ACVR1_CHICK
ID ACVR1_CHICK Reviewed; 504 AA.
AC Q90ZK6; Q9YH45;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Activin receptor type-1;
DE EC=2.7.11.30;
DE AltName: Full=Activin receptor type I;
DE AltName: Full=Type I TGF B receptor;
DE Flags: Precursor;
GN Name=ACVR1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Leghorn; TISSUE=Heart;
RA Brames G.P., Barnett J.V.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Derco brown;
RA Kuchler K.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: On ligand binding, forms a receptor complex consisting of two
CC type II and two type I transmembrane serine/threonine kinases. Type II
CC receptors phosphorylate and activate type I receptors which
CC autophosphorylate, then bind and activate SMAD transcriptional
CC regulators. Receptor for activin (By similarity). {ECO:0000250}.
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;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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; U38622; AAC98806.1; -; mRNA.
DR EMBL; AJ318064; CAC39433.1; -; mRNA.
DR RefSeq; NP_989891.1; NM_204560.1.
DR RefSeq; XP_015145616.1; XM_015290130.1.
DR RefSeq; XP_015145617.1; XM_015290131.1.
DR RefSeq; XP_015145618.1; XM_015290132.1.
DR RefSeq; XP_015145619.1; XM_015290133.1.
DR RefSeq; XP_015145620.1; XM_015290134.1.
DR AlphaFoldDB; Q90ZK6; -.
DR SMR; Q90ZK6; -.
DR STRING; 9031.ENSGALP00000020469; -.
DR PaxDb; Q90ZK6; -.
DR GeneID; 395246; -.
DR KEGG; gga:395246; -.
DR CTD; 395246; -.
DR VEuPathDB; HostDB:geneid_395246; -.
DR eggNOG; KOG2052; Eukaryota.
DR HOGENOM; CLU_000288_8_5_1; -.
DR InParanoid; Q90ZK6; -.
DR PhylomeDB; Q90ZK6; -.
DR PRO; PR:Q90ZK6; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0048179; C:activin receptor complex; ISA:AgBase.
DR GO; GO:0045177; C:apical part of cell; ISA:AgBase.
DR GO; GO:0070724; C:BMP receptor complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISA:AgBase.
DR GO; GO:0016020; C:membrane; IC:AgBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0048185; F:activin binding; ISA:AgBase.
DR GO; GO:0016361; F:activin receptor activity, type I; ISA:AgBase.
DR GO; GO:0005524; F:ATP binding; ISA:AgBase.
DR GO; GO:0019838; F:growth factor binding; ISA:AgBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISA:AgBase.
DR GO; GO:0004672; F:protein kinase activity; ISA:AgBase.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISA:AgBase.
DR GO; GO:0046332; F:SMAD binding; ISA:AgBase.
DR GO; GO:0050431; F:transforming growth factor beta binding; IPI:AgBase.
DR GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IDA:AgBase.
DR GO; GO:0032924; P:activin receptor signaling pathway; IDA:AgBase.
DR GO; GO:0002526; P:acute inflammatory response; ISA:AgBase.
DR GO; GO:0003289; P:atrial septum primum morphogenesis; ISA:AgBase.
DR GO; GO:0003181; P:atrioventricular valve morphogenesis; ISS:AgBase.
DR GO; GO:0030509; P:BMP signaling pathway; ISA:AgBase.
DR GO; GO:0061312; P:BMP signaling pathway involved in heart development; ISS:AgBase.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISA:AgBase.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IMP:AgBase.
DR GO; GO:0060923; P:cardiac muscle cell fate commitment; ISA:AgBase.
DR GO; GO:0016477; P:cell migration; IMP:AgBase.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISA:AgBase.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0007368; P:determination of left/right symmetry; ISA:AgBase.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IBA:GO_Central.
DR GO; GO:0003143; P:embryonic heart tube morphogenesis; ISA:AgBase.
DR GO; GO:0061445; P:endocardial cushion cell fate commitment; ISA:AgBase.
DR GO; GO:0003274; P:endocardial cushion fusion; ISS:AgBase.
DR GO; GO:0003203; P:endocardial cushion morphogenesis; ISS:AgBase.
DR GO; GO:0042118; P:endothelial cell activation; IMP:AgBase.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISA:AgBase.
DR GO; GO:0007369; P:gastrulation; ISA:AgBase.
DR GO; GO:0001702; P:gastrulation with mouth forming second; ISA:AgBase.
DR GO; GO:0007281; P:germ cell development; ISA:AgBase.
DR GO; GO:0007507; P:heart development; IMP:AgBase.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:AgBase.
DR GO; GO:0048762; P:mesenchymal cell differentiation; IMP:AgBase.
DR GO; GO:0007498; P:mesoderm development; ISA:AgBase.
DR GO; GO:0001707; P:mesoderm formation; ISA:AgBase.
DR GO; GO:0003183; P:mitral valve morphogenesis; ISA:AgBase.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISA:AgBase.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISA:AgBase.
DR GO; GO:0009968; P:negative regulation of signal transduction; ISA:AgBase.
DR GO; GO:0001755; P:neural crest cell migration; ISA:AgBase.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISA:AgBase.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISA:AgBase.
DR GO; GO:0060037; P:pharyngeal system development; ISA:AgBase.
DR GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; IMP:AgBase.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IDA:AgBase.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISA:AgBase.
DR GO; GO:0030335; P:positive regulation of cell migration; ISA:AgBase.
DR GO; GO:2000017; P:positive regulation of determination of dorsal identity; ISA:AgBase.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:AgBase.
DR GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:AgBase.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISA:AgBase.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISA:AgBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISA:AgBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:AgBase.
DR GO; GO:0006468; P:protein phosphorylation; ISA:AgBase.
DR GO; GO:0030278; P:regulation of ossification; ISA:AgBase.
DR GO; GO:0051145; P:smooth muscle cell differentiation; ISA:AgBase.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:AgBase.
DR GO; GO:0060412; P:ventricular septum morphogenesis; ISS:AgBase.
DR Gene3D; 2.10.60.10; -; 1.
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; 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; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..504
FT /note="Activin receptor type-1"
FT /id="PRO_0000253593"
FT TOPO_DOM 17..119
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 173..202
FT /note="GS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00585"
FT DOMAIN 203..497
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 331
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 209..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 211..212
FT /note="KG -> SN (in Ref. 2; AAC98806)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 56225 MW; C7F045D6A25A071E CRC64;
MALPVLLLLL ALPSRSVQDE ELKLNECVCE GMSCGNGDRC QGQQCFASLS INDGAKVYQK
GCFQVYEQGK MTCKTPPSPD QAVECCQGYL CNMNITAKLP SSKGQTLQGE AAGYSMETLI
IVILAPVVVL VIFSVVAVLI IRRIQKNHME RLNSRDAEYG TIEGLIASNV GDSTLADLLD
HSCTSGSGSG LPFLVQRTVA RQITLVECVG KGRYGEVWRG QWQGENVAVK IFSSRDEKSW
FRETELYNTV LLRHENILGF IASDMTSRNS STQLWLITHY HEMGSLYDYL QLTTLDTVSC
LRIVLSIASG LAHLHIEIFG TQGKPAISHR DLKSKNILVK KNGQCCIADL GLAVMHSQST
NQLDVGNNPR VGTKRYMAPE VLDETIQADC FDSYKRVDIW AFGLVLWEVA RRMVSNGIVE
DYKPPFYDLV PNDPSFEDMR KVVCVDQQRP NIPNRWFSDP TLTSLAKLMK ECWYQNPSAR
LTALRIKKTL TKIDNSLDKL KADC
