Y4361_ARATH
ID Y4361_ARATH Reviewed; 1136 AA.
AC C0LGS2; O65510; Q8RXY8;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At4g36180;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At4g36180; ORFNames=F23E13.70;
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].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 730-1136.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200;
RA Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA Barbier-Brygoo H., Ephritikhine G.;
RT "A high content in lipid-modified peripheral proteins and integral receptor
RT kinases features in the arabidopsis plasma membrane proteome.";
RL Mol. Cell. Proteomics 6:1980-1996(2007).
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 C0LGS2; F4I065: At1g49100; NbExp=2; IntAct=EBI-16955302, EBI-20654598;
CC C0LGS2; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-16955302, EBI-20651541;
CC C0LGS2; C0LGL4: At2g28960; NbExp=2; IntAct=EBI-16955302, EBI-16946048;
CC C0LGS2; O81069: At2g28990; NbExp=2; IntAct=EBI-16955302, EBI-16887698;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17644812};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:17644812}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18124.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB81527.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL022141; CAA18124.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161588; CAB81527.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE86628.1; -; Genomic_DNA.
DR EMBL; FJ708764; ACN59357.1; -; mRNA.
DR EMBL; AY080606; AAL86290.1; -; mRNA.
DR PIR; T04587; T04587.
DR RefSeq; NP_195341.2; NM_119785.4.
DR AlphaFoldDB; C0LGS2; -.
DR SMR; C0LGS2; -.
DR BioGRID; 15057; 37.
DR IntAct; C0LGS2; 40.
DR STRING; 3702.AT4G36180.1; -.
DR iPTMnet; C0LGS2; -.
DR PaxDb; C0LGS2; -.
DR PRIDE; C0LGS2; -.
DR ProteomicsDB; 242369; -.
DR EnsemblPlants; AT4G36180.1; AT4G36180.1; AT4G36180.
DR GeneID; 829775; -.
DR Gramene; AT4G36180.1; AT4G36180.1; AT4G36180.
DR KEGG; ath:AT4G36180; -.
DR Araport; AT4G36180; -.
DR TAIR; locus:2122239; AT4G36180.
DR eggNOG; ENOG502QTHE; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; C0LGS2; -.
DR OMA; QYLWLDF; -.
DR OrthoDB; 569427at2759; -.
DR PhylomeDB; C0LGS2; -.
DR PRO; PR:C0LGS2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; C0LGS2; baseline and differential.
DR Genevisible; C0LGS2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:TAIR.
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; -; 5.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 13.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1136
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At4g36180"
FT /id="PRO_0000387557"
FT TOPO_DOM 23..751
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 752..772
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 773..1136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 93..115
FT /note="LRR 1"
FT REPEAT 117..139
FT /note="LRR 2"
FT REPEAT 141..162
FT /note="LRR 3"
FT REPEAT 163..186
FT /note="LRR 4"
FT REPEAT 187..210
FT /note="LRR 5"
FT REPEAT 211..233
FT /note="LRR 6"
FT REPEAT 235..256
FT /note="LRR 7"
FT REPEAT 259..280
FT /note="LRR 8"
FT REPEAT 283..304
FT /note="LRR 9"
FT REPEAT 309..330
FT /note="LRR 10"
FT REPEAT 333..355
FT /note="LRR 11"
FT REPEAT 357..379
FT /note="LRR 12"
FT REPEAT 381..403
FT /note="LRR 13"
FT REPEAT 405..426
FT /note="LRR 14"
FT REPEAT 429..452
FT /note="LRR 15"
FT REPEAT 453..479
FT /note="LRR 16"
FT REPEAT 480..500
FT /note="LRR 17"
FT REPEAT 501..524
FT /note="LRR 18"
FT REPEAT 525..546
FT /note="LRR 19"
FT REPEAT 549..571
FT /note="LRR 30"
FT REPEAT 573..595
FT /note="LRR 21"
FT REPEAT 597..620
FT /note="LRR 22"
FT REPEAT 621..643
FT /note="LRR 23"
FT REPEAT 645..666
FT /note="LRR 24"
FT REPEAT 669..691
FT /note="LRR 25"
FT REPEAT 694..716
FT /note="LRR 26"
FT DOMAIN 841..1123
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 786..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 830
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 838
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 915
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 1010
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
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 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 699
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1136 AA; 123664 MW; 7AA32A277F6F2820 CRC64;
MAMDISLFFI FLVIYAPLVS YADESQAEID ALTAFKLNLH DPLGALTSWD PSTPAAPCDW
RGVGCTNHRV TEIRLPRLQL SGRISDRISG LRMLRKLSLR SNSFNGTIPT SLAYCTRLLS
VFLQYNSLSG KLPPAMRNLT SLEVFNVAGN RLSGEIPVGL PSSLQFLDIS SNTFSGQIPS
GLANLTQLQL LNLSYNQLTG EIPASLGNLQ SLQYLWLDFN LLQGTLPSAI SNCSSLVHLS
ASENEIGGVI PAAYGALPKL EVLSLSNNNF SGTVPFSLFC NTSLTIVQLG FNAFSDIVRP
ETTANCRTGL QVLDLQENRI SGRFPLWLTN ILSLKNLDVS GNLFSGEIPP DIGNLKRLEE
LKLANNSLTG EIPVEIKQCG SLDVLDFEGN SLKGQIPEFL GYMKALKVLS LGRNSFSGYV
PSSMVNLQQL ERLNLGENNL NGSFPVELMA LTSLSELDLS GNRFSGAVPV SISNLSNLSF
LNLSGNGFSG EIPASVGNLF KLTALDLSKQ NMSGEVPVEL SGLPNVQVIA LQGNNFSGVV
PEGFSSLVSL RYVNLSSNSF SGEIPQTFGF LRLLVSLSLS DNHISGSIPP EIGNCSALEV
LELRSNRLMG HIPADLSRLP RLKVLDLGQN NLSGEIPPEI SQSSSLNSLS LDHNHLSGVI
PGSFSGLSNL TKMDLSVNNL TGEIPASLAL ISSNLVYFNV SSNNLKGEIP ASLGSRINNT
SEFSGNTELC GKPLNRRCES STAEGKKKKR KMILMIVMAA IGAFLLSLFC CFYVYTLLKW
RKKLKQQSTT GEKKRSPGRT SAGSRVRSST SRSSTENGEP KLVMFNNKIT LAETIEATRQ
FDEENVLSRT RYGLLFKANY NDGMVLSIRR LPNGSLLNEN LFKKEAEVLG KVKHRNITVL
RGYYAGPPDL RLLVYDYMPN GNLSTLLQEA SHQDGHVLNW PMRHLIALGI ARGLGFLHQS
NMVHGDIKPQ NVLFDADFEA HISDFGLDRL TIRSPSRSAV TANTIGTLGY VSPEATLSGE
ITRESDIYSF GIVLLEILTG KRPVMFTQDE DIVKWVKKQL QRGQVTELLE PGLLELDPES
SEWEEFLLGI KVGLLCTATD PLDRPTMSDV VFMLEGCRVG PDVPSSADPT SQPSPA
