ID ACVL1_PONAB Reviewed; 503 AA. AC Q5RAN0; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 105. DE RecName: Full=Serine/threonine-protein kinase receptor R3; DE Short=SKR3; DE EC=2.7.11.30; DE AltName: Full=Activin receptor-like kinase 1; DE Short=ALK-1; DE Flags: Precursor; GN Name=ACVRL1; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Type I receptor for TGF-beta family ligands BMP9/GDF2 and CC BMP10 and important regulator of normal blood vessel development. On CC ligand binding, forms a receptor complex consisting of two type II and CC two type I transmembrane serine/threonine kinases. Type II receptors CC phosphorylate and activate type I receptors which autophosphorylate, CC then bind and activate SMAD transcriptional regulators. May bind CC activin as well (By similarity). {ECO:0000250|UniProtKB:P37023}. 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 -!- SUBUNIT: Interacts with TSC22D1/TSC-22. {ECO:0000250|UniProtKB:P37023}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P37023}; CC Single-pass type I membrane protein {ECO:0000255}. 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; CR858985; CAH91180.1; -; mRNA. DR RefSeq; NP_001125692.1; NM_001132220.1. DR AlphaFoldDB; Q5RAN0; -. DR BMRB; Q5RAN0; -. DR SMR; Q5RAN0; -. DR STRING; 9601.ENSPPYP00000005173; -. DR GlyCosmos; Q5RAN0; 1 site, No reported glycans. DR GeneID; 100172614; -. DR KEGG; pon:100172614; -. DR CTD; 94; -. DR eggNOG; KOG2052; Eukaryota. DR InParanoid; Q5RAN0; -. DR OrthoDB; 3900892at2759; -. DR Proteomes; UP000001595; Unplaced. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0098821; F:BMP receptor activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0009893; P:positive regulation of metabolic process; IEA:UniProt. DR GO; GO:0051239; P:regulation of multicellular organismal process; IEA:UniProt. DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt. 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; 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:SF66; SERINE_THREONINE-PROTEIN KINASE RECEPTOR R3; 1. DR PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 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 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 Angiogenesis; ATP-binding; Cell membrane; Disulfide bond; Glycoprotein; KW Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding; KW Phosphoprotein; Receptor; Reference proteome; KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..503 FT /note="Serine/threonine-protein kinase receptor R3" FT /id="PRO_0000234418" FT TOPO_DOM 22..118 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 119..141 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 142..503 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 172..201 FT /note="GS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00585" FT DOMAIN 202..492 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 73..76 FT /note="Mediates specificity for BMP ligand" FT /evidence="ECO:0000250" FT ACT_SITE 330 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 208..216 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 229 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 155 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q61288" FT MOD_RES 160 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q61288" FT MOD_RES 161 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q61288" FT CARBOHYD 98 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 34..51 FT /evidence="ECO:0000250|UniProtKB:P37023" FT DISULFID 36..41 FT /evidence="ECO:0000250|UniProtKB:P37023" FT DISULFID 46..69 FT /evidence="ECO:0000250|UniProtKB:P37023" FT DISULFID 77..89 FT /evidence="ECO:0000250|UniProtKB:P37023" FT DISULFID 90..95 FT /evidence="ECO:0000250|UniProtKB:P37023" SQ SEQUENCE 503 AA; 56200 MW; 8339B39C42688060 CRC64; MTLGSPRRGL LMLLMALVTQ GDPVKPSRGP LVTCTCESPH CRGPTCRGAW CTVVLVREEG RHPQEHRGCG NLHRELCRGR PTEFVNHYCC DSHLCNHNVS LVLEATQSPS EQPGTDGQLA LILGPVLALL ALVALGVLGL WHVRRRQEKQ RGLHSELGES SLILKASEQG DSMLGDLLDS DCTTGSGSGL PFLVQRTVAR QVALVECVGK GRYGEVWRGL WHGESVAVKI FSSRDEQSWF RETEIYNTVL LRHDNILGFI ASDMTSRNSS TQLWLITHYH EHGSLYDFLQ RQTLEPHLAL RLTVSAACGL AHLHVEIFGT QGKPAIAHRD FKSRNVLVKS NLQCCIADLG LAVMHSQGSD YLDIGNNPRV GTKRYMAPEV LDEQIRTDCF ESYKWTDIWA FGLVLWEIAR RTIVNGIVED YRPPFYDVVP NDPSFEDMKK VVCVDQQTPT IPNRLAADPV LSGLAQMMRE CWYPNPSARL TALRIKKTLQ KISNSPEKPK VIQ //