Y4052_ARATH
ID Y4052_ARATH Reviewed; 648 AA.
AC Q8VYT3; Q9M0A8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At4g30520;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At4g30520; ORFNames=F17I23_140;
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).
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 Q8VYT3; O04567: At1g27190; NbExp=2; IntAct=EBI-16902452, EBI-1238687;
CC Q8VYT3; C0LGI5: At1g69990; NbExp=2; IntAct=EBI-16902452, EBI-20651225;
CC Q8VYT3; Q9ZQR3: At2g14510; NbExp=2; IntAct=EBI-16902452, EBI-20651957;
CC Q8VYT3; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-16902452, EBI-16902452;
CC Q8VYT3; Q9ASS4: At5g48380; NbExp=2; IntAct=EBI-16902452, EBI-6298290;
CC Q8VYT3; Q94F62: BAK1; NbExp=2; IntAct=EBI-16902452, EBI-617138;
CC Q8VYT3; Q9ZWC8: BRL1; NbExp=2; IntAct=EBI-16902452, EBI-590903;
CC Q8VYT3; Q9LJF3: BRL3; NbExp=2; IntAct=EBI-16902452, EBI-20651413;
CC Q8VYT3; C0LGT6: EFR; NbExp=2; IntAct=EBI-16902452, EBI-8801168;
CC Q8VYT3; C0LGW6: ERL1; NbExp=3; IntAct=EBI-16902452, EBI-16914248;
CC Q8VYT3; Q6XAT2: ERL2; NbExp=3; IntAct=EBI-16902452, EBI-16895926;
CC Q8VYT3; C0LGQ5: GSO1; NbExp=2; IntAct=EBI-16902452, EBI-16905069;
CC Q8VYT3; C0LGX3: HSL2; NbExp=2; IntAct=EBI-16902452, EBI-16904927;
CC Q8VYT3; Q9C8I6: IOS1; NbExp=3; IntAct=EBI-16902452, EBI-16924837;
CC Q8VYT3; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-16902452, EBI-20651739;
CC Q8VYT3; Q9LFS4: NIK1; NbExp=4; IntAct=EBI-16902452, EBI-16146189;
CC Q8VYT3; Q9C7S5: PSY1R; NbExp=2; IntAct=EBI-16902452, EBI-16904988;
CC Q8VYT3; Q9ZRF9: RPK1; NbExp=4; IntAct=EBI-16902452, EBI-1238953;
CC Q8VYT3; Q94AG2: SERK1; NbExp=2; IntAct=EBI-16902452, EBI-1555537;
CC Q8VYT3; Q9SKG5: SERK4; NbExp=2; IntAct=EBI-16902452, EBI-6290483;
CC Q8VYT3; Q9FG24: SRF2; NbExp=2; IntAct=EBI-16902452, EBI-16955365;
CC Q8VYT3; Q9C8M9: SRF6; NbExp=2; IntAct=EBI-16902452, EBI-16954301;
CC Q8VYT3; Q6R2J8: SRF8; NbExp=2; IntAct=EBI-16902452, EBI-16941202;
CC Q8VYT3; Q8RWZ1: SUB; NbExp=2; IntAct=EBI-16902452, EBI-17072125;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB79770.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL161577; CAB79770.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85776.1; -; Genomic_DNA.
DR EMBL; AY070043; AAL49800.1; -; mRNA.
DR EMBL; AY096538; AAM20188.1; -; mRNA.
DR EMBL; FJ708760; ACN59353.1; -; mRNA.
DR PIR; A85357; A85357.
DR RefSeq; NP_194781.2; NM_119198.5.
DR AlphaFoldDB; Q8VYT3; -.
DR SMR; Q8VYT3; -.
DR BioGRID; 14462; 64.
DR IntAct; Q8VYT3; 82.
DR STRING; 3702.AT4G30520.1; -.
DR iPTMnet; Q8VYT3; -.
DR PaxDb; Q8VYT3; -.
DR PRIDE; Q8VYT3; -.
DR ProteomicsDB; 242874; -.
DR EnsemblPlants; AT4G30520.1; AT4G30520.1; AT4G30520.
DR GeneID; 829175; -.
DR Gramene; AT4G30520.1; AT4G30520.1; AT4G30520.
DR KEGG; ath:AT4G30520; -.
DR Araport; AT4G30520; -.
DR TAIR; locus:2118811; AT4G30520.
DR eggNOG; ENOG502QQXY; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; Q8VYT3; -.
DR OMA; GASGPCY; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q8VYT3; -.
DR PRO; PR:Q8VYT3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VYT3; baseline and differential.
DR Genevisible; Q8VYT3; 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:0015026; F:coreceptor activity; IGI:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:TAIR.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0048653; P:anther development; IGI:TAIR.
DR GO; GO:0007639; P:homeostasis of number of meristem cells; IGI:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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; IPR013210; LRR_N_plant-typ.
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 InterPro; IPR045271; SRF-like.
DR PANTHER; PTHR27001; PTHR27001; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 5.
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; 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..30
FT /evidence="ECO:0000255"
FT CHAIN 31..648
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At4g30520"
FT /id="PRO_0000409728"
FT TOPO_DOM 31..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 100..125
FT /note="LRR 1"
FT REPEAT 127..148
FT /note="LRR 2"
FT REPEAT 149..172
FT /note="LRR 3"
FT REPEAT 174..199
FT /note="LRR 4"
FT DOMAIN 303..582
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 426
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 309..317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 300
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 459
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 460
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 465
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 473
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 476
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 555
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 648 AA; 71194 MW; 601166B450D17428 CRC64;
MVVVTKKTMK IQIHLLYSFL FLCFSTLTLS SEPRNPEVEA LISIRNNLHD PHGALNNWDE
FSVDPCSWAM ITCSPDNLVI GLGAPSQSLS GGLSESIGNL TNLRQVSLQN NNISGKIPPE
LGFLPKLQTL DLSNNRFSGD IPVSIDQLSS LQYLRLNNNS LSGPFPASLS QIPHLSFLDL
SYNNLSGPVP KFPARTFNVA GNPLICRSNP PEICSGSINA SPLSVSLSSS SGRRSNRLAI
ALSVSLGSVV ILVLALGSFC WYRKKQRRLL ILNLNDKQEE GLQGLGNLRS FTFRELHVYT
DGFSSKNILG AGGFGNVYRG KLGDGTMVAV KRLKDINGTS GDSQFRMELE MISLAVHKNL
LRLIGYCATS GERLLVYPYM PNGSVASKLK SKPALDWNMR KRIAIGAARG LLYLHEQCDP
KIIHRDVKAA NILLDECFEA VVGDFGLAKL LNHADSHVTT AVRGTVGHIA PEYLSTGQSS
EKTDVFGFGI LLLELITGLR ALEFGKTVSQ KGAMLEWVRK LHEEMKVEEL LDRELGTNYD
KIEVGEMLQV ALLCTQYLPA HRPKMSEVVL MLEGDGLAER WAASHNHSHF YHANISFKTI
SSLSTTSVSR LDAHCNDPTY QMFGSSAFDD DDDHQPLDSF AMELSGPR
