IPR007672

In molecular biology the protein domain SelP stands for selenoprotein P which is the only known eukaryotic selenoprotein that contains multiple selenocysteine (Sec) residues. It is a secreted glycoprotein, often found in the plasma. It's 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]

Function[edit]

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[edit]

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[edit]

Function[edit]

N-terminal domain allows conservation of whole body selenium and appears to supply selenium to the kidney[5]

Structure[edit]

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[edit]

Function[edit]

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[edit]

The N-terminal domain is smaller in size but far more rich in selenium.[5]

Protein interactions[edit]

Binds to herapin in a pH-dependent manner[2]

References[edit]

  1. ^ 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. 
  2. ^ 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. 
  3. ^ 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. PMID 11168591. 
  4. ^ 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. 
  5. ^ 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. 

This article incorporates text from the public domain Pfam and InterPro IPR007672

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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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

  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


External database links

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.

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 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_HI0045

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Representative proteomes NCBI
(89)
Meta
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RP35
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RP55
(34)
RP75
(49)
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(6)
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Representative proteomes NCBI
(89)
Meta
(1)
RP15
(10)
RP35
(14)
RP55
(34)
RP75
(49)
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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: 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 View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.9 22.9
Trusted cut-off 23.4 23.3
Noise cut-off 22.8 22.8
Model length: 238
Family (HMM) version: 9
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Species distribution

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