P01572 · IFNA1_MOUSE
- ProteinInterferon alpha-1
- GeneIfna1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids189 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
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 | cytokine activity | |
Molecular Function | type I interferon receptor binding | |
Biological Process | adaptive immune response | |
Biological Process | B cell differentiation | |
Biological Process | B cell proliferation | |
Biological Process | cytokine-mediated signaling pathway | |
Biological Process | defense response to bacterium | |
Biological Process | defense response to virus | |
Biological Process | humoral immune response | |
Biological Process | natural killer cell activation involved in immune response | |
Biological Process | positive regulation of peptidyl-serine phosphorylation of STAT protein | |
Biological Process | regulation of defense response to virus by host | |
Biological Process | response to exogenous dsRNA | |
Biological Process | T cell activation involved in immune response | |
Biological Process | type I interferon-mediated signaling pathway |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInterferon alpha-1
- Short namesIFN-alpha-1
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP01572
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, disulfide bond, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MARLCAFLMVLAVLSYWPTCSLG | ||||||
Disulfide bond | 24↔122 | |||||
Sequence: CDLPQTHNLRNKRALTLLVQMRRLSPLSCLKDRKDFGFPQEKVDAQQIKKAQAIPVLSELTQQILNIFTSKDSSAAWNTTLLDSFCNDLHQQLNDLQGC | ||||||
Chain | PRO_0000016375 | 24-189 | Interferon alpha-1 | |||
Sequence: CDLPQTHNLRNKRALTLLVQMRRLSPLSCLKDRKDFGFPQEKVDAQQIKKAQAIPVLSELTQQILNIFTSKDSSAAWNTTLLDSFCNDLHQQLNDLQGCLMQQVGVQEFPLTQEDALLAVRKYFHRITVYLREKKHSPCAWEVVRAEVWRALSSSANVLGRLREEK | ||||||
Disulfide bond | 52↔162 | |||||
Sequence: CLKDRKDFGFPQEKVDAQQIKKAQAIPVLSELTQQILNIFTSKDSSAAWNTTLLDSFCNDLHQQLNDLQGCLMQQVGVQEFPLTQEDALLAVRKYFHRITVYLREKKHSPC | ||||||
Glycosylation | 101 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length189
- Mass (Da)21,646
- Last updated2011-02-08 v2
- ChecksumD6F4BC96DCE7D67E
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 14 | in Ref. 1; no nucleotide entry and 2; CAA26006 | ||||
Sequence: L → M | ||||||
Sequence conflict | 102 | in Ref. 1; no nucleotide entry and 2; CAA26006 | ||||
Sequence: T → A | ||||||
Sequence conflict | 126 | in Ref. 6; AA sequence | ||||
Sequence: Q → E | ||||||
Sequence conflict | 132 | in Ref. 6; AA sequence | ||||
Sequence: F → P | ||||||
Sequence conflict | 139 | in Ref. 6; AA sequence | ||||
Sequence: A → Y | ||||||
Sequence conflict | 145 | in Ref. 6; AA sequence | ||||
Sequence: K → T | ||||||
Sequence conflict | 175 | in Ref. 6; AA sequence | ||||
Sequence: L → M | ||||||
Sequence conflict | 180-181 | in Ref. 6; AA sequence | ||||
Sequence: NV → KL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X01974 EMBL· GenBank· DDBJ | CAA26006.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY225950 EMBL· GenBank· DDBJ | AAO63592.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX530016 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466527 EMBL· GenBank· DDBJ | EDL30958.1 EMBL· GenBank· DDBJ | Genomic DNA |