ID D3DPA4_HUMAN Unreviewed; 509 AA. AC D3DPA4; D3DPA5; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 24-JAN-2024, entry version 118. DE RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271}; DE EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271}; DE Flags: Fragment; GN Name=ACVR1 {ECO:0000313|EMBL:ALQ33343.1}; GN ORFNames=hCG_1811747 {ECO:0000313|EMBL:EAX11439.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:ALQ33343.1}; RN [1] {ECO:0000313|EMBL:EAX11439.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=11181995; DOI=10.1126/science.1058040; RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., RA Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H., RA Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., RA Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., RA McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., RA Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., RA Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., RA Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., RA Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., RA Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., RA Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., RA Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., RA Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., RA Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., RA Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., RA Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., RA Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., RA Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., RA Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., RA Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., RA Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., RA Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., RA McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., RA Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., RA Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., RA Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., RA Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., RA Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., RA Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., RA Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., RA Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., RA Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., RA Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., RA Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., RA Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., RA Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., RA Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.; RT "The sequence of the human genome."; RL Science 291:1304-1351(2001). RN [2] {ECO:0000313|EMBL:EAX11439.1} RP NUCLEOTIDE SEQUENCE. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ADL14509.1} RP NUCLEOTIDE SEQUENCE. RA Rieder M.J., Bertucci C., Stanaway I.B., Johnson E.J., Swanson J.E., RA Siegel D.L., da Ponte S.H., Igartua C., Patterson K., Nickerson D.A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:ALQ33343.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26871637; DOI=10.1016/j.cell.2016.01.029; RA Yang X., Coulombe-Huntington J., Kang S., Sheynkman G.M., Hao T., RA Richardson A., Sun S., Yang F., Shen Y.A., Murray R., Spirohn K., RA Begg B.E., Duran-Frigola M., MacWilliams A., Pevzner S.J., Zhong Q., RA Trigg S.A., Tam S., Ghamsari L., Sahni N., Yi S., Rodriguez M.D., RA Balcha D., Tan G., Costanzo M., Andrews B., Boone C., Zhou X.J., RA Salehi-Ashtiani K., Charloteaux B., Chen A., Calderwood M.A., Aloy P., RA Roth F.P., Hill D.E., Iakoucheva L.M., Xia Y., Vidal M.; RT "Widespread Expansion of Protein Interaction Capabilities by Alternative RT Splicing."; RL Cell 164:805-817(2016). 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:0000256|ARBA:ARBA00023945}; 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 Evidence={ECO:0000256|ARBA:ARBA00023948, CC ECO:0000256|RuleBase:RU361271}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU361271}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|RuleBase:RU361271}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479, CC ECO:0000256|RuleBase:RU361271}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr CC protein kinase family. TGFB receptor subfamily. CC {ECO:0000256|ARBA:ARBA00009605, ECO:0000256|RuleBase:RU361271}. 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; HM015588; ADL14509.1; -; Genomic_DNA. DR EMBL; KU177885; ALQ33343.1; -; mRNA. DR EMBL; CH471058; EAX11439.1; -; Genomic_DNA. DR RefSeq; NP_001096.1; NM_001105.4. DR RefSeq; NP_001104537.1; NM_001111067.2. DR RefSeq; NP_001334592.1; NM_001347663.1. DR RefSeq; NP_001334593.1; NM_001347664.1. DR RefSeq; NP_001334594.1; NM_001347665.1. DR RefSeq; NP_001334595.1; NM_001347666.1. DR RefSeq; NP_001334596.1; NM_001347667.1. DR RefSeq; XP_006712888.1; XM_006712825.3. DR RefSeq; XP_011510410.1; XM_011512108.2. DR SMR; D3DPA4; -. DR Antibodypedia; 2371; 694 antibodies from 41 providers. DR DNASU; 90; -. DR GeneID; 90; -. DR KEGG; hsa:90; -. DR CTD; 90; -. DR VEuPathDB; HostDB:ENSG00000115170; -. DR HOGENOM; CLU_000288_8_5_1; -. DR OMA; VFERGCI; -. DR OrthoDB; 3900892at2759; -. DR BioGRID-ORCS; 90; 18 hits in 1201 CRISPR screens. DR ChiTaRS; ACVR1; human. DR GenomeRNAi; 90; -. DR ExpressionAtlas; D3DPA4; baseline and differential. DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl. DR GO; GO:0098802; C:plasma membrane signaling receptor complex; IEA:UniProt. DR GO; GO:0048185; F:activin binding; IEA:Ensembl. DR GO; GO:0016361; F:activin receptor activity, type I; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050431; F:transforming growth factor beta binding; IEA:Ensembl. DR GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IEA:Ensembl. DR GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl. DR GO; GO:0003289; P:atrial septum primum morphogenesis; IEA:Ensembl. DR GO; GO:0003181; P:atrioventricular valve morphogenesis; IEA:Ensembl. DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl. DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl. DR GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl. DR GO; GO:0003272; P:endocardial cushion formation; IEA:Ensembl. DR GO; GO:0003274; P:endocardial cushion fusion; IEA:Ensembl. DR GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl. DR GO; GO:0007281; P:germ cell development; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl. DR GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl. DR GO; GO:0060037; P:pharyngeal system development; IEA:Ensembl. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0062043; P:positive regulation of cardiac epithelial to mesenchymal transition; IEA:Ensembl. DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0051145; P:smooth muscle cell differentiation; IEA:Ensembl. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl. DR GO; GO:0060412; P:ventricular septum morphogenesis; IEA:Ensembl. 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000256|RuleBase:RU361271}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU361271}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU361271}; KW Membrane {ECO:0000256|RuleBase:RU361271}; KW Metal-binding {ECO:0000256|RuleBase:RU361271}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU361271}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|RuleBase:RU361271}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|RuleBase:RU361271}; KW Transmembrane {ECO:0000256|RuleBase:RU361271}; KW Transmembrane helix {ECO:0000256|RuleBase:RU361271}. FT SIGNAL 1..22 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 23..509 FT /note="Serine/threonine-protein kinase receptor" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5014302489" FT TRANSMEM 124..146 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361271" FT DOMAIN 178..207 FT /note="GS" FT /evidence="ECO:0000259|PROSITE:PS51256" FT DOMAIN 208..502 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 235 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" FT NON_TER 509 FT /evidence="ECO:0000313|EMBL:ALQ33343.1" SQ SEQUENCE 509 AA; 57153 MW; E2B0F051D19DD052 CRC64; MVDGVMILPV LIMIALPSPS MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG 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 //