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Y4291_ARATH
ID   Y4291_ARATH             Reviewed;         913 AA.
AC   C0LGR6; Q9SZE6;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At4g29180;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=At4g29180; ORFNames=F19B15.210;
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=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).
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   -!- 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;
CC   -!- INTERACTION:
CC       C0LGR6; Q9SH71: At1g64210; NbExp=2; IntAct=EBI-20654480, EBI-20651385;
CC       C0LGR6; Q9M9C5: At1g68400; NbExp=2; IntAct=EBI-20654480, EBI-1238661;
CC       C0LGR6; C0LGL4: At2g28960; NbExp=2; IntAct=EBI-20654480, EBI-16946048;
CC       C0LGR6; Q9SUQ3: At4g23740; NbExp=2; IntAct=EBI-20654480, EBI-16912451;
CC       C0LGR6; C0LGR9: At4g31250; NbExp=2; IntAct=EBI-20654480, EBI-16955262;
CC       C0LGR6; A0A1P8B6S7: At4g39270; NbExp=2; IntAct=EBI-20654480, EBI-20661308;
CC       C0LGR6; Q8W4S5: At5g63710; NbExp=2; IntAct=EBI-20654480, EBI-16934827;
CC       C0LGR6; O65440-2: BAM3; NbExp=2; IntAct=EBI-20654480, EBI-20653325;
CC       C0LGR6; C0LGQ5: GSO1; NbExp=2; IntAct=EBI-20654480, EBI-16905069;
CC       C0LGR6; Q9LJM4: IKU2; NbExp=2; IntAct=EBI-20654480, EBI-20664220;
CC       C0LGR6; F4K6B8: RGI4; NbExp=2; IntAct=EBI-20654480, EBI-1238236;
CC       C0LGR6; Q9LP77: RKL1; NbExp=2; IntAct=EBI-20654480, EBI-1544507;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=C0LGR6-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB43932.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79676.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL078470; CAB43932.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161574; CAB79676.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85599.1; -; Genomic_DNA.
DR   EMBL; FJ708757; ACN59351.1; -; mRNA.
DR   PIR; T08973; T08973.
DR   RefSeq; NP_001190865.1; NM_001203936.2. [C0LGR6-1]
DR   AlphaFoldDB; C0LGR6; -.
DR   SMR; C0LGR6; -.
DR   BioGRID; 14326; 53.
DR   IntAct; C0LGR6; 65.
DR   STRING; 3702.AT4G29180.2; -.
DR   PaxDb; C0LGR6; -.
DR   PRIDE; C0LGR6; -.
DR   EnsemblPlants; AT4G29180.2; AT4G29180.2; AT4G29180. [C0LGR6-1]
DR   GeneID; 829039; -.
DR   Gramene; AT4G29180.2; AT4G29180.2; AT4G29180. [C0LGR6-1]
DR   KEGG; ath:AT4G29180; -.
DR   Araport; AT4G29180; -.
DR   TAIR; locus:2119896; AT4G29180.
DR   eggNOG; ENOG502QQCZ; Eukaryota.
DR   HOGENOM; CLU_000288_41_1_1; -.
DR   InParanoid; C0LGR6; -.
DR   OMA; MSCVKDR; -.
DR   PhylomeDB; C0LGR6; -.
DR   PRO; PR:C0LGR6; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; C0LGR6; baseline and differential.
DR   Genevisible; C0LGR6; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR024788; Malectin-like_Carb-bd_dom.
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; 1.
DR   Pfam; PF12819; Malectin_like; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
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   Alternative splicing; ATP-binding; Glycoprotein; Kinase;
KW   Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW   Signal; Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..913
FT                   /note="Probable LRR receptor-like serine/threonine-protein
FT                   kinase At4g29180"
FT                   /id="PRO_0000387554"
FT   TOPO_DOM        23..509
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        510..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        531..913
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          413..434
FT                   /note="LRR 1"
FT   REPEAT          437..460
FT                   /note="LRR 2"
FT   REPEAT          461..482
FT                   /note="LRR 3"
FT   DOMAIN          567..877
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          862..896
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        862..877
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        878..896
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        704
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         573..581
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         595
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         558
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         653
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         739
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         744
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         752
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        296
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        434
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        471
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        724
FT                   /note="G -> W (in Ref. 3; ACN59351)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   913 AA;  101593 MW;  204B4F336D82455C CRC64;
     MGAHSVFLIL FSVIAIAIVV HGQGQAGFIS IDCGSPPNIN YVDTDTGISY TWDAPFINAG
     VNLNVSEEYG YPKNPVLPFP LADVRSFPQG NRNCYTLTPS DGKGNLYLIR ASFMYGNYDG
     KNALPEFDLY VNVNFWTSVK LRNASENVIK EILSFAESDT IYVCLVNKGK GTPFISALEL
     RPMNSSIYGT EFGRNVSLVL YQRWDTGYLN GTGRYQKDTY DRIWSPYSPV SWNTTMTTGY
     IDIFQSGYRP PDEVIKTAAS PKSDDEPLEL SWTSSDPDTR FYAYLYFAEL ENLKRNESRE
     IKIFWNGSPV SGAFNPSPEY SMTVSNSRAF TGKDHWISVQ KTAESTRPPI LNAIEIFSAQ
     SLDEFYTRID DVQAIESIKS TYKVNKIWTG DPCSPRLFPW EGIGCSYNTS SYQIKSLNLS
     SSGLHGPIAF AFRNLSLLES LDLSNNNLKG IVPEFLADLK YLKSLNLKGN NLTGFIPRSL
     RKRATANGLA LSVDEQNICH SRSCRDGNRI MVPIVVSTLV IILIAALAII CIMRRESKIM
     YSGAYSGPLL PSGKRRFTYS EVSSITNNFN KVIGKGGFGI VYLGSLEDGT EIAVKMINDS
     SFGKSKGSSS SSSSSQVSKE FQVEAELLLT VHHRNLASFV GYCDDGRSMA LIYEYMANGN
     LQDYLSSENA EDLSWEKRLH IAIDSAQGLE YLHHGCRPPI VHRDVKTANI LLNDNLEAKI
     ADFGLSKVFP EDDLSHVVTA VMGTPGYVDP EYYNTFKLNE KSDVYSFGIV LLELITGKRS
     IMKTDDGEKM NVVHYVEPFL KMGDIDGVVD PRLHGDFSSN SAWKFVEVAM SCVRDRGTNR
     PNTNQIVSDL KQCLAAELAR EPKSNHEKKE VVKEKYTKTK STVQNYSSNE YNSSSGSVSL
     SFGDYSTFGP MAR
 
 
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