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Protein

Activin receptor type-1

Gene

Acvr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei235 – 2351ATPPROSITE-ProRule annotation
Active sitei336 – 3361Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi214 – 2229ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. activin binding Source: MGI
  2. activin receptor activity, type I Source: MGI
  3. ATP binding Source: MGI
  4. growth factor binding Source: MGI
  5. metal ion binding Source: UniProtKB-KW
  6. protein homodimerization activity Source: MGI
  7. protein kinase activity Source: MGI
  8. protein serine/threonine kinase activity Source: MGI
  9. receptor signaling protein serine/threonine kinase activity Source: Ensembl
  10. SMAD binding Source: MGI
  11. transforming growth factor beta binding Source: MGI
  12. transforming growth factor beta receptor activity, type I Source: MGI

GO - Biological processi

  1. activin receptor signaling pathway Source: MGI
  2. acute inflammatory response Source: UniProtKB
  3. atrial septum primum morphogenesis Source: MGI
  4. BMP signaling pathway Source: MGI
  5. cardiac muscle cell fate commitment Source: MGI
  6. cellular response to glucocorticoid stimulus Source: Ensembl
  7. determination of left/right symmetry Source: MGI
  8. embryonic heart tube morphogenesis Source: MGI
  9. endocardial cushion cell fate commitment Source: MGI
  10. G1/S transition of mitotic cell cycle Source: MGI
  11. gastrulation Source: MGI
  12. gastrulation with mouth forming second Source: MGI
  13. germ cell development Source: MGI
  14. heart development Source: MGI
  15. in utero embryonic development Source: MGI
  16. mesoderm development Source: MGI
  17. mesoderm formation Source: MGI
  18. mitral valve morphogenesis Source: MGI
  19. negative regulation of activin receptor signaling pathway Source: MGI
  20. negative regulation of extrinsic apoptotic signaling pathway Source: MGI
  21. negative regulation of signal transduction Source: MGI
  22. neural crest cell migration Source: MGI
  23. pathway-restricted SMAD protein phosphorylation Source: MGI
  24. patterning of blood vessels Source: MGI
  25. peptidyl-threonine phosphorylation Source: MGI
  26. pharyngeal system development Source: MGI
  27. positive regulation of bone mineralization Source: MGI
  28. positive regulation of determination of dorsal identity Source: MGI
  29. positive regulation of osteoblast differentiation Source: MGI
  30. positive regulation of pathway-restricted SMAD protein phosphorylation Source: MGI
  31. positive regulation of transcription, DNA-templated Source: MGI
  32. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  33. protein phosphorylation Source: MGI
  34. regulation of ossification Source: MGI
  35. regulation of skeletal muscle tissue development Source: Ensembl
  36. smooth muscle cell differentiation Source: MGI
  37. transforming growth factor beta receptor signaling pathway Source: MGI
  38. urogenital system development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Acvr1
Synonyms:Acvrlk2, Tgfb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:87911. Acvr1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 123103ExtracellularSequence AnalysisAdd
BLAST
Transmembranei124 – 14623HelicalSequence AnalysisAdd
BLAST
Topological domaini147 – 509363CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. activin receptor complex Source: MGI
  2. apical part of cell Source: MGI
  3. integral component of plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020By similarityAdd
BLAST
Chaini21 – 509489Activin receptor type-1PRO_0000024395Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
Modified residuei501 – 5011PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP37172.
PRIDEiP37172.

PTM databases

PhosphoSiteiP37172.

Expressioni

Tissue specificityi

Expressed in normal parenchymal cells, endothelial cells, fibroblasts and tumor-derived epithelial cells.

Developmental stagei

Highly expressed in the node and midline and weakly expressed in E8.5 embryos and in the lateral plate mesoderm.1 Publication

Gene expression databases

BgeeiP37172.
CleanExiMM_ACVR1.
MM_TGFB1.
ExpressionAtlasiP37172. baseline and differential.
GenevestigatoriP37172.

Interactioni

Subunit structurei

Interacts with FKBP1A. Interacts with FCHO1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi197953. 3 interactions.
DIPiDIP-5798N.
MINTiMINT-1341279.

Structurei

3D structure databases

ProteinModelPortaliP37172.
SMRiP37172. Positions 158-499.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini178 – 20730GSPROSITE-ProRule annotationAdd
BLAST
Domaini208 – 502295Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 GS domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118876.
HOGENOMiHOG000230587.
HOVERGENiHBG054502.
InParanoidiP37172.
KOiK04675.
OMAiVCEGMSC.
OrthoDBiEOG7Q8CN3.
PhylomeDBiP37172.
TreeFamiTF314724.

Family and domain databases

InterProiIPR000472. 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]
PANTHERiPTHR23255. PTHR23255. 1 hit.
PfamiPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
PRINTSiPR00653. ACTIVIN2R.
SMARTiSM00467. GS. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P37172-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDGVMILPV LMMMAFPSPS VEDEKPKVNQ KLYMCVCEGL SCGNEDHCEG
60 70 80 90 100
QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT CKTPPSPGQA VECCQGDWCN
110 120 130 140 150
RNITAQLPTK GKSFPGTQNF HLEVGLIILS VVFAVCLLAC ILGVALRKFK
160 170 180 190 200
RRNQERLNPR DVEYGTIEGL ITTNVGDSTL AELLDHSCTS GSGSGLPFLV
210 220 230 240 250
QRTVARQITL LECVGKGRYG EVWRGSWQGE NVAVKIFSSR DEKSWFRETE
260 270 280 290 300
LYNTVMLRHE NILGFIASDM TSRHSSTQLW LITHYHEMGS LYDYLQLTTL
310 320 330 340 350
DTVSCLRIVL SIASGLAHLH IEIFGTQGKS AIAHRDLKSK NILVKKNGQC
360 370 380 390 400
CIADLGLAVM HSQSTNQLDV GNNPRVGTKR YMAPEVLDET IQVDCFDSYK
410 420 430 440 450
RVDIWAFGLV LWEVARRMVS NGIVEDYKPP FYDVVPNDPS FEDMRKVVCV
460 470 480 490 500
DQQRPNIPNR WFSDPTLTSL AKLMKECWYQ NPSARLTALR IKKTLTKIDN

SLDKLKTDC
Length:509
Mass (Da):57,226
Last modified:October 17, 2006 - v2
Checksum:i05BCFC22C5740028
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271K → E in BAE29239 (PubMed:16141072).Curated
Sequence conflicti27 – 271K → E in BAE29286 (PubMed:16141072).Curated
Sequence conflicti60 – 601N → Y in AAA40495 (PubMed:8388127).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16050.1.
PIRiA37489. I59576.
RefSeqiNP_001103674.1. NM_001110204.1.
NP_001103675.1. NM_001110205.1.
NP_031420.2. NM_007394.3.
XP_006497685.1. XM_006497622.1.
UniGeneiMm.689.

Genome annotation databases

EnsembliENSMUST00000056376; ENSMUSP00000056784; ENSMUSG00000026836.
ENSMUST00000090935; ENSMUSP00000088453; ENSMUSG00000026836.
ENSMUST00000112599; ENSMUSP00000108218; ENSMUSG00000026836.
ENSMUST00000112601; ENSMUSP00000108220; ENSMUSG00000026836.
GeneIDi11477.
KEGGimmu:11477.
UCSCiuc008jss.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16050.1.
PIRiA37489. I59576.
RefSeqiNP_001103674.1. NM_001110204.1.
NP_001103675.1. NM_001110205.1.
NP_031420.2. NM_007394.3.
XP_006497685.1. XM_006497622.1.
UniGeneiMm.689.

3D structure databases

ProteinModelPortaliP37172.
SMRiP37172. Positions 158-499.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi197953. 3 interactions.
DIPiDIP-5798N.
MINTiMINT-1341279.

Chemistry

BindingDBiP37172.

PTM databases

PhosphoSiteiP37172.

Proteomic databases

PaxDbiP37172.
PRIDEiP37172.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056376; ENSMUSP00000056784; ENSMUSG00000026836.
ENSMUST00000090935; ENSMUSP00000088453; ENSMUSG00000026836.
ENSMUST00000112599; ENSMUSP00000108218; ENSMUSG00000026836.
ENSMUST00000112601; ENSMUSP00000108220; ENSMUSG00000026836.
GeneIDi11477.
KEGGimmu:11477.
UCSCiuc008jss.1. mouse.

Organism-specific databases

CTDi90.
MGIiMGI:87911. Acvr1.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118876.
HOGENOMiHOG000230587.
HOVERGENiHBG054502.
InParanoidiP37172.
KOiK04675.
OMAiVCEGMSC.
OrthoDBiEOG7Q8CN3.
PhylomeDBiP37172.
TreeFamiTF314724.

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.

Miscellaneous databases

ChiTaRSiAcvr1. mouse.
NextBioi278820.
PROiP37172.
SOURCEiSearch...

Gene expression databases

BgeeiP37172.
CleanExiMM_ACVR1.
MM_TGFB1.
ExpressionAtlasiP37172. baseline and differential.
GenevestigatoriP37172.

Family and domain databases

InterProiIPR000472. 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]
PANTHERiPTHR23255. PTHR23255. 1 hit.
PfamiPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
PRINTSiPR00653. ACTIVIN2R.
SMARTiSM00467. GS. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiACVR1_MOUSE
AccessioniPrimary (citable) accession number: P37172
Secondary accession number(s): Q3UDH5, Q91VF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 17, 2006
Last modified: March 4, 2015
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.