TGFR2_MOUSE
ID TGFR2_MOUSE Reviewed; 567 AA.
AC Q62312; Q63947;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=TGF-beta receptor type-2;
DE Short=TGFR-2;
DE EC=2.7.11.30;
DE AltName: Full=TGF-beta type II receptor;
DE AltName: Full=Transforming growth factor-beta receptor type II;
DE Short=TGF-beta receptor type II;
DE Short=TbetaR-II;
DE Flags: Precursor;
GN Name=Tgfbr2;
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] (ISOFORM RII-2), AND ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=7957954; DOI=10.1016/0014-5793(94)01156-7;
RA Suzuki A., Shioda N., Maeda T., Tada M., Ueno N.;
RT "Cloning of an isoform of mouse TGF-beta type II receptor gene.";
RL FEBS Lett. 355:19-22(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RII-1).
RX PubMed=8119124; DOI=10.1242/dev.120.1.165;
RA Lawler S., Candia A.F., Ebner R., Shum L., Lopez A.R., Moses H.L.,
RA Wright C.V., Derynck R.;
RT "The murine type II TGF-beta receptor has a coincident embryonic expression
RT and binding preference for TGF-beta 1.";
RL Development 120:165-175(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM RII-2).
RC TISSUE=Olfactory epithelium;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 AND SER-553, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transmembrane serine/threonine kinase forming with the TGF-
CC beta type I serine/threonine kinase receptor, TGFBR1, the non-
CC promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3.
CC Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to
CC the cytoplasm and is thus regulating a plethora of physiological and
CC pathological processes including cell cycle arrest in epithelial and
CC hematopoietic cells, control of mesenchymal cell proliferation and
CC differentiation, wound healing, extracellular matrix production,
CC immunosuppression and carcinogenesis. The formation of the receptor
CC complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound
CC to the cytokine dimer results in the phosphorylation and the activation
CC of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1
CC phosphorylates SMAD2 which dissociates from the receptor and interacts
CC with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the
CC nucleus where it modulates the transcription of the TGF-beta-regulated
CC genes. This constitutes the canonical SMAD-dependent TGF-beta signaling
CC cascade. Also involved in non-canonical, SMAD-independent TGF-beta
CC signaling pathways (By similarity). {ECO:0000250|UniProtKB:P37173}.
CC -!- FUNCTION: [Isoform RII-1]: Has transforming growth factor beta-
CC activated receptor activity. {ECO:0000250|UniProtKB:P37173}.
CC -!- FUNCTION: [Isoform RII-2]: Has transforming growth factor beta-
CC activated receptor activity. {ECO:0000250|UniProtKB:P37173}.
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: Homodimer. Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric
CC ligands assemble a functional receptor composed of two TGFBR1 and
CC TGFBR2 heterodimers to form a ligand-receptor heterohexamer. The
CC respective affinity of TGFRB1 and TGFRB2 for the ligands may modulate
CC the kinetics of assembly of the receptor and may explain the different
CC biological activities of TGFB1, TGFB2 and TGFB3. Interacts with DAXX.
CC Interacts with DYNLT4. Interacts with ZFYVE9; ZFYVE9 recruits SMAD2 and
CC SMAD3 to the TGF-beta receptor (By similarity). Interacts with and is
CC activated by SCUBE3; this interaction does not affect TGFB1-binding to
CC TGFBR2 (By similarity). Interacts with VPS39; this interaction is
CC independent of the receptor kinase activity and of the presence of TGF-
CC beta (By similarity). Interacts with CLU (By similarity).
CC {ECO:0000250|UniProtKB:P37173}.
CC -!- INTERACTION:
CC Q62312; P55284: Cdh5; NbExp=4; IntAct=EBI-2899332, EBI-7087433;
CC Q62312; P98083-1: Shc1; NbExp=2; IntAct=EBI-2899332, EBI-7533258;
CC Q62312; P98083-2: Shc1; NbExp=3; IntAct=EBI-2899332, EBI-1019301;
CC Q62312; Q64729: Tgfbr1; NbExp=3; IntAct=EBI-2899332, EBI-2899393;
CC Q62312; Q8TDM6: DLG5; Xeno; NbExp=3; IntAct=EBI-2899332, EBI-715138;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P37173};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P37173}.
CC Membrane raft {ECO:0000250|UniProtKB:P37173}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=RII-1;
CC IsoId=Q62312-2; Sequence=Displayed;
CC Name=RII-2;
CC IsoId=Q62312-1; Sequence=VSP_061515;
CC -!- TISSUE SPECIFICITY: Widely expressed in adult. Expressed primarily in
CC mesenchyme and epidermis of the midgestational fetus.
CC -!- PTM: Phosphorylated on a Ser/Thr residue in the cytoplasmic domain.
CC {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; D32072; BAA06840.1; -; mRNA.
DR EMBL; S69114; AAB30100.2; -; mRNA.
DR EMBL; BC052629; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS23601.1; -. [Q62312-2]
DR CCDS; CCDS23602.1; -. [Q62312-2]
DR PIR; S51371; S51371.
DR RefSeq; NP_033397.3; NM_009371.3. [Q62312-1]
DR AlphaFoldDB; Q62312; -.
DR SMR; Q62312; -.
DR BioGRID; 204164; 5.
DR ComplexPortal; CPX-823; TGF-beta-1-TGFR complex.
DR ComplexPortal; CPX-826; TGF-beta-3-TGFR complex.
DR ComplexPortal; CPX-836; TGF-beta-2-TGFR complex.
DR CORUM; Q62312; -.
DR DIP; DIP-44605N; -.
DR IntAct; Q62312; 9.
DR MINT; Q62312; -.
DR STRING; 10090.ENSMUSP00000062333; -.
DR GlyGen; Q62312; 3 sites.
DR iPTMnet; Q62312; -.
DR PhosphoSitePlus; Q62312; -.
DR SwissPalm; Q62312; -.
DR EPD; Q62312; -.
DR MaxQB; Q62312; -.
DR PaxDb; Q62312; -.
DR PRIDE; Q62312; -.
DR ProteomicsDB; 262896; -. [Q62312-1]
DR ProteomicsDB; 262897; -. [Q62312-2]
DR Antibodypedia; 11570; 801 antibodies from 39 providers.
DR DNASU; 21813; -.
DR Ensembl; ENSMUST00000035014; ENSMUSP00000035014; ENSMUSG00000032440. [Q62312-2]
DR Ensembl; ENSMUST00000061101; ENSMUSP00000062333; ENSMUSG00000032440. [Q62312-1]
DR GeneID; 21813; -.
DR KEGG; mmu:21813; -.
DR UCSC; uc009rys.2; mouse. [Q62312-2]
DR UCSC; uc009ryt.2; mouse. [Q62312-2]
DR CTD; 7048; -.
DR MGI; MGI:98729; Tgfbr2.
DR VEuPathDB; HostDB:ENSMUSG00000032440; -.
DR eggNOG; KOG3653; Eukaryota.
DR GeneTree; ENSGT00940000157527; -.
DR HOGENOM; CLU_000288_8_3_1; -.
DR InParanoid; Q62312; -.
DR OMA; MCSCSAE; -.
DR PhylomeDB; Q62312; -.
DR TreeFam; TF314724; -.
DR BRENDA; 2.7.10.2; 3474.
DR Reactome; R-MMU-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-MMU-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR BioGRID-ORCS; 21813; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Tgfbr2; mouse.
DR PRO; PR:Q62312; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q62312; protein.
DR Bgee; ENSMUSG00000032440; Expressed in left lung lobe and 289 other tissues.
DR ExpressionAtlas; Q62312; baseline and differential.
DR Genevisible; Q62312; MM.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0070021; C:transforming growth factor beta ligand-receptor complex; ISO:MGI.
DR GO; GO:0048185; F:activin binding; IBA:GO_Central.
DR GO; GO:0017002; F:activin receptor activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005539; F:glycosaminoglycan binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:MGI.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0046332; F:SMAD binding; IDA:BHF-UCL.
DR GO; GO:0050431; F:transforming growth factor beta binding; IPI:MGI.
DR GO; GO:0005024; F:transforming growth factor beta receptor activity; IGI:MGI.
DR GO; GO:0005026; F:transforming growth factor beta receptor activity, type II; ISO:MGI.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISO:MGI.
DR GO; GO:0034714; F:type III transforming growth factor beta receptor binding; ISO:MGI.
DR GO; GO:0032147; P:activation of protein kinase activity; IDA:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0009887; P:animal organ morphogenesis; ISO:MGI.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0003181; P:atrioventricular valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:0007420; P:brain development; IMP:BHF-UCL.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:MGI.
DR GO; GO:0060433; P:bronchus development; IMP:MGI.
DR GO; GO:0060434; P:bronchus morphogenesis; IMP:MGI.
DR GO; GO:0003214; P:cardiac left ventricle morphogenesis; IMP:BHF-UCL.
DR GO; GO:0051216; P:cartilage development; IMP:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0007182; P:common-partner SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:BHF-UCL.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:BHF-UCL.
DR GO; GO:0003274; P:endocardial cushion fusion; IMP:BHF-UCL.
DR GO; GO:0007369; P:gastrulation; IMP:MGI.
DR GO; GO:0003430; P:growth plate cartilage chondrocyte growth; IMP:MGI.
DR GO; GO:0003417; P:growth plate cartilage development; IGI:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001947; P:heart looping; IMP:BHF-UCL.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:1905317; P:inferior endocardial cushion morphogenesis; IMP:BHF-UCL.
DR GO; GO:0061520; P:Langerhans cell differentiation; IMP:MGI.
DR GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR GO; GO:1990086; P:lens fiber cell apoptotic process; IDA:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0060463; P:lung lobe morphogenesis; IMP:MGI.
DR GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
DR GO; GO:0060443; P:mammary gland morphogenesis; IMP:MGI.
DR GO; GO:0003149; P:membranous septum morphogenesis; IMP:BHF-UCL.
DR GO; GO:1990428; P:miRNA transport; IMP:BHF-UCL.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; IMP:BHF-UCL.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IGI:MGI.
DR GO; GO:0002663; P:positive regulation of B cell tolerance induction; IMP:MGI.
DR GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; ISO:MGI.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:MGI.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; 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:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:BHF-UCL.
DR GO; GO:0051138; P:positive regulation of NK T cell differentiation; IMP:MGI.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0043415; P:positive regulation of skeletal muscle tissue regeneration; IEA:Ensembl.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0002666; P:positive regulation of T cell tolerance induction; IMP:MGI.
DR GO; GO:0002651; P:positive regulation of tolerance induction to self antigen; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0072091; P:regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0070723; P:response to cholesterol; IDA:BHF-UCL.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0062009; P:secondary palate development; IMP:BHF-UCL.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR GO; GO:0060440; P:trachea formation; IMP:MGI.
DR GO; GO:0060439; P:trachea morphogenesis; IMP:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR GO; GO:0003186; P:tricuspid valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:0001570; P:vasculogenesis; IMP:BHF-UCL.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR Gene3D; 2.10.60.10; -; 1.
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 InterPro; IPR017194; Transform_growth_fac-b_typ-2.
DR InterPro; IPR015013; Transforming_GF_b_rcpt_2_ecto.
DR PANTHER; PTHR23255; PTHR23255; 1.
DR Pfam; PF08917; ecTbetaR2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF037393; TGFRII; 1.
DR PRINTS; PR00653; ACTIVIN2R.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; ATP-binding; Cell membrane;
KW Differentiation; Disulfide bond; Glycoprotein; Growth regulation; Kinase;
KW 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..567
FT /note="TGF-beta receptor type-2"
FT /id="PRO_0000024427"
FT TOPO_DOM 24..166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..567
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 244..546
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 545..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 250..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P37173"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..84
FT /evidence="ECO:0000250|UniProtKB:P37173"
FT DISULFID 54..71
FT /evidence="ECO:0000250|UniProtKB:P37173"
FT DISULFID 61..67
FT /evidence="ECO:0000250|UniProtKB:P37173"
FT DISULFID 77..101
FT /evidence="ECO:0000250|UniProtKB:P37173"
FT DISULFID 121..136
FT /evidence="ECO:0000250|UniProtKB:P37173"
FT DISULFID 138..143
FT /evidence="ECO:0000250|UniProtKB:P37173"
FT VAR_SEQ 32
FT /note="V -> DVEMEAQKDASIHLSCNRTIHPLKHF (in isoform RII-2)"
FT /id="VSP_061515"
FT CONFLICT 8
FT /note="G -> A (in Ref. 2; AAB30100)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="D -> N (in Ref. 2; AAB30100)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="A -> R (in Ref. 2; AAB30100)"
FT /evidence="ECO:0000305"
FT CONFLICT 415..418
FT /note="NSGQ -> KQRE (in Ref. 2; AAB30100)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="C -> W (in Ref. 2; AAB30100)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="H -> P (in Ref. 2; AAB30100)"
FT /evidence="ECO:0000305"
FT CONFLICT 544..545
FT /note="PE -> MD (in Ref. 2; AAB30100)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 567 AA; 64219 MW; 4C66067ADA84F986 CRC64;
MGRGLLRGLW PLHIVLWTRI ASTIPPHVPK SVNSDVMASD NGGAVKLPQL CKFCDVRLST
CDNQKSCMSN CSITAICEKP HEVCVAVWRK NDKNITLETV CHDPKLTYHG FTLEDAASPK
CVMKEKKRAG ETFFMCACNM EECNDYIIFS EEYTTSSPDL LLVIIQVTGV SLLPPLGIAI
AVIIIFYCYR VHRQQKLSPS WESSKPRKLM DFSDNCAIIL EDDRSDISST CANNINHNTE
LLPIELDTLV GKGRFAEVYK AKLKQNTSEQ FETVAVKIFP YEEYSSWKTE KDIFSDINLK
HENILQFLTA EERKTELGKQ YWLITAFHAK GNLQEYLTRH VISWEDLRKL GSSLARGIAH
LHSDHTPCGR PKMPIVHRDL KSSNILVKND LTCCLCDFGL SLRLDPTLSV DDLANSGQVG
TARYMAPEVL ESRMNLENVE SFKQTDVYSM ALVLWEMTSR CNAVGEVKDY EPPFGSKVRE
HPCVESMKDS VLRDRGRPEI PSFWLNHQGI QIVCETLTEC WDHDPEARLT AQCVAERFSE
LEHPERLSGR SCSQEKIPED GSLNTTK
