P38444 · AVR2A_RAT
- ProteinActivin receptor type-2A
- GeneAcvr2a
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids513 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A. Mediates induction of adipogenesis by GDF6.
Catalytic activity
- ATP + L-threonyl-[receptor-protein] = ADP + H+ + O-phospho-L-threonyl-[receptor-protein]This reaction proceeds in the forward direction.
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameActivin receptor type-2A
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP38444
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 20-135 | Extracellular | ||||
Sequence: AILGRSETQECLFFNANWERDRTNQTGVEPCYGDKDKRRHCFATWKNISGSIEIVKQGCWLDDINCYDRTDCIEKKDSPEVYFCCCEGNMCNEKFSYFPEMEVTQPTSNPVTPKPP | ||||||
Transmembrane | 136-161 | Helical | ||||
Sequence: YYNILLYSLVPLMLIAGIVICAFWVY | ||||||
Topological domain | 162-513 | Cytoplasmic | ||||
Sequence: RHHMMAYPPVLVPTQDPGPPPPSPLLGLKPLQLLEVKARGRFGCVWKAQLLNEYVAVKIFPIQDKQSWQNEYEVYSLPGMKHENILQFIGAEKRGTSVDVDLWLITAFHEKGSLSDFLKANVVSWNELCHIAETMARGLAYLHEDIPGLKDGHKPAISHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSGGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELASRCTAADGPVDEYMLPFEEEIGQHPSLEDMQEVVVHKKKRPVLRDYWQKHAGMAMLCETIEECWDHDAEARLSAGCLGERITQMQRLTNIITTEDIVTVVTMVTNVDFPPKESSL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MGAAAKLAFAVFLISCSSG | ||||||
Chain | PRO_0000024401 | 20-513 | Activin receptor type-2A | |||
Sequence: AILGRSETQECLFFNANWERDRTNQTGVEPCYGDKDKRRHCFATWKNISGSIEIVKQGCWLDDINCYDRTDCIEKKDSPEVYFCCCEGNMCNEKFSYFPEMEVTQPTSNPVTPKPPYYNILLYSLVPLMLIAGIVICAFWVYRHHMMAYPPVLVPTQDPGPPPPSPLLGLKPLQLLEVKARGRFGCVWKAQLLNEYVAVKIFPIQDKQSWQNEYEVYSLPGMKHENILQFIGAEKRGTSVDVDLWLITAFHEKGSLSDFLKANVVSWNELCHIAETMARGLAYLHEDIPGLKDGHKPAISHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSGGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELASRCTAADGPVDEYMLPFEEEIGQHPSLEDMQEVVVHKKKRPVLRDYWQKHAGMAMLCETIEECWDHDAEARLSAGCLGERITQMQRLTNIITTEDIVTVVTMVTNVDFPPKESSL | ||||||
Disulfide bond | 30↔60 | |||||
Sequence: CLFFNANWERDRTNQTGVEPCYGDKDKRRHC | ||||||
Glycosylation | 43 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 50↔78 | |||||
Sequence: CYGDKDKRRHCFATWKNISGSIEIVKQGC | ||||||
Glycosylation | 66 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 85↔104 | |||||
Sequence: CYDRTDCIEKKDSPEVYFCC | ||||||
Disulfide bond | 91↔103 | |||||
Sequence: CIEKKDSPEVYFC | ||||||
Disulfide bond | 105↔110 | |||||
Sequence: CEGNMC |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Part of a complex consisting of MAGI2/ARIP1, ACVR2A, ACVR1B and SMAD3 (By similarity).
Interacts with MAGI2/ARIP1 (By similarity).
Interacts with type I receptor ACVR1 (By similarity).
Interacts with BMP7 (By similarity).
Interacts with TSC22D1/TSC-22 (By similarity).
Interacts with MAGI2/ARIP1 (By similarity).
Interacts with type I receptor ACVR1 (By similarity).
Interacts with BMP7 (By similarity).
Interacts with TSC22D1/TSC-22 (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 192-485 | Protein kinase | ||||
Sequence: LQLLEVKARGRFGCVWKAQLLNEYVAVKIFPIQDKQSWQNEYEVYSLPGMKHENILQFIGAEKRGTSVDVDLWLITAFHEKGSLSDFLKANVVSWNELCHIAETMARGLAYLHEDIPGLKDGHKPAISHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSGGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELASRCTAADGPVDEYMLPFEEEIGQHPSLEDMQEVVVHKKKRPVLRDYWQKHAGMAMLCETIEECWDHDAEARLSAGCLGERITQMQRL |
Sequence similarities
Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length513
- Mass (Da)57,893
- Last updated1994-10-01 v1
- ChecksumCE3A8742EF91DD7D
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I5ZYE8 | A0A8I5ZYE8_RAT | Acvr2a | 518 | ||
F1MA24 | F1MA24_RAT | Acvr2a | 521 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 165 | in Ref. 2; AAB23958 | ||||
Sequence: M → K | ||||||
Sequence conflict | 218 | in Ref. 2; AAB23958 | ||||
Sequence: V → I | ||||||
Sequence conflict | 353 | in Ref. 2; AAB23958 | ||||
Sequence: G → A | ||||||
Sequence conflict | 475 | in Ref. 2; AAB23958 | ||||
Sequence: L → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
S48190 EMBL· GenBank· DDBJ | AAB23958.1 EMBL· GenBank· DDBJ | mRNA | ||
L10639 EMBL· GenBank· DDBJ | AAA40674.1 EMBL· GenBank· DDBJ | mRNA |