ID ACVR1_BOVIN Reviewed; 509 AA. AC Q28041; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 08-NOV-2023, entry version 153. DE RecName: Full=Activin receptor type-1; DE EC=2.7.11.30; DE AltName: Full=Activin receptor type I; DE Short=ACTR-I; DE AltName: Full=Serine/threonine-protein kinase receptor R1; DE Short=SKR1; DE Flags: Precursor; GN Name=ACVR1; Synonyms=ACVRLK2; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Ethier J.-F., Lussier J.G., Daneau I., Silversides D.W.; RT "Bovine activin receptor type I can be expressed as a kinase-domain RT truncated receptor."; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Bone morphogenetic protein (BMP) type I receptor that is CC involved in a wide variety of biological processes, including bone, CC heart, cartilage, nervous, and reproductive system development and CC regulation. As a type I receptor, forms heterotetrameric receptor CC complexes with the type II receptors AMHR2, ACVR2A ors ACVR2B. Upon CC binding of ligands such as BMP7 or BMP9 to the heteromeric complexes, CC type II receptors transphosphorylate ACVR1 intracellular domain. In CC turn, ACVR1 kinase domain is activated and subsequently phosphorylates CC SMAD1/5/8 proteins that transduce the signal. In addition to its role CC in mediating BMP pathway-specific signaling, suppresses TGFbeta/activin CC pathway signaling by interfering with the binding of activin to its CC type II receptor. Besides canonical SMAD signaling, can activate non- CC canonical signaling pathways. May promote the expression of HAMP, CC potentially via its interaction with BMP6 (By similarity). CC {ECO:0000250|UniProtKB:P37172, ECO:0000250|UniProtKB:Q04771}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho- CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA- CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, CC ChEBI:CHEBI:456216; EC=2.7.11.30; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L- CC seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022, CC Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; CC EC=2.7.11.30; Evidence={ECO:0000250|UniProtKB:Q04771}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC -!- SUBUNIT: Interacts with FKBP1A (By similarity). Interacts with FCHO1 CC (By similarity). Interacts with CLU. Interacts with type II receptors CC AMHR2 and ACVR2A (By similarity). Interacts with BMP7 (By similarity). CC Interacts with BMP9 (By similarity). Interacts with BMP6 (when CC glycosylated); the interaction may induce HAMP expression (By CC similarity). Interacts with TSC22D1/TSC-22 (By similarity). CC {ECO:0000250|UniProtKB:P37172, ECO:0000250|UniProtKB:Q04771}. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U58095; AAB02696.1; -; mRNA. DR AlphaFoldDB; Q28041; -. DR SMR; Q28041; -. DR STRING; 9913.ENSBTAP00000015797; -. DR GlyCosmos; Q28041; 1 site, No reported glycans. DR PaxDb; 9913-ENSBTAP00000015797; -. DR eggNOG; KOG2052; Eukaryota. DR InParanoid; Q28041; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0048179; C:activin receptor complex; ISS:AgBase. DR GO; GO:0070724; C:BMP receptor complex; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; ISS:AgBase. DR GO; GO:0016361; F:activin receptor activity, type I; ISS:AgBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046332; F:SMAD binding; IBA:GO_Central. DR GO; GO:0050431; F:transforming growth factor beta binding; ISS:AgBase. DR GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IBA:GO_Central. DR GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central. DR GO; GO:0007368; P:determination of left/right symmetry; ISS:AgBase. DR GO; GO:0009953; P:dorsal/ventral pattern formation; IBA:GO_Central. DR GO; GO:0007281; P:germ cell development; ISS:AgBase. DR GO; GO:0007507; P:heart development; ISS:AgBase. DR GO; GO:0001701; P:in utero embryonic development; ISS:AgBase. DR GO; GO:0001755; P:neural crest cell migration; ISS:AgBase. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:AgBase. DR GO; GO:0001655; P:urogenital system development; ISS:AgBase. DR CDD; cd14142; STKc_ACVR1_ALK1; 1. DR Gene3D; 2.10.60.10; CD59; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000472; Activin_recp. DR InterPro; IPR003605; GS_dom. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR045860; Snake_toxin-like_sf. DR InterPro; IPR000333; TGFB_receptor. DR PANTHER; PTHR23255:SF69; ACTIVIN RECEPTOR TYPE-1; 1. DR PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1. DR Pfam; PF01064; Activin_recp; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF08515; TGF_beta_GS; 1. DR PRINTS; PR00653; ACTIVIN2R. DR SMART; SM00467; GS; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF57302; Snake toxin-like; 1. DR PROSITE; PS51256; GS; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 2: Evidence at transcript level; KW ATP-binding; Glycoprotein; Kinase; Magnesium; Manganese; Membrane; KW Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor; KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..20 FT /evidence="ECO:0000250" FT CHAIN 21..509 FT /note="Activin receptor type-1" FT /id="PRO_0000024393" FT TOPO_DOM 21..123 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 124..146 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 147..509 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 178..207 FT /note="GS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00585" FT DOMAIN 208..502 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT ACT_SITE 336 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 214..222 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 235 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 501 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q04771" FT CARBOHYD 102 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 509 AA; 57190 MW; 365B9D4A518773FB CRC64; MVDGVMILPV LVMIAFPFPS MEDEKPKVNP KLYMCVCEGL SCGDEAHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLEVGLIILS VVFAVCLLAC LLGVALRKFK RRNQERLNPR DVEYGTIEGL ITTNVGDSTL ADLLDHSCTS GSGSGLPFLV QRTVARQITL LECVGKGRYG EVWRGSWQGE NVAVKIFSSR DEKSWFRETE LYNTVMLRHE NILGFIASDM TSRHSSTQLW LITHYHEMGS LYDYLQLTTL DTVSCLRIVL SIASGLAHLH IEIFGTQGKP AIAHRDLKSK NILVKKNGQC CIADLGLAVM HSQSTNQLDV GNNPRVGTKR YMAPEVLDET IQVDCFDSYK RVDIWAFGLV LWEVARRMVS NGIVEDYKPP FYDVVPNDPS FEDMRKVVCV DQQRPNIPNR WFSDPTLTSL AKLMKECWYQ NPSARLTALR IKKTLTKIDN SLDKLKTDC //