ACVR1_MOUSE
ID ACVR1_MOUSE Reviewed; 509 AA.
AC P37172; Q3UDH5; Q91VF1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 198.
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 AltName: Full=TGF-B superfamily receptor type I;
DE Short=TSR-I;
DE AltName: Full=TSK-7L;
DE Flags: Precursor;
GN Name=Acvr1; Synonyms=Acvrlk2, Tgfb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=8388127; DOI=10.1126/science.8388127;
RA Ebner R., Chen H., Shum L., Lawler S., Lee A.L., Zioncheck T.F.,
RA Lopez A.R., Derynck R.;
RT "Cloning of a type I TGF-beta receptor and its effect on TGF-beta binding
RT to the type II receptor.";
RL Science 260:1344-1348(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10479450; DOI=10.1006/dbio.1999.9378;
RA Mishina Y., Crombie R., Bradley A., Behringer R.R.;
RT "Multiple roles for activin-like kinase-2 signaling during mouse
RT embryogenesis.";
RL Dev. Biol. 213:314-326(1999).
RN [6]
RP DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=15531373; DOI=10.1016/j.ydbio.2004.08.042;
RA Kishigami S., Yoshikawa S., Castranio T., Okazaki K., Furuta Y.,
RA Mishina Y.;
RT "BMP signaling through ACVRI is required for left-right patterning in the
RT early mouse embryo.";
RL Dev. Biol. 276:185-193(2004).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=21945937; DOI=10.1016/j.bbrc.2011.09.060;
RA Kamiya N., Kaartinen V.M., Mishina Y.;
RT "Loss-of-function of ACVR1 in osteoblasts increases bone mass and activates
RT canonical Wnt signaling through suppression of Wnt inhibitors SOST and
RT DKK1.";
RL Biochem. Biophys. Res. Commun. 414:326-330(2011).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25413979; DOI=10.1002/jbmr.2385;
RA Rigueur D., Brugger S., Anbarchian T., Kim J.K., Lee Y., Lyons K.M.;
RT "The type I BMP receptor ACVR1/ALK2 is required for chondrogenesis during
RT development.";
RL J. Bone Miner. Res. 30:733-741(2015).
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 (PubMed:10479450, PubMed:15531373, PubMed:21945937). As a
CC type I receptor, forms heterotetrameric receptor complexes with the
CC type II receptors AMHR2, ACVR2A ors ACVR2B. Upon binding of ligands
CC such as BMP7 or BMP9 to the heteromeric complexes, type II receptors
CC transphosphorylate ACVR1 intracellular domain. In turn, ACVR1 kinase
CC domain is activated and subsequently phosphorylates SMAD1/5/8 proteins
CC that transduce the signal. In addition to its role in mediating BMP
CC pathway-specific signaling, suppresses TGFbeta/activin pathway
CC signaling by interfering with the binding of activin to its type II
CC receptor. Besides canonical SMAD signaling, can activate non-canonical
CC pathways such as p38 mitogen-activated protein kinases/MAPKs
CC (PubMed:25413979, PubMed:10479450, PubMed:15531373, PubMed:21945937)
CC (By similarity). {ECO:0000250|UniProtKB:Q04771,
CC ECO:0000269|PubMed:10479450, ECO:0000269|PubMed:15531373,
CC ECO:0000269|PubMed:21945937, ECO:0000269|PubMed:25413979}.
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 -!- TISSUE SPECIFICITY: Highly expressed in bone during developmental
CC stages (PubMed:21945937). Expressed in normal parenchymal cells,
CC endothelial cells, fibroblasts and tumor-derived epithelial cells.
CC {ECO:0000269|PubMed:21945937}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the node and midline and
CC weakly expressed in 8.5 dpc embryos and in the lateral plate mesoderm.
CC {ECO:0000269|PubMed:15531373}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants show a recessive embryonic
CC lethality. At 7.0 dpc, mutant embryos did not show any special
CC abnormalities except a smaller size. However, at 8.0 dpc, mesoderm
CC formation is initiated but its development is arrested around the
CC mid/late streak stage (PubMed:10479450). In an osteoblast-specific
CC manner loss of BMP signaling via ACVR1 directs osteoblasts to increase
CC endogenous bone mass (PubMed:21945937). Additionally, mice lacking
CC ACVR1 in cartilage show reduced SMAD responses, but also decreased p38
CC MAPK activation (PubMed:25413979). {ECO:0000269|PubMed:10479450,
CC ECO:0000269|PubMed:21945937, ECO:0000269|PubMed:25413979}.
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; L15436; AAA40495.1; -; mRNA.
DR EMBL; AF332087; AAK56115.1; -; mRNA.
DR EMBL; AF332088; AAK56116.1; -; mRNA.
DR EMBL; AK150014; BAE29239.1; -; mRNA.
DR EMBL; AK150075; BAE29286.1; -; mRNA.
DR EMBL; BC058718; AAH58718.1; -; mRNA.
DR CCDS; CCDS16050.1; -.
DR PIR; A37489; I59576.
DR RefSeq; NP_001103674.1; NM_001110204.1.
DR RefSeq; NP_001103675.1; NM_001110205.1.
DR RefSeq; NP_031420.2; NM_007394.3.
DR RefSeq; XP_006497685.1; XM_006497622.3.
DR RefSeq; XP_017170494.1; XM_017315005.1.
DR RefSeq; XP_017170495.1; XM_017315006.1.
DR AlphaFoldDB; P37172; -.
DR SMR; P37172; -.
DR BioGRID; 197953; 3.
DR DIP; DIP-5798N; -.
DR MINT; P37172; -.
DR STRING; 10090.ENSMUSP00000088453; -.
DR BindingDB; P37172; -.
DR ChEMBL; CHEMBL3309042; -.
DR GlyGen; P37172; 1 site.
DR iPTMnet; P37172; -.
DR PhosphoSitePlus; P37172; -.
DR SwissPalm; P37172; -.
DR EPD; P37172; -.
DR MaxQB; P37172; -.
DR PaxDb; P37172; -.
DR PeptideAtlas; P37172; -.
DR PRIDE; P37172; -.
DR ProteomicsDB; 285599; -.
DR Antibodypedia; 2371; 626 antibodies from 41 providers.
DR DNASU; 11477; -.
DR Ensembl; ENSMUST00000056376; ENSMUSP00000056784; ENSMUSG00000026836.
DR Ensembl; ENSMUST00000090935; ENSMUSP00000088453; ENSMUSG00000026836.
DR Ensembl; ENSMUST00000112599; ENSMUSP00000108218; ENSMUSG00000026836.
DR Ensembl; ENSMUST00000112601; ENSMUSP00000108220; ENSMUSG00000026836.
DR GeneID; 11477; -.
DR KEGG; mmu:11477; -.
DR UCSC; uc008jss.1; mouse.
DR CTD; 90; -.
DR MGI; MGI:87911; Acvr1.
DR VEuPathDB; HostDB:ENSMUSG00000026836; -.
DR eggNOG; KOG2052; Eukaryota.
DR GeneTree; ENSGT00940000160160; -.
DR HOGENOM; CLU_000288_8_5_1; -.
DR InParanoid; P37172; -.
DR OMA; NQAVECC; -.
DR OrthoDB; 776697at2759; -.
DR PhylomeDB; P37172; -.
DR TreeFam; TF314724; -.
DR BRENDA; 2.7.10.2; 3474.
DR BioGRID-ORCS; 11477; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Acvr1; mouse.
DR PRO; PR:P37172; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P37172; protein.
DR Bgee; ENSMUSG00000026836; Expressed in atrioventricular valve and 289 other tissues.
DR ExpressionAtlas; P37172; baseline and differential.
DR Genevisible; P37172; MM.
DR GO; GO:0048179; C:activin receptor complex; ISO:MGI.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0070724; C:BMP receptor complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
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; IPI:MGI.
DR GO; GO:0016361; F:activin receptor activity, type I; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0019838; F:growth factor binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0050431; F:transforming growth factor beta binding; IDA:MGI.
DR GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IDA:MGI.
DR GO; GO:0032924; P:activin receptor signaling pathway; ISO:MGI.
DR GO; GO:0002526; P:acute inflammatory response; IEP:UniProtKB.
DR GO; GO:0003289; P:atrial septum primum morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003181; P:atrioventricular valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:0030509; P:BMP signaling pathway; ISO:MGI.
DR GO; GO:0061312; P:BMP signaling pathway involved in heart development; IMP:BHF-UCL.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:MGI.
DR GO; GO:0060923; P:cardiac muscle cell fate commitment; ISO:MGI.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISO:MGI.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IBA:GO_Central.
DR GO; GO:0003143; P:embryonic heart tube morphogenesis; ISO:MGI.
DR GO; GO:0061445; P:endocardial cushion cell fate commitment; ISO:MGI.
DR GO; GO:0003274; P:endocardial cushion fusion; IMP:BHF-UCL.
DR GO; GO:0003203; P:endocardial cushion morphogenesis; IMP:BHF-UCL.
DR GO; GO:0007369; P:gastrulation; IMP:MGI.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR GO; GO:0007281; P:germ cell development; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0007498; P:mesoderm development; IMP:MGI.
DR GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR GO; GO:0003183; P:mitral valve morphogenesis; ISO:MGI.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISO:MGI.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0009968; P:negative regulation of signal transduction; ISO:MGI.
DR GO; GO:0001755; P:neural crest cell migration; IMP:MGI.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0060037; P:pharyngeal system development; IMP:MGI.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:2000017; P:positive regulation of determination of dorsal identity; ISO:MGI.
DR GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; IMP:BHF-UCL.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:MGI.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IMP:BHF-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0030278; P:regulation of ossification; ISO:MGI.
DR GO; GO:0051145; P:smooth muscle cell differentiation; IMP:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:MGI.
DR GO; GO:0001655; P:urogenital system development; ISO:MGI.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
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_0000024395"
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"
FT CONFLICT 27
FT /note="K -> E (in Ref. 3; BAE29239/BAE29286)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="N -> Y (in Ref. 1; AAA40495)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 57226 MW; 05BCFC22C5740028 CRC64;
MVDGVMILPV LMMMAFPSPS VEDEKPKVNQ KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN
DGFHVYQKGC FQVYEQGKMT CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF
HLEVGLIILS VVFAVCLLAC ILGVALRKFK RRNQERLNPR DVEYGTIEGL ITTNVGDSTL
AELLDHSCTS GSGSGLPFLV QRTVARQITL LECVGKGRYG EVWRGSWQGE NVAVKIFSSR
DEKSWFRETE LYNTVMLRHE NILGFIASDM TSRHSSTQLW LITHYHEMGS LYDYLQLTTL
DTVSCLRIVL SIASGLAHLH IEIFGTQGKS AIAHRDLKSK NILVKKNGQC CIADLGLAVM
HSQSTNQLDV GNNPRVGTKR YMAPEVLDET IQVDCFDSYK RVDIWAFGLV LWEVARRMVS
NGIVEDYKPP FYDVVPNDPS FEDMRKVVCV DQQRPNIPNR WFSDPTLTSL AKLMKECWYQ
NPSARLTALR IKKTLTKIDN SLDKLKTDC
