Y4312_ARATH
ID Y4312_ARATH Reviewed; 676 AA.
AC C0LGR9; O49575; Q0WRL7; Q67Z85;
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=Probable LRR receptor-like serine/threonine-protein kinase At4g31250;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At4g31250; ORFNames=F8F16.70;
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 C0LGR9; C0LGH8: At1g63430; NbExp=2; IntAct=EBI-16955262, EBI-20657656;
CC C0LGR9; C0LGR6: At4g29180; NbExp=2; IntAct=EBI-16955262, EBI-20654480;
CC C0LGR9; A0A178UAF6: AXX17_At5g67350; NbExp=2; IntAct=EBI-16955262, EBI-20661274;
CC C0LGR9; Q9FZ59: PEPR2; NbExp=2; IntAct=EBI-16955262, EBI-20652612;
CC C0LGR9; Q9SKB2: SOBIR1; NbExp=2; IntAct=EBI-16955262, EBI-16905883;
CC C0LGR9; P43298: TMK1; NbExp=2; IntAct=EBI-16955262, EBI-2023970;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=C0LGR9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=C0LGR9-2; Sequence=VSP_038293, VSP_038294;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16528.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79843.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021633; CAA16528.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161578; CAB79843.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85882.1; -; Genomic_DNA.
DR EMBL; AK176198; BAD43961.1; -; mRNA.
DR EMBL; AK176233; BAD43996.1; -; mRNA.
DR EMBL; AK176245; BAD44008.1; -; mRNA.
DR EMBL; AK176283; BAD44046.1; -; mRNA.
DR EMBL; AK176290; BAD44053.1; -; mRNA.
DR EMBL; AK176304; BAD44067.1; -; mRNA.
DR EMBL; AK176329; BAD44092.1; -; mRNA.
DR EMBL; AK221228; BAD93819.1; -; mRNA.
DR EMBL; AK228286; BAF00232.1; -; mRNA.
DR EMBL; FJ708761; ACN59354.1; -; mRNA.
DR PIR; T04492; T04492.
DR RefSeq; NP_567870.1; NM_119274.5. [C0LGR9-1]
DR AlphaFoldDB; C0LGR9; -.
DR SMR; C0LGR9; -.
DR BioGRID; 14538; 64.
DR IntAct; C0LGR9; 67.
DR STRING; 3702.AT4G31250.1; -.
DR iPTMnet; C0LGR9; -.
DR PaxDb; C0LGR9; -.
DR PRIDE; C0LGR9; -.
DR ProteomicsDB; 242876; -. [C0LGR9-1]
DR EnsemblPlants; AT4G31250.1; AT4G31250.1; AT4G31250. [C0LGR9-1]
DR GeneID; 829252; -.
DR Gramene; AT4G31250.1; AT4G31250.1; AT4G31250. [C0LGR9-1]
DR KEGG; ath:AT4G31250; -.
DR Araport; AT4G31250; -.
DR TAIR; locus:2128156; AT4G31250.
DR eggNOG; ENOG502QUJJ; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; C0LGR9; -.
DR OMA; RTEWTAD; -.
DR PhylomeDB; C0LGR9; -.
DR PRO; PR:C0LGR9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; C0LGR9; baseline and differential.
DR Genevisible; C0LGR9; 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; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..676
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At4g31250"
FT /id="PRO_0000387556"
FT TOPO_DOM 27..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..676
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 98..122
FT /note="LRR 1"
FT REPEAT 123..146
FT /note="LRR 2"
FT REPEAT 148..171
FT /note="LRR 3"
FT REPEAT 172..195
FT /note="LRR 4"
FT REPEAT 197..218
FT /note="LRR 5"
FT DOMAIN 366..640
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 319..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 372..380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..88
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_038293"
FT VAR_SEQ 89..98
FT /note="ELDVQALGSI -> MERSDVFKRL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_038294"
FT CONFLICT 487..488
FT /note="DL -> RI (in Ref. 3; BAF00232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 676 AA; 75235 MW; 65162EF1D0782579 CRC64;
MTRDDKFPIV YSLLLIVLLF VSPIYGDGDA DALLKFKSSL VNASSLGGWD SGEPPCSGDK
GSDSKWKGVM CSNGSVFALR LENMSLSGEL DVQALGSIRG LKSISFMRNH FEGKIPRGID
GLVSLAHLYL AHNQFTGEID GDLFSGMKAL LKVHLEGNRF SGEIPESLGK LPKLTELNLE
DNMFTGKIPA FKQKNLVTVN VANNQLEGRI PLTLGLMNIT FFSGNKGLCG APLLPCRYTR
PPFFTVFLLA LTILAVVVLI TVFLSVCILS RRQGKGQDQI QNHGVGHFHG QVYGQPEQQQ
HSEKSSQDSK VYRKLANETV QRDSTATSGA ISVGGLSPDE DKRGDQRKLH FVRNDQERFT
LQDMLRASAE VLGSGGFGSS YKAALSSGRA VVVKRFRFMS NIGREEFYDH MKKIGRLSHP
NLLPLIAFYY RKEEKLLVTN YISNGSLANL LHANRTPGQV VLDWPIRLKI VRGVTRGLAY
LYRVFPDLNL PHGHLKSSNV LLDPNFEPLL TDYALVPVVN RDQSQQFMVA YKAPEFTQQD
RTSRRSDVWS LGILILEILT GKFPANYLRQ GKGADDELAA WVESVARTEW TADVFDKEMK
AGKEHEAQML KLLKIGLRCC DWDIEKRIEL HEAVDRIEEV DRDAGGGQES VRSSYVTASD
GDHRSSRAMT EEFSLM
