P37172 · ACVR1_MOUSE

  • Protein
    Activin receptor type-1
  • Gene
    Acvr1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Bone morphogenetic protein (BMP) type I receptor that is involved in a wide variety of biological processes, including bone, heart, cartilage, nervous, and reproductive system development and regulation (PubMed:10479450, PubMed:15531373, PubMed:21945937).
As a type I receptor, forms heterotetrameric receptor complexes with the type II receptors AMHR2, ACVR2A ors ACVR2B. Upon binding of ligands such as BMP7 or BMP9 to the heteromeric complexes, type II receptors transphosphorylate ACVR1 intracellular domain. In turn, ACVR1 kinase domain is activated and subsequently phosphorylates SMAD1/5/8 proteins that transduce the signal. In addition to its role in mediating BMP pathway-specific signaling, suppresses TGFbeta/activin pathway signaling by interfering with the binding of activin to its type II receptor. Besides canonical SMAD signaling, can activate non-canonical pathways such as p38 mitogen-activated protein kinases/MAPKs (By similarity) (PubMed:10479450, PubMed:15531373, PubMed:21945937, PubMed:25413979).
May promote the expression of HAMP, potentially via its interaction with BMP6 (PubMed:31800957).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site214-222ATP (UniProtKB | ChEBI)
Binding site235ATP (UniProtKB | ChEBI)
Active site336Proton acceptor

GO annotations

AspectTerm
Cellular Componentactivin receptor complex
Cellular Componentapical part of cell
Cellular ComponentBMP receptor complex
Cellular Componentplasma membrane
Molecular Functionactivin binding
Molecular Functionactivin receptor activity, type I
Molecular FunctionATP binding
Molecular FunctionBMP receptor activity
Molecular Functioncadherin binding
Molecular Functiongrowth factor binding
Molecular Functionmetal ion binding
Molecular Functionprotein homodimerization activity
Molecular Functionprotein tyrosine kinase binding
Molecular FunctionSMAD binding
Molecular Functiontransforming growth factor beta binding
Molecular Functiontransforming growth factor beta receptor activity, type I
Biological Processacute inflammatory response
Biological Processatrial septum primum morphogenesis
Biological Processatrioventricular valve morphogenesis
Biological ProcessBMP signaling pathway
Biological Processbranching involved in blood vessel morphogenesis
Biological Processcardiac muscle cell fate commitment
Biological Processcellular response to growth factor stimulus
Biological Processdetermination of left/right symmetry
Biological Processdorsal/ventral pattern formation
Biological Processembryonic heart tube morphogenesis
Biological Processendocardial cushion cell fate commitment
Biological Processendocardial cushion formation
Biological Processendocardial cushion fusion
Biological Processgastrulation
Biological Processgastrulation with mouth forming second
Biological Processgerm cell development
Biological Processheart development
Biological Processin utero embryonic development
Biological Processmesoderm development
Biological Processmesoderm formation
Biological Processmitral valve morphogenesis
Biological Processnegative regulation of activin receptor signaling pathway
Biological Processnegative regulation of extrinsic apoptotic signaling pathway
Biological Processnegative regulation of G1/S transition of mitotic cell cycle
Biological Processneural crest cell migration
Biological Processpharyngeal system development
Biological Processpositive regulation of bone mineralization
Biological Processpositive regulation of cardiac epithelial to mesenchymal transition
Biological Processpositive regulation of cell migration
Biological Processpositive regulation of determination of dorsal identity
Biological Processpositive regulation of osteoblast differentiation
Biological Processpositive regulation of peptidyl-tyrosine phosphorylation
Biological Processpositive regulation of SMAD protein signal transduction
Biological Processpositive regulation of transcription by RNA polymerase II
Biological Processsmooth muscle cell differentiation
Biological Processtransforming growth factor beta receptor signaling pathway
Biological Processurogenital system development
Biological Processventricular septum morphogenesis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Activin receptor type-1
  • EC number
  • Alternative names
    • Activin receptor type I (ACTR-I)
    • Serine/threonine-protein kinase receptor R1 (SKR1)
    • TGF-B superfamily receptor type I (TSR-I)
    • TSK-7L

Gene names

    • Name
      Acvr1
    • Synonyms
      Acvrlk2, Tgfb1

Organism names

  • Taxonomic identifier
  • Strains
    • ILS
    • ISS
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P37172
  • Secondary accessions
    • Q3UDH5
    • Q91VF1

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain21-123Extracellular
Transmembrane124-146Helical
Topological domain147-509Cytoplasmic

Keywords

Phenotypes & Variants

Disruption phenotype

Deletion mutants show a recessive embryonic lethality. At 7.0 dpc, mutant embryos did not show any special abnormalities except a smaller size. However, at 8.0 dpc, mesoderm formation is initiated but its development is arrested around the mid/late streak stage (PubMed:10479450).
In an osteoblast-specific manner loss of BMP signaling via ACVR1 directs osteoblasts to increase endogenous bone mass (PubMed:21945937).
Additionally, mice lacking ACVR1 in cartilage show reduced SMAD responses, but also decreased p38 MAPK activation (PubMed:25413979).

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 20 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for signal, chain, glycosylation, modified residue.

TypeIDPosition(s)Description
Signal1-20
ChainPRO_000002439521-509Activin receptor type-1
Glycosylation102N-linked (GlcNAc...) asparagine
Modified residue501Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Highly expressed in bone during developmental stages (PubMed:21945937).
Expressed in normal parenchymal cells, endothelial cells, fibroblasts and tumor-derived epithelial cells

Developmental stage

Highly expressed in the node and midline and weakly expressed in 8.5 dpc embryos and in the lateral plate mesoderm.

Gene expression databases

Interaction

Subunit

Interacts with FKBP1A (By similarity).
Interacts with FCHO1 (By similarity).
Interacts with CLU. Interacts with type II receptors AMHR2 and ACVR2A (By similarity).
Interacts with BMP7 (By similarity).
Interacts with BMP9 (By similarity).
Interacts with BMP6 (when glycosylated); the interaction may induce HAMP expression (PubMed:31800957).
Interacts with TSC22D1/TSC-22 (By similarity).

Protein-protein interaction databases

Chemistry

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain178-207GS
Domain208-502Protein kinase

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    509
  • Mass (Da)
    57,226
  • Last updated
    2006-10-17 v2
  • Checksum
    05BCFC22C5740028
MVDGVMILPVLMMMAFPSPSVEDEKPKVNQKLYMCVCEGLSCGNEDHCEGQQCFSSLSINDGFHVYQKGCFQVYEQGKMTCKTPPSPGQAVECCQGDWCNRNITAQLPTKGKSFPGTQNFHLEVGLIILSVVFAVCLLACILGVALRKFKRRNQERLNPRDVEYGTIEGLITTNVGDSTLAELLDHSCTSGSGSGLPFLVQRTVARQITLLECVGKGRYGEVWRGSWQGENVAVKIFSSRDEKSWFRETELYNTVMLRHENILGFIASDMTSRHSSTQLWLITHYHEMGSLYDYLQLTTLDTVSCLRIVLSIASGLAHLHIEIFGTQGKSAIAHRDLKSKNILVKKNGQCCIADLGLAVMHSQSTNQLDVGNNPRVGTKRYMAPEVLDETIQVDCFDSYKRVDIWAFGLVLWEVARRMVSNGIVEDYKPPFYDVVPNDPSFEDMRKVVCVDQQRPNIPNRWFSDPTLTSLAKLMKECWYQNPSARLTALRIKKTLTKIDNSLDKLKTDC

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
B1AW87B1AW87_MOUSEAcvr1130

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict27in Ref. 3; BAE29239/BAE29286
Sequence conflict60in Ref. 1; AAA40495

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L15436
EMBL· GenBank· DDBJ
AAA40495.1
EMBL· GenBank· DDBJ
mRNA
AF332087
EMBL· GenBank· DDBJ
AAK56115.1
EMBL· GenBank· DDBJ
mRNA
AF332088
EMBL· GenBank· DDBJ
AAK56116.1
EMBL· GenBank· DDBJ
mRNA
AK150014
EMBL· GenBank· DDBJ
BAE29239.1
EMBL· GenBank· DDBJ
mRNA
AK150075
EMBL· GenBank· DDBJ
BAE29286.1
EMBL· GenBank· DDBJ
mRNA
BC058718
EMBL· GenBank· DDBJ
AAH58718.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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