ACVR1_BOVIN
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 03-AUG-2022, entry version 148.
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. {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. Interacts with FCHO1. Interacts with
CC CLU. Interacts with type II receptors AMHR2 and ACVR2A. Interacts with
CC BMP7. Interacts with BMP9. Interacts with BMP6.
CC {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}.
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DR EMBL; U58095; AAB02696.1; -; mRNA.
DR AlphaFoldDB; Q28041; -.
DR SMR; Q28041; -.
DR STRING; 9913.ENSBTAP00000015797; -.
DR PaxDb; Q28041; -.
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:0005887; C:integral component of plasma membrane; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
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:0006468; P:protein phosphorylation; IBA:GO_Central.
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 Gene3D; 2.10.60.10; -; 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; PTHR23255; 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; SSF56112; 1.
DR SUPFAM; SSF57302; SSF57302; 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
