RGI3_ARATH
ID RGI3_ARATH Reviewed; 1091 AA.
AC C0LGR3; O65580; Q8W556;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase RGI3 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Protein RECEPTOR OF RGF1 1 {ECO:0000303|PubMed:27229311};
DE AltName: Full=Protein RGF1 INSENSITIVE 3 {ECO:0000303|PubMed:27229312};
DE Flags: Precursor;
GN Name=RGI3 {ECO:0000303|PubMed:27229312};
GN Synonyms=RGFR1 {ECO:0000303|PubMed:27229311},
GN RGFR3 {ECO:0000303|PubMed:27001831};
GN OrderedLocusNames=At4g26540 {ECO:0000312|Araport:AT4G26540};
GN ORFNames=M3E9.30 {ECO:0000312|EMBL:CAA18216.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 57-689 IN COMPLEX WITH SMALL
RP PEPTIDE, FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, INTERACTION WITH RGF1,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, 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).
CC -!- FUNCTION: Together with RGI1, RGI2, 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:27229311, PubMed:27229312, 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: Binds to RGF peptides such as RGF1, GLV5/CLEL1/RGF2,
CC GLV7/CLEL3/RGF3, GLV3/RGF4, GLV10/CLEL7/RGF5 and RGF10/CLELN; these
CC interactions trigger the formation of heterodimers with SERK1, SERK2 or
CC BAK1/SERK3 via LRR regions. {ECO:0000269|PubMed:27001831,
CC ECO:0000269|PubMed:27229311}.
CC -!- INTERACTION:
CC C0LGR3; C0LGI5: At1g69990; NbExp=3; IntAct=EBI-20659695, EBI-20651225;
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: In roots, detected in the more basal region of the
CC elongation zone and the differentiation zone, mainly restricted to
CC columella, transition zone and root stem cell niche.
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.
CC {ECO:0000250|UniProtKB:Q9LHP4}.
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=AAL32011.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA18216.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA18216.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB79509.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79509.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL022223; CAA18216.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161565; CAB79509.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85216.1; -; Genomic_DNA.
DR EMBL; AF436829; AAL32011.1; ALT_FRAME; mRNA.
DR EMBL; FJ708754; ACN59348.1; -; mRNA.
DR PIR; T05050; T05050.
DR RefSeq; NP_567748.5; NM_118787.6.
DR PDB; 5HYX; X-ray; 2.60 A; B=57-689.
DR PDB; 5HZ0; X-ray; 2.56 A; B=57-689.
DR PDB; 5HZ1; X-ray; 2.59 A; B=57-689.
DR PDB; 5HZ3; X-ray; 2.86 A; B=57-689.
DR PDBsum; 5HYX; -.
DR PDBsum; 5HZ0; -.
DR PDBsum; 5HZ1; -.
DR PDBsum; 5HZ3; -.
DR AlphaFoldDB; C0LGR3; -.
DR SMR; C0LGR3; -.
DR BioGRID; 14047; 44.
DR IntAct; C0LGR3; 44.
DR STRING; 3702.AT4G26540.1; -.
DR iPTMnet; C0LGR3; -.
DR PaxDb; C0LGR3; -.
DR PRIDE; C0LGR3; -.
DR ProteomicsDB; 236934; -.
DR EnsemblPlants; AT4G26540.1; AT4G26540.1; AT4G26540.
DR GeneID; 828760; -.
DR Gramene; AT4G26540.1; AT4G26540.1; AT4G26540.
DR KEGG; ath:AT4G26540; -.
DR Araport; AT4G26540; -.
DR TAIR; locus:2131518; AT4G26540.
DR eggNOG; ENOG502QSU9; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; C0LGR3; -.
DR OMA; PNTPFFH; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; C0LGR3; -.
DR PRO; PR:C0LGR3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; C0LGR3; baseline and differential.
DR Genevisible; C0LGR3; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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 Gene3D; 3.80.10.10; -; 7.
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; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 8.
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 3D-structure; ATP-binding; Cell membrane; Disulfide bond; Glycoprotein;
KW Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1091
FT /note="LRR receptor-like serine/threonine-protein kinase
FT RGI3"
FT /id="PRO_0000387553"
FT TOPO_DOM 25..703
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 704..724
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 725..1091
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 33..56
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 67..91
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 92..115
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 116..140
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 142..166
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 168..188
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 190..213
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 214..237
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 239..261
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 262..285
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 287..309
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 311..332
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 333..357
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 359..383
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 385..405
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 406..429
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 431..453
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 454..477
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 478..501
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 503..524
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 525..548
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 549..572
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 574..596
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 598..620
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 621..644
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REPEAT 645..668
FT /note="LRR 26"
FT /evidence="ECO:0000255"
FT REPEAT 669..690
FT /note="LRR 27"
FT /evidence="ECO:0000255"
FT DOMAIN 760..1046
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 173..174
FT /note="Small peptide recognition"
FT /evidence="ECO:0000269|PubMed:27229311,
FT ECO:0007744|PDB:5HYX, ECO:0007744|PDB:5HZ0,
FT ECO:0007744|PDB:5HZ1, ECO:0007744|PDB:5HZ3"
FT MOTIF 195..198
FT /note="Small peptide recognition"
FT /evidence="ECO:0000269|PubMed:27229311,
FT ECO:0007744|PDB:5HYX, ECO:0007744|PDB:5HZ0,
FT ECO:0007744|PDB:5HZ1, ECO:0007744|PDB:5HZ3"
FT MOTIF 218..223
FT /note="Small peptide recognition"
FT /evidence="ECO:0000269|PubMed:27229311,
FT ECO:0007744|PDB:5HYX, ECO:0007744|PDB:5HZ0,
FT ECO:0007744|PDB:5HZ1, ECO:0007744|PDB:5HZ3"
FT MOTIF 246
FT /note="Small peptide recognition"
FT /evidence="ECO:0000269|PubMed:27229311,
FT ECO:0007744|PDB:5HYX, ECO:0007744|PDB:5HZ0,
FT ECO:0007744|PDB:5HZ1, ECO:0007744|PDB:5HZ3"
FT MOTIF 268..270
FT /note="Small peptide recognition"
FT /evidence="ECO:0000269|PubMed:27229311,
FT ECO:0007744|PDB:5HYX, ECO:0007744|PDB:5HZ0,
FT ECO:0007744|PDB:5HZ1, ECO:0007744|PDB:5HZ3"
FT MOTIF 316..319
FT /note="Small peptide recognition"
FT /evidence="ECO:0000269|PubMed:27229311,
FT ECO:0007744|PDB:5HYX, ECO:0007744|PDB:5HZ0,
FT ECO:0007744|PDB:5HZ1, ECO:0007744|PDB:5HZ3"
FT MOTIF 338..340
FT /note="Small peptide recognition"
FT /evidence="ECO:0000269|PubMed:27229311,
FT ECO:0007744|PDB:5HYX, ECO:0007744|PDB:5HZ0,
FT ECO:0007744|PDB:5HZ1, ECO:0007744|PDB:5HZ3"
FT MOTIF 386..390
FT /note="Small peptide recognition"
FT /evidence="ECO:0000269|PubMed:27229311,
FT ECO:0007744|PDB:5HYX, ECO:0007744|PDB:5HZ0,
FT ECO:0007744|PDB:5HZ1, ECO:0007744|PDB:5HZ3"
FT MOTIF 412..415
FT /note="Small peptide recognition"
FT /evidence="ECO:0000269|PubMed:27229311,
FT ECO:0007744|PDB:5HYX, ECO:0007744|PDB:5HZ0,
FT ECO:0007744|PDB:5HZ1, ECO:0007744|PDB:5HZ3"
FT MOTIF 434..438
FT /note="Small peptide recognition"
FT /evidence="ECO:0000269|PubMed:27229311,
FT ECO:0007744|PDB:5HYX, ECO:0007744|PDB:5HZ0,
FT ECO:0007744|PDB:5HZ1, ECO:0007744|PDB:5HZ3"
FT MOTIF 458..460
FT /note="Small peptide recognition"
FT /evidence="ECO:0000269|PubMed:27229311,
FT ECO:0007744|PDB:5HYX, ECO:0007744|PDB:5HZ0,
FT ECO:0007744|PDB:5HZ1, ECO:0007744|PDB:5HZ3"
FT ACT_SITE 883
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 766..774
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 788
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 788
FT /note="Essential for autophosphorylation activity"
FT /evidence="ECO:0000250|UniProtKB:Q9LHP4"
FT MOD_RES 831
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 870
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 933
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 57..64
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CONFLICT 221
FT /note="L -> P (in Ref. 3; AAL32011)"
FT /evidence="ECO:0000305"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:5HYX"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:5HZ1"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:5HYX"
FT HELIX 304..308
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 328..332
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:5HZ3"
FT HELIX 352..356
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 376..380
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 400..404
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 424..428
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 439..444
FT /evidence="ECO:0007829|PDB:5HZ1"
FT HELIX 448..452
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 463..466
FT /evidence="ECO:0007829|PDB:5HZ1"
FT HELIX 472..476
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 487..490
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 496..500
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:5HZ3"
FT HELIX 543..547
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 553..555
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 567..571
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 582..585
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:5HZ1"
FT HELIX 591..595
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 601..604
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 611..613
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 616..620
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 626..628
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 639..641
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 658..661
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 665..669
FT /evidence="ECO:0007829|PDB:5HZ0"
FT HELIX 672..676
FT /evidence="ECO:0007829|PDB:5HZ0"
FT STRAND 678..683
FT /evidence="ECO:0007829|PDB:5HZ0"
SQ SEQUENCE 1091 AA; 119529 MW; 061EFB0EDF281988 CRC64;
MPPNIYRLSF FSSLLCFFFI PCFSLDQQGQ ALLSWKSQLN ISGDAFSSWH VADTSPCNWV
GVKCNRRGEV SEIQLKGMDL QGSLPVTSLR SLKSLTSLTL SSLNLTGVIP KEIGDFTELE
LLDLSDNSLS GDIPVEIFRL KKLKTLSLNT NNLEGHIPME IGNLSGLVEL MLFDNKLSGE
IPRSIGELKN LQVLRAGGNK NLRGELPWEI GNCENLVMLG LAETSLSGKL PASIGNLKRV
QTIAIYTSLL SGPIPDEIGY CTELQNLYLY QNSISGSIPT TIGGLKKLQS LLLWQNNLVG
KIPTELGNCP ELWLIDFSEN LLTGTIPRSF GKLENLQELQ LSVNQISGTI PEELTNCTKL
THLEIDNNLI TGEIPSLMSN LRSLTMFFAW QNKLTGNIPQ SLSQCRELQA IDLSYNSLSG
SIPKEIFGLR NLTKLLLLSN DLSGFIPPDI GNCTNLYRLR LNGNRLAGSI PSEIGNLKNL
NFVDISENRL VGSIPPAISG CESLEFLDLH TNSLSGSLLG TTLPKSLKFI DFSDNALSST
LPPGIGLLTE LTKLNLAKNR LSGEIPREIS TCRSLQLLNL GENDFSGEIP DELGQIPSLA
ISLNLSCNRF VGEIPSRFSD LKNLGVLDVS HNQLTGNLNV LTDLQNLVSL NISYNDFSGD
LPNTPFFRRL PLSDLASNRG LYISNAISTR PDPTTRNSSV VRLTILILVV VTAVLVLMAV
YTLVRARAAG KQLLGEEIDS WEVTLYQKLD FSIDDIVKNL TSANVIGTGS SGVVYRITIP
SGESLAVKKM WSKEESGAFN SEIKTLGSIR HRNIVRLLGW CSNRNLKLLF YDYLPNGSLS
SRLHGAGKGG CVDWEARYDV VLGVAHALAY LHHDCLPTII HGDVKAMNVL LGPHFEPYLA
DFGLARTISG YPNTGIDLAK PTNRPPMAGS YGYMAPEHAS MQRITEKSDV YSYGVVLLEV
LTGKHPLDPD LPGGAHLVKW VRDHLAEKKD PSRLLDPRLD GRTDSIMHEM LQTLAVAFLC
VSNKANERPL MKDVVAMLTE IRHIDVGRSE TEKIKAGGCG SKEPQQFMSN EKIINSHGSS
NCSFAFSDDS V
