RGI1_ARATH
ID RGI1_ARATH Reviewed; 1141 AA.
AC Q9LHP4; Q84RP5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase RGI1 {ECO:0000303|PubMed:27229312};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Protein RECEPTOR OF RGF1 4 {ECO:0000303|PubMed:27229311};
DE AltName: Full=Protein RGF1 INSENSITIVE 1 {ECO:0000303|PubMed:27229312};
DE AltName: Full=Protein ROOT CLAVATA-HOMOLOG1 2 {ECO:0000303|Ref.1, ECO:0000312|EMBL:CAD79350.1};
DE Flags: Precursor;
GN Name=RGI1 {ECO:0000303|PubMed:27229312};
GN Synonyms=RCH2 {ECO:0000303|Ref.1}, RGFR1 {ECO:0000303|PubMed:27001831,
GN ECO:0000303|PubMed:29339500}, RGFR4 {ECO:0000303|PubMed:27229311};
GN OrderedLocusNames=At3g24240 {ECO:0000312|Araport:AT3G24240};
GN ORFNames=K13K6.1 {ECO:0000312|EMBL:BAB03091.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Casamitjana-Martinez E.;
RT "Receptor kinase signaling in Arabidopsis root meristem maintenance.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP INTERACTION WITH BEET CURLY TOP VIRUS C4, AND AUTOPHOSPHORYLATION.
RX PubMed=17280695; DOI=10.1016/j.virol.2006.12.034;
RA Piroux N., Saunders K., Page A., Stanley J.;
RT "Geminivirus pathogenicity protein C4 interacts with Arabidopsis thaliana
RT shaggy-related protein kinase AtSKeta, a component of the brassinosteroid
RT signalling pathway.";
RL Virology 362:428-440(2007).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INTERACTION WITH RGF1, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=27229311; DOI=10.1038/cr.2016.62;
RA Song W., Liu L., Wang J., Wu Z., Zhang H., Tang J., Lin G., Wang Y.,
RA Wen X., Li W., Han Z., Guo H., Chai J.;
RT "Signature motif-guided identification of receptors for peptide hormones
RT essential for root meristem growth.";
RL Cell Res. 26:674-685(2016).
RN [7]
RP FUNCTION, MUTAGENESIS OF LYS-814 AND LYS-815, DISRUPTION PHENOTYPE,
RP INTERACTION WITH RGF1, PHOSPHORYLATION, AND UBIQUITINATION.
RC STRAIN=cv. Columbia;
RX PubMed=27229312; DOI=10.1038/cr.2016.63;
RA Ou Y., Lu X., Zi Q., Xun Q., Zhang J., Wu Y., Shi H., Wei Z., Zhao B.,
RA Zhang X., He K., Gou X., Li C., Li J.;
RT "RGF1 INSENSITIVE 1 to 5, a group of LRR receptor-like kinases, are
RT essential for the perception of root meristem growth factor 1 in
RT Arabidopsis thaliana.";
RL Cell Res. 26:686-698(2016).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH RGF1; GLV5/CLEL1/RGF2;
RP GLV7/CLEL3/RGF3; GLV3/RGF4; GLV10/CLEL7/RGF5 AND RGF10/CLELN, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=27001831; DOI=10.1073/pnas.1522639113;
RA Shinohara H., Mori A., Yasue N., Sumida K., Matsubayashi Y.;
RT "Identification of three LRR-RKs involved in perception of root meristem
RT growth factor in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:3897-3902(2016).
RN [9]
RP INTERACTION WITH UBP13, AND PTM.
RC STRAIN=cv. Columbia;
RX PubMed=29339500; DOI=10.1073/pnas.1714177115;
RA An Z., Liu Y., Ou Y., Li J., Zhang B., Sun D., Sun Y., Tang W.;
RT "Regulation of the stability of RGF1 receptor by the ubiquitin-specific
RT proteases UBP12/UBP13 is critical for root meristem maintenance.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:1123-1128(2018).
CC -!- FUNCTION: Together with RGI2, RGI3, RGI4 and RGI5, acts as receptor of
CC RGF peptides (e.g. RGF1, GLV5/CLEL1/RGF2, GLV7/CLEL3/RGF3, GLV3/RGF4,
CC GLV10/CLEL7/RGF5 and RGF10/CLELN), peptide hormones which maintain the
CC postembryonic root stem cell niche by regulating the expression levels
CC and patterns of the transcription factor PLETHORA (PLT, e.g. PLT1 and
CC PLT2) (PubMed:27229312, PubMed:27229311, PubMed:27001831). Links RGF
CC peptides signal with their downstream components (PubMed:27229311,
CC PubMed:27001831). {ECO:0000269|PubMed:27001831,
CC ECO:0000269|PubMed:27229311, ECO:0000269|PubMed:27229312}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
CC -!- SUBUNIT: Interacts with beet curly top virus AL4/C4 (PubMed:17280695).
CC Binds to RGF peptides such as RGF1, GLV5/CLEL1/RGF2, GLV7/CLEL3/RGF3,
CC GLV3/RGF4, GLV10/CLEL7/RGF5 and RGF10/CLELN; these interactions trigger
CC the formation of heterodimers with SERK1, SERK2 or BAK1/SERK3 via LRR
CC regions (PubMed:27001831, PubMed:27229311, PubMed:27229312). Interacts
CC with UBP13 (PubMed:29339500). {ECO:0000269|PubMed:17280695,
CC ECO:0000269|PubMed:27001831, ECO:0000269|PubMed:27229311,
CC ECO:0000269|PubMed:27229312, ECO:0000269|PubMed:29339500}.
CC -!- INTERACTION:
CC Q9LHP4; Q9LT96: At5g49770; NbExp=2; IntAct=EBI-20660903, EBI-17123993;
CC Q9LHP4; Q9ZPS9: BRL2; NbExp=4; IntAct=EBI-20660903, EBI-2292728;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:27001831,
CC ECO:0000269|PubMed:27229311}.
CC -!- DEVELOPMENTAL STAGE: Present in the whole roots with a predominant
CC expression in the proximal meristem, including the elongation zone, and
CC a gradual decreases toward the differentiation zone.
CC {ECO:0000269|PubMed:27001831, ECO:0000269|PubMed:27229311}.
CC -!- PTM: Phosphorylated and ubiquitinated upon interaction with RGF1, thus
CC leading to activation a subsequent degradation (PubMed:27229312).
CC Stabilized by UBP12 and UBP13-mediated deubiquitination
CC (PubMed:29339500). {ECO:0000269|PubMed:27229312,
CC ECO:0000269|PubMed:29339500}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O22476}.
CC -!- DISRUPTION PHENOTYPE: Smaller root meristem size and fewer root
CC meristematic cortex cells, associated with shorter roots and a slighty
CC reduced sensitivity to RGF1 (PubMed:27229311). Quintuple mutants rgi1
CC rgi2 rgi3 rgi4 rgi5 display a consistent short primary root phenotype
CC with a small size of meristem associated with a total insensitivity to
CC RGF1 and undetectable levels of PLT1 and PLT2 (PubMed:27229312). The
CC triple mutant missing RGI1, RGI2 and RGI3 is insensitive to externally
CC applied RGF peptides (e.g. RGF1 and RGF2) and has short roots
CC characterized by a strong decrease in meristematic cell number and
CC declined levels of PLT1 and PLT2 at the root tip (PubMed:27001831).
CC {ECO:0000269|PubMed:27001831, ECO:0000269|PubMed:27229311,
CC ECO:0000269|PubMed:27229312}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD79350.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ550163; CAD79350.1; ALT_FRAME; mRNA.
DR EMBL; AP002037; BAB03091.1; -; Genomic_DNA.
DR EMBL; AB028621; BAB03091.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE76878.1; -; Genomic_DNA.
DR RefSeq; NP_189066.1; NM_113329.3.
DR AlphaFoldDB; Q9LHP4; -.
DR SMR; Q9LHP4; -.
DR BioGRID; 7343; 18.
DR IntAct; Q9LHP4; 19.
DR STRING; 3702.AT3G24240.1; -.
DR PaxDb; Q9LHP4; -.
DR PRIDE; Q9LHP4; -.
DR ProteomicsDB; 236514; -.
DR EnsemblPlants; AT3G24240.1; AT3G24240.1; AT3G24240.
DR GeneID; 822011; -.
DR Gramene; AT3G24240.1; AT3G24240.1; AT3G24240.
DR KEGG; ath:AT3G24240; -.
DR Araport; AT3G24240; -.
DR TAIR; locus:2085949; AT3G24240.
DR eggNOG; ENOG502QQEU; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9LHP4; -.
DR OMA; NWTFITC; -.
DR OrthoDB; 205337at2759; -.
DR PhylomeDB; Q9LHP4; -.
DR PRO; PR:Q9LHP4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHP4; baseline and differential.
DR Genevisible; Q9LHP4; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042277; F:peptide binding; IPI:UniProtKB.
DR GO; GO:0001653; F:peptide receptor activity; IMP:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0010074; P:maintenance of meristem identity; IMP:UniProtKB.
DR GO; GO:0010078; P:maintenance of root meristem identity; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:2000280; P:regulation of root development; IMP:UniProtKB.
DR GO; GO:0010082; P:regulation of root meristem growth; IGI:TAIR.
DR GO; GO:0010449; P:root meristem growth; IGI:TAIR.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_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 Pfam; PF13855; LRR_8; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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 ATP-binding; Cell membrane; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1141
FT /note="LRR receptor-like serine/threonine-protein kinase
FT RGI1"
FT /id="PRO_0000287221"
FT TOPO_DOM 34..726
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 727..747
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 748..1141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 80..104
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 105..128
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 130..152
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 153..176
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 178..200
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 202..225
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 226..249
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 250..273
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 275..297
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 298..321
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 322..345
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 347..369
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 370..392
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 394..417
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 418..441
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 443..464
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 465..489
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 490..513
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 514..537
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 538..561
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 563..585
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 586..609
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 610..634
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 636..657
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 658..682
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT DOMAIN 786..1074
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 185..186
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 207..210
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 230..235
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 258
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 280..282
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 328..331
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 350..352
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 398..402
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 424..427
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 446..450
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 470..472
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT ACT_SITE 919
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 792..800
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 814
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 814
FT /note="Essential for autophosphorylation activity"
FT /evidence="ECO:0000269|PubMed:17280695"
FT MOD_RES 868
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 906
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 962
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 969
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 69..77
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MUTAGEN 814
FT /note="K->E: Lost autophosphorylation."
FT /evidence="ECO:0000269|PubMed:17280695"
FT MUTAGEN 815
FT /note="K->E: Normal autophosphorylation."
FT /evidence="ECO:0000269|PubMed:17280695"
FT CONFLICT 220
FT /note="S -> L (in Ref. 1; CAD79350)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1141 AA; 124504 MW; 1C9CE94DADC78B01 CRC64;
MSLHSLIFFS SSSSSLLFSF FFIFIFCFSL SDAEQNPEAS ILYSWLHSSS PTPSSLSLFN
WNSIDNTPCN NWTFITCSSQ GFITDIDIES VPLQLSLPKN LPAFRSLQKL TISGANLTGT
LPESLGDCLG LKVLDLSSNG LVGDIPWSLS KLRNLETLIL NSNQLTGKIP PDISKCSKLK
SLILFDNLLT GSIPTELGKL SGLEVIRIGG NKEISGQIPS EIGDCSNLTV LGLAETSVSG
NLPSSLGKLK KLETLSIYTT MISGEIPSDL GNCSELVDLF LYENSLSGSI PREIGQLTKL
EQLFLWQNSL VGGIPEEIGN CSNLKMIDLS LNLLSGSIPS SIGRLSFLEE FMISDNKFSG
SIPTTISNCS SLVQLQLDKN QISGLIPSEL GTLTKLTLFF AWSNQLEGSI PPGLADCTDL
QALDLSRNSL TGTIPSGLFM LRNLTKLLLI SNSLSGFIPQ EIGNCSSLVR LRLGFNRITG
EIPSGIGSLK KINFLDFSSN RLHGKVPDEI GSCSELQMID LSNNSLEGSL PNPVSSLSGL
QVLDVSANQF SGKIPASLGR LVSLNKLILS KNLFSGSIPT SLGMCSGLQL LDLGSNELSG
EIPSELGDIE NLEIALNLSS NRLTGKIPSK IASLNKLSIL DLSHNMLEGD LAPLANIENL
VSLNISYNSF SGYLPDNKLF RQLSPQDLEG NKKLCSSTQD SCFLTYRKGN GLGDDGDASR
TRKLRLTLAL LITLTVVLMI LGAVAVIRAR RNIDNERDSE LGETYKWQFT PFQKLNFSVD
QIIRCLVEPN VIGKGCSGVV YRADVDNGEV IAVKKLWPAM VNGGHDEKTK NVRDSFSAEV
KTLGTIRHKN IVRFLGCCWN RNTRLLMYDY MPNGSLGSLL HERRGSSLDW DLRYRILLGA
AQGLAYLHHD CLPPIVHRDI KANNILIGLD FEPYIADFGL AKLVDEGDIG RCSNTVAGSY
GYIAPEYGYS MKITEKSDVY SYGVVVLEVL TGKQPIDPTV PEGIHLVDWV RQNRGSLEVL
DSTLRSRTEA EADEMMQVLG TALLCVNSSP DERPTMKDVA AMLKEIKQER EEYAKVDLLL
KKSPPPTTTM QEECRKNEMM MIPAAAASSS KEMRREERLL KSNNTSFSAS SLLYSSSSSI
E
