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P37172 (ACVR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Activin receptor type-1

EC=2.7.11.30
Alternative name(s):
Activin receptor type I
Short name=ACTR-I
Serine/threonine-protein kinase receptor R1
Short name=SKR1
TGF-B superfamily receptor type I
Short name=TSR-I
TSK-7L
Gene names
Name:Acvr1
Synonyms:Acvrlk2, Tgfb1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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. May be involved in left-right pattern formation during embryogenesis. Ref.5

Catalytic activity

ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.

Cofactor

Magnesium or manganese By similarity.

Subunit structure

Interacts with FKBP1A. Interacts with FCHO1 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

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 E8.5 embryos and in the lateral plate mesoderm. Ref.5

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.

Contains 1 GS domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Serine/threonine-protein kinase
Transferase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from electronic annotation. Source: Ensembl

G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

acute inflammatory response

Inferred from expression pattern PubMed 12151307. Source: UniProtKB

atrial septum primum morphogenesis

Inferred from electronic annotation. Source: Ensembl

cardiac muscle cell fate commitment

Inferred from electronic annotation. Source: Ensembl

cellular response to glucocorticoid stimulus

Inferred from electronic annotation. Source: Ensembl

determination of left/right symmetry

Inferred from mutant phenotype Ref.5. Source: MGI

embryonic heart tube morphogenesis

Inferred from electronic annotation. Source: Ensembl

endocardial cushion cell fate commitment

Inferred from electronic annotation. Source: Ensembl

gastrulation

Inferred from mutant phenotype PubMed 10226013. Source: MGI

gastrulation with mouth forming second

Inferred from mutant phenotype PubMed 17117439. Source: MGI

germ cell development

Inferred from mutant phenotype PubMed 15289457. Source: MGI

heart development

Inferred from mutant phenotype PubMed 15226263PubMed 16140292PubMed 17078885. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 14729481PubMed 15037318PubMed 17117439. Source: MGI

mesoderm development

Inferred from mutant phenotype PubMed 17117439. Source: MGI

mesoderm formation

Inferred from mutant phenotype PubMed 10479450PubMed 17117439. Source: MGI

mitral valve morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of activin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

neural crest cell migration

Inferred from mutant phenotype PubMed 15226263. Source: MGI

pathway-restricted SMAD protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

patterning of blood vessels

Inferred from mutant phenotype PubMed 17078885. Source: MGI

peptidyl-threonine phosphorylation

Inferred from electronic annotation. Source: Ensembl

pharyngeal system development

Inferred from mutant phenotype PubMed 17078885. Source: MGI

positive regulation of bone mineralization

Inferred from electronic annotation. Source: Ensembl

positive regulation of determination of dorsal identity

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of pathway-restricted SMAD protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of skeletal muscle tissue development

Inferred from electronic annotation. Source: Ensembl

smooth muscle cell differentiation

Inferred from mutant phenotype PubMed 17078885. Source: MGI

transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 11376112. Source: MGI

urogenital system development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentactivin receptor complex

Inferred from electronic annotation. Source: Ensembl

apical part of cell

Inferred from direct assay PubMed 10704880PubMed 11290335. Source: MGI

integral component of plasma membrane

Inferred from direct assay PubMed 11376112. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

activin binding

Inferred from physical interaction PubMed 1646080PubMed 7577669. Source: MGI

activin receptor activity, type I

Inferred from direct assay PubMed 11376112. Source: MGI

growth factor binding

Inferred from direct assay Ref.1. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

receptor signaling protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta binding

Inferred from direct assay PubMed 12054694. Source: MGI

transforming growth factor beta receptor activity, type I

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Chain21 – 509489Activin receptor type-1
PRO_0000024395

Regions

Topological domain21 – 123103Extracellular Potential
Transmembrane124 – 14623Helical; Potential
Topological domain147 – 509363Cytoplasmic Potential
Domain178 – 20730GS
Domain208 – 502295Protein kinase
Nucleotide binding214 – 2229ATP By similarity

Sites

Active site3361Proton acceptor By similarity
Binding site2351ATP By similarity

Amino acid modifications

Modified residue5011Phosphoserine By similarity
Glycosylation1021N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict271K → E in BAE29239. Ref.3
Sequence conflict271K → E in BAE29286. Ref.3
Sequence conflict601N → Y in AAA40495. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P37172 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 05BCFC22C5740028

FASTA50957,226
        10         20         30         40         50         60 
MVDGVMILPV LMMMAFPSPS VEDEKPKVNQ KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN 

        70         80         90        100        110        120 
DGFHVYQKGC FQVYEQGKMT CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF 

       130        140        150        160        170        180 
HLEVGLIILS VVFAVCLLAC ILGVALRKFK RRNQERLNPR DVEYGTIEGL ITTNVGDSTL 

       190        200        210        220        230        240 
AELLDHSCTS GSGSGLPFLV QRTVARQITL LECVGKGRYG EVWRGSWQGE NVAVKIFSSR 

       250        260        270        280        290        300 
DEKSWFRETE LYNTVMLRHE NILGFIASDM TSRHSSTQLW LITHYHEMGS LYDYLQLTTL 

       310        320        330        340        350        360 
DTVSCLRIVL SIASGLAHLH IEIFGTQGKS AIAHRDLKSK NILVKKNGQC CIADLGLAVM 

       370        380        390        400        410        420 
HSQSTNQLDV GNNPRVGTKR YMAPEVLDET IQVDCFDSYK RVDIWAFGLV LWEVARRMVS 

       430        440        450        460        470        480 
NGIVEDYKPP FYDVVPNDPS FEDMRKVVCV DQQRPNIPNR WFSDPTLTSL AKLMKECWYQ 

       490        500 
NPSARLTALR IKKTLTKIDN SLDKLKTDC 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a type I TGF-beta receptor and its effect on TGF-beta binding to the type II receptor."
Ebner R., Chen H., Shum L., Lawler S., Lee A.L., Zioncheck T.F., Lopez A.R., Derynck R.
Science 260:1344-1348(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary gland.
[2]"High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ILS and ISS.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[5]"BMP signaling through ACVRI is required for left-right patterning in the early mouse embryo."
Kishigami S., Yoshikawa S., Castranio T., Okazaki K., Furuta Y., Mishina Y.
Dev. Biol. 276:185-193(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L15436 mRNA. Translation: AAA40495.1.
AF332087 mRNA. Translation: AAK56115.1.
AF332088 mRNA. Translation: AAK56116.1.
AK150014 mRNA. Translation: BAE29239.1.
AK150075 mRNA. Translation: BAE29286.1.
BC058718 mRNA. Translation: AAH58718.1.
CCDSCCDS16050.1.
PIRI59576. A37489.
RefSeqNP_001103674.1. NM_001110204.1.
NP_001103675.1. NM_001110205.1.
NP_031420.2. NM_007394.3.
XP_006497685.1. XM_006497622.1.
UniGeneMm.689.

3D structure databases

ProteinModelPortalP37172.
SMRP37172. Positions 158-499.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid197953. 3 interactions.
DIPDIP-5798N.
MINTMINT-1341279.

PTM databases

PhosphoSiteP37172.

Proteomic databases

PaxDbP37172.
PRIDEP37172.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000056376; ENSMUSP00000056784; ENSMUSG00000026836.
ENSMUST00000090935; ENSMUSP00000088453; ENSMUSG00000026836.
ENSMUST00000112599; ENSMUSP00000108218; ENSMUSG00000026836.
ENSMUST00000112601; ENSMUSP00000108220; ENSMUSG00000026836.
GeneID11477.
KEGGmmu:11477.
UCSCuc008jss.1. mouse.

Organism-specific databases

CTD90.
MGIMGI:87911. Acvr1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000110868.
HOGENOMHOG000230587.
HOVERGENHBG054502.
InParanoidP37172.
KOK04675.
OMAVCEGMSC.
OrthoDBEOG7Q8CN3.
PhylomeDBP37172.
TreeFamTF314724.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.

Gene expression databases

ArrayExpressP37172.
BgeeP37172.
CleanExMM_ACVR1.
MM_TGFB1.
GenevestigatorP37172.

Family and domain databases

InterProIPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR003605. TGF_beta_rcpt_GS.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERPTHR23255. PTHR23255. 1 hit.
PfamPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
PRINTSPR00653. ACTIVIN2R.
SMARTSM00467. GS. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACVR1. mouse.
NextBio278820.
PROP37172.
SOURCESearch...

Entry information

Entry nameACVR1_MOUSE
AccessionPrimary (citable) accession number: P37172
Secondary accession number(s): Q3UDH5, Q91VF1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot