P20848 · A1ATR_HUMAN
- ProteinAlpha-1-antitrypsin-related protein
- GeneSERPINA2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids421 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Putative serine protease inhibitor.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 385-386 | Reactive bond | ||||
Sequence: WS |
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 | endoplasmic reticulum | |
Cellular Component | extracellular space | |
Molecular Function | serine-type endopeptidase inhibitor activity |
Keywords
- Molecular function
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-1-antitrypsin-related protein
- Short namesAAT-related protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP20848
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_070190 | 330 | in allele V1 and allele V3 | |||
Sequence: L → P | ||||||
Natural variant | VAR_070191 | 342 | in allele V1 | |||
Sequence: E → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 239 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MPFSVSWGILLLAGLCCLVPS | ||||||
Chain | PRO_0000032410 | 22-421 | Alpha-1-antitrypsin-related protein | |||
Sequence: SLVEDPQEDAAQKTDTSHHDQGDWEDLACQKISYNVTDLAFDLYKELADLSQTSNVLVTPTSVAMAFAMLSLGTKADTRTEILEGLNVNLTETPEAKIHECFQQVLQALSRPDTRLQLTTGSSLFVNKSMKLVDTFLEDTKKLYHSEASSINFRDTEEAKEQINNYVEKRTGRKVVDLVKHLKKDTSLALVDYISFHGKWKDKFKAEHIMVEGFHVDDKTIIRVPMINHLGRFDIHRDRELSSWVLAQHYVGNATAFFILPDPKKMWQLEEKLTYSHLENIQRAFDIRSINLHFPKLSISGTYKLKRVLRNLGITKIFSNEADLSGVSQEAPLKLSKAVHVAVLTIDEKGTEATGAPHLEEKAWSKYQTVMFNRPFLVIIKDDITNFPLFIGKVVNPTQK | ||||||
Glycosylation | 56 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 110 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 148 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 274 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the liver, leukocytes and testis. Also detected in brain, colon, uterus, esophagus, spleen, trachea, kidney and lung.
Structure
Family & Domains
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 carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable (By similarity).
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.
- Length421
- Mass (Da)47,707
- Last updated2022-08-03 v2
- Checksum33A46EF9896FC91D
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0U1RQB8 | A0A0U1RQB8_HUMAN | SERPINA2 | 309 | ||
A0A0G2JS25 | A0A0G2JS25_HUMAN | SERPINA2 | 64 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 9 | in Ref. 1; AAA51544 and 2; AGI62067 | ||||
Sequence: I → V | ||||||
Sequence conflict | 29 | in Ref. 1; AAA51544 | ||||
Sequence: E → G | ||||||
Sequence conflict | 67-76 | in Ref. 1; AAA51544 | ||||
Sequence: ELADLSQTSN → SWLIYHNQH | ||||||
Sequence conflict | 89 | in Ref. 1; AAA51544 | ||||
Sequence: A → R | ||||||
Sequence conflict | 229 | in Ref. 1; AAA51544 and 2; AGI62067 | ||||
Sequence: H → R | ||||||
Sequence conflict | 403-404 | in Ref. 1; AAA51544 | ||||
Sequence: DD → EY |
Polymorphism
The SERPINA2 gene is highly polymorphic. Deletions, frameshift mutations and a critical start codon variation (ATG->ATA, dbSNP:rs1956172) have been found in some populations. Population studies suggest that a pseudogenization process may be ongoing in humans (PubMed:17135331, PubMed:23826168, PubMed:9383284).
3 potentially functional alleles, V1, V2 and V3, have been described in the literature. The sequence shown in this entry is that of allele V2 (PubMed:23826168).
3 potentially functional alleles, V1, V2 and V3, have been described in the literature. The sequence shown in this entry is that of allele V2 (PubMed:23826168).
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M19684 EMBL· GenBank· DDBJ | AAA51544.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M19685 EMBL· GenBank· DDBJ | AAA51544.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JX680599 EMBL· GenBank· DDBJ | AGI62067.1 EMBL· GenBank· DDBJ | mRNA | ||
AC235087 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |