P70274 · SEPP1_MOUSE
- ProteinSelenoprotein P
- GeneSelenop
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids380 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Might be responsible for some of the extracellular antioxidant defense properties of selenium or might be involved in the transport of selenium (By similarity).
May supply selenium to tissues such as brain and testis
May supply selenium to tissues such as brain and testis
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Molecular Function | selenium binding | |
Biological Process | brain development | |
Biological Process | locomotory behavior | |
Biological Process | post-embryonic development | |
Biological Process | regulation of growth | |
Biological Process | response to selenium ion | |
Biological Process | selenium compound metabolic process | |
Biological Process | sexual reproduction |
Keywords
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSelenoprotein P
- Short namesSeP
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP70274
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Passes from plasma into the glomerular filtrate where it is removed by endocytosis mediated by LRP2 in the proximal tubule epithelium.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MWRSLGLALALCLLPYGGA | ||||||
Chain | PRO_0000022314 | 20-380 | Selenoprotein P | |||
Sequence: ESQGQSSACYKAPEWYIGDQNPMLNSEGKVTVVALLQASUYLCLLQASRLEDLRIKLESQGYFNISYIVVNHQGSPSQLKHSHLKKQVSEHIAVYRQEEDGIDVWTLLNGNKDDFLIYDRCGRLVYHLGLPYSFLTFPYVEEAIKIAYCEERCGNCNLTSLEDEDFCKTVTSATANKTAEPSEAHSHHKHHNKHGQEHLGSSKPSENQQPGPSETTLPPSGLHHHHRHRGQHRQGHLESUDTTASEGLHLSLAQRKLURRGCINQLLCKLSKESEAAPSSCCCHCRHLIFEKSGSAIAUQCAENLPSLCSUQGLFAEEKVTESCQCRSPPAAUQNQPMNPMEANPNUSUDNQTRKUKUHSN | ||||||
Glycosylation | 83 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 176 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 195 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 264 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 365 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 370 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Phosphorylation sites are present in the extracellular medium.
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 196-263 | Disordered | ||||
Sequence: KTAEPSEAHSHHKHHNKHGQEHLGSSKPSENQQPGPSETTLPPSGLHHHHRHRGQHRQGHLESUDTTA | ||||||
Compositional bias | 220-235 | Polar residues | ||||
Sequence: SSKPSENQQPGPSETT | ||||||
Compositional bias | 346-374 | Polar residues | ||||
Sequence: RSPPAAUQNQPMNPMEANPNUSUDNQTRK | ||||||
Region | 346-380 | Disordered | ||||
Sequence: RSPPAAUQNQPMNPMEANPNUSUDNQTRKUKUHSN |
Domain
The C-terminus is not required for endocytic uptake in the proximal tubule epithelium.
Sequence similarities
Belongs to the selenoprotein P family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length380
- Mass (Da)42,706
- Last updated2008-02-26 v3
- Checksum0972BF4993CC208D
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for non-standard residue, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-standard residue | 59 | Selenocysteine | ||||
Sequence: U | ||||||
Sequence conflict | 184 | in Ref. 3; BAC55264 | ||||
Sequence: D → Y | ||||||
Sequence conflict | 188 | in Ref. 2; AAD01684 and 4; AAH01991 | ||||
Sequence: T → N | ||||||
Sequence conflict | 192 | in Ref. 2; AAD01684 | ||||
Sequence: A → V | ||||||
Sequence conflict | 203 | in Ref. 2; AAD01684 | ||||
Sequence: A → V | ||||||
Compositional bias | 220-235 | Polar residues | ||||
Sequence: SSKPSENQQPGPSETT | ||||||
Non-standard residue | 259 | Selenocysteine | ||||
Sequence: U | ||||||
Sequence conflict | 264 | in Ref. 3; BAE34948 | ||||
Sequence: S → R | ||||||
Non-standard residue | 277 | Selenocysteine | ||||
Sequence: U | ||||||
Sequence conflict | 308 | in Ref. 3; BAC55264 | ||||
Sequence: I → V | ||||||
Non-standard residue | 318 | Selenocysteine | ||||
Sequence: U | ||||||
Sequence conflict | 321 | in Ref. 4; AAH01991 | ||||
Sequence: A → C | ||||||
Non-standard residue | 330 | Selenocysteine | ||||
Sequence: U | ||||||
Compositional bias | 346-374 | Polar residues | ||||
Sequence: RSPPAAUQNQPMNPMEANPNUSUDNQTRK | ||||||
Non-standard residue | 352 | Selenocysteine | ||||
Sequence: U | ||||||
Non-standard residue | 366 | Selenocysteine | ||||
Sequence: U | ||||||
Non-standard residue | 368 | Selenocysteine | ||||
Sequence: U | ||||||
Non-standard residue | 375 | Selenocysteine | ||||
Sequence: U | ||||||
Non-standard residue | 377 | Selenocysteine | ||||
Sequence: U |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X99807 EMBL· GenBank· DDBJ | CAA68140.2 EMBL· GenBank· DDBJ | mRNA | ||
AF021345 EMBL· GenBank· DDBJ | AAD01684.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK002450 EMBL· GenBank· DDBJ | BAC55246.3 EMBL· GenBank· DDBJ | mRNA | ||
AK077265 EMBL· GenBank· DDBJ | BAC55264.3 EMBL· GenBank· DDBJ | mRNA | ||
AK146774 EMBL· GenBank· DDBJ | BAE27423.1 EMBL· GenBank· DDBJ | mRNA | ||
AK148623 EMBL· GenBank· DDBJ | BAE28626.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159269 EMBL· GenBank· DDBJ | BAE34948.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159524 EMBL· GenBank· DDBJ | BAE35153.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159894 EMBL· GenBank· DDBJ | BAE35460.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159911 EMBL· GenBank· DDBJ | BAE35474.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159935 EMBL· GenBank· DDBJ | BAE35495.1 EMBL· GenBank· DDBJ | mRNA | ||
AK167611 EMBL· GenBank· DDBJ | BAE39664.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168463 EMBL· GenBank· DDBJ | BAE40359.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168583 EMBL· GenBank· DDBJ | BAE40452.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168631 EMBL· GenBank· DDBJ | BAE40491.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168747 EMBL· GenBank· DDBJ | BAE40587.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168926 EMBL· GenBank· DDBJ | BAE40739.1 EMBL· GenBank· DDBJ | mRNA | ||
AK169011 EMBL· GenBank· DDBJ | BAE40808.1 EMBL· GenBank· DDBJ | mRNA | ||
AK169158 EMBL· GenBank· DDBJ | BAE40937.1 EMBL· GenBank· DDBJ | mRNA | ||
AK169362 EMBL· GenBank· DDBJ | BAE41111.1 EMBL· GenBank· DDBJ | mRNA | ||
BC001991 EMBL· GenBank· DDBJ | AAH01991.2 EMBL· GenBank· DDBJ | mRNA |