P09006 · SPA3N_RAT
- ProteinSerine protease inhibitor A3N
- GeneSerpina3n
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids418 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
Miscellaneous
The single human alpha1-antichymotrypsin gene (SERPINA3) is represented by a cluster of 6 individual rat paralogs.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 381-382 | Reactive bond | ||||
Sequence: MS |
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 | serine-type endopeptidase inhibitor activity | |
Biological Process | cellular response to cAMP | |
Biological Process | cellular response to glucocorticoid stimulus | |
Biological Process | cellular response to interleukin-1 | |
Biological Process | cellular response to interleukin-6 | |
Biological Process | cellular response to type II interferon | |
Biological Process | response to bacterium | |
Biological Process | response to cytokine | |
Biological Process | response to lipopolysaccharide | |
Biological Process | response to peptide hormone | |
Biological Process | response to vitamin B6 |
Keywords
- Molecular function
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSerine protease inhibitor A3N
- Short namesSerpin A3N
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP09006
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-29 | |||||
Sequence: MTRLVTLELLMAGIGSALLCFPDCILGED | ||||||
Chain | PRO_0000032423 | 30-418 | Serine protease inhibitor A3N | |||
Sequence: TLFHEDQDKGTQLDSLTLASINTDFAFSLYKKLALRNPDKNVVFSPLSISAALAVVSLGAKGNSMEEILEGLKFNLTETPETEIHRGFGHLLQRLSQPRDEIQISTGNALFIEKRLQVLAEFQEKAKALYQAEAFTADFQQSREAKKLINDYVSKQTQGKIQGLITNLAKKTSMVLVNYIYFKGKWKVPFDPRDTFQSEFYSGKRRPVKVPMMKLEDLTTPYVRDEELNCTVVELKYTGNASALFILPDQGKMQQVEASLQPETLRRWKDSLRPSMIDELYLPKFSISADYNLEDVLPELGIKEVFSTQADLSGITGDKDLMVSQVVHKAVLDVAETGTEAAAATGVKFVPMSAKLDPLIIAFDRPFLMIISDTETAIAPFLAKIFNPK | ||||||
Modified residue | 93 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 104 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 258 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 269 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Liver.
Induction
By acute inflammation.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 367-394 | RCL | ||||
Sequence: GTEAAAATGVKFVPMSAKLDPLIIAFDR |
Domain
The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the serpin reactive site and the protease. The resulting inactive serpin-protease complex is highly stable (By similarity).
Variability within the reactive center loop (RCL) sequences of Serpina3 paralogs may determine target protease specificity
Variability within the reactive center loop (RCL) sequences of Serpina3 paralogs may determine target protease specificity
Sequence similarities
Belongs to the serpin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length418
- Mass (Da)46,652
- Last updated1997-11-01 v3
- ChecksumAADEFF087190B44F
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 12 | in Ref. 3; CAA34408 | ||||
Sequence: A → D | ||||||
Sequence conflict | 20 | in Ref. 3; CAA34408 | ||||
Sequence: C → S | ||||||
Sequence conflict | 68 | in Ref. 3; CAA34408 | ||||
Sequence: D → H | ||||||
Sequence conflict | 92 | in Ref. 3; CAA34408 | ||||
Sequence: N → S | ||||||
Sequence conflict | 236 | in Ref. 3; CAA34408 | ||||
Sequence: P → S | ||||||
Sequence conflict | 323 | in Ref. 4; CAA31548 | ||||
Sequence: E → EE | ||||||
Sequence conflict | 334 | in Ref. 4; CAA31548 | ||||
Sequence: V → A | ||||||
Sequence conflict | 353 | in Ref. 3; CAA34408 | ||||
Sequence: S → F | ||||||
Sequence conflict | 354 | in Ref. 4; CAA31548 | ||||
Sequence: Q → E | ||||||
Sequence conflict | 381 | in Ref. 4; CAA31548 | ||||
Sequence: M → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X16359 EMBL· GenBank· DDBJ | CAA34408.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
D00753 EMBL· GenBank· DDBJ | BAA00650.1 EMBL· GenBank· DDBJ | mRNA | ||
BC078796 EMBL· GenBank· DDBJ | AAH78796.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
X13150 EMBL· GenBank· DDBJ | CAA31548.1 EMBL· GenBank· DDBJ | mRNA |