ERL2_ARATH
ID ERL2_ARATH Reviewed; 967 AA.
AC Q6XAT2; Q9LYP7;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase ERL2;
DE EC=2.7.11.1;
DE AltName: Full=Protein ERECTA-like kinase 2;
DE Flags: Precursor;
GN Name=ERL2; OrderedLocusNames=At5g07180; ORFNames=T28J14.120;
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 [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=14985254; DOI=10.1242/dev.01028;
RA Shpak E.D., Berthiaume C.T., Hill E.J., Torii K.U.;
RT "Synergistic interaction of three ERECTA-family receptor-like kinases
RT controls Arabidopsis organ growth and flower development by promoting cell
RT proliferation.";
RL Development 131:1491-1501(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [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.
RX PubMed=16002616; DOI=10.1126/science.1109710;
RA Shpak E.D., McAbee J.M., Pillitteri L.J., Torii K.U.;
RT "Stomatal patterning and differentiation by synergistic interactions of
RT receptor kinases.";
RL Science 309:290-293(2005).
RN [6]
RP FUNCTION.
RX PubMed=17652352; DOI=10.1242/dev.004788;
RA Pillitteri L.J., Bemis S.M., Shpak E.D., Torii K.U.;
RT "Haploinsufficiency after successive loss of signaling reveals a role for
RT ERECTA-family genes in Arabidopsis ovule development.";
RL Development 134:3099-3109(2007).
CC -!- FUNCTION: Receptor kinase that regulates inflorescence architecture and
CC organ shape as well as stomatal patterning, including density and
CC clustering, together with ERL1 and ER. {ECO:0000269|PubMed:14985254,
CC ECO:0000269|PubMed:16002616, ECO:0000269|PubMed:17652352}.
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 Q6XAT2; O04567: At1g27190; NbExp=2; IntAct=EBI-16895926, EBI-1238687;
CC Q6XAT2; C0LGI5: At1g69990; NbExp=3; IntAct=EBI-16895926, EBI-20651225;
CC Q6XAT2; Q9ZQR3: At2g14510; NbExp=2; IntAct=EBI-16895926, EBI-20651957;
CC Q6XAT2; Q8VYT3: At4g30520; NbExp=3; IntAct=EBI-16895926, EBI-16902452;
CC Q6XAT2; Q9ASS4: At5g48380; NbExp=2; IntAct=EBI-16895926, EBI-6298290;
CC Q6XAT2; Q94F62: BAK1; NbExp=4; IntAct=EBI-16895926, EBI-617138;
CC Q6XAT2; O22476: BRI1; NbExp=2; IntAct=EBI-16895926, EBI-1797828;
CC Q6XAT2; Q9ZWC8: BRL1; NbExp=2; IntAct=EBI-16895926, EBI-590903;
CC Q6XAT2; Q9LJF3: BRL3; NbExp=2; IntAct=EBI-16895926, EBI-20651413;
CC Q6XAT2; Q42371: ERECTA; NbExp=4; IntAct=EBI-16895926, EBI-16940407;
CC Q6XAT2; C0LGW6: ERL1; NbExp=2; IntAct=EBI-16895926, EBI-16914248;
CC Q6XAT2; Q6XAT2: ERL2; NbExp=3; IntAct=EBI-16895926, EBI-16895926;
CC Q6XAT2; Q9FL28: FLS2; NbExp=4; IntAct=EBI-16895926, EBI-1799448;
CC Q6XAT2; Q9C8I6: IOS1; NbExp=3; IntAct=EBI-16895926, EBI-16924837;
CC Q6XAT2; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-16895926, EBI-20651739;
CC Q6XAT2; Q9LFS4: NIK1; NbExp=4; IntAct=EBI-16895926, EBI-16146189;
CC Q6XAT2; Q8RY65: NIK2; NbExp=4; IntAct=EBI-16895926, EBI-20664696;
CC Q6XAT2; Q9C7S5: PSY1R; NbExp=3; IntAct=EBI-16895926, EBI-16904988;
CC Q6XAT2; Q9ZRF9: RPK1; NbExp=3; IntAct=EBI-16895926, EBI-1238953;
CC Q6XAT2; Q94AG2: SERK1; NbExp=4; IntAct=EBI-16895926, EBI-1555537;
CC Q6XAT2; Q9SKG5: SERK4; NbExp=3; IntAct=EBI-16895926, EBI-6290483;
CC Q6XAT2; Q8LPS5: SERK5; NbExp=4; IntAct=EBI-16895926, EBI-16887868;
CC Q6XAT2; Q06BH3: SRF1; NbExp=2; IntAct=EBI-16895926, EBI-16955764;
CC Q6XAT2; Q9FG24: SRF2; NbExp=2; IntAct=EBI-16895926, EBI-16955365;
CC Q6XAT2; Q6R2K3: SRF3; NbExp=2; IntAct=EBI-16895926, EBI-20651925;
CC Q6XAT2; Q6R2K1: SRF5; NbExp=3; IntAct=EBI-16895926, EBI-20651875;
CC Q6XAT2; Q9C8M9: SRF6; NbExp=3; IntAct=EBI-16895926, EBI-16954301;
CC Q6XAT2; Q9LUL4: SRF7; NbExp=3; IntAct=EBI-16895926, EBI-16964596;
CC Q6XAT2; Q8RWZ1: SUB; NbExp=4; IntAct=EBI-16895926, EBI-17072125;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in developing organs, including
CC bud clusters, flowers, siliques and young rosettes. Also detected in
CC mature aboveground organs, such as leaves, stems and pedicels, but
CC barely in roots. {ECO:0000269|PubMed:14985254}.
CC -!- DEVELOPMENTAL STAGE: At the vegetative stage, strongly expressed in the
CC shoot meristem, leaf primordia and juvenile leaves. At the reproductive
CC stage, localized in the young developing flowers.
CC {ECO:0000269|PubMed:14985254}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87274.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY244746; AAP69764.1; -; mRNA.
DR EMBL; AL163652; CAB87274.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91118.1; -; Genomic_DNA.
DR EMBL; FJ708772; ACN59363.1; -; mRNA.
DR PIR; T48489; T48489.
DR RefSeq; NP_196335.2; NM_120800.4.
DR PDB; 5XKN; X-ray; 3.65 A; A/B=30-575.
DR PDBsum; 5XKN; -.
DR AlphaFoldDB; Q6XAT2; -.
DR SMR; Q6XAT2; -.
DR BioGRID; 15888; 28.
DR IntAct; Q6XAT2; 56.
DR STRING; 3702.AT5G07180.1; -.
DR PaxDb; Q6XAT2; -.
DR PRIDE; Q6XAT2; -.
DR ProteomicsDB; 220694; -.
DR EnsemblPlants; AT5G07180.1; AT5G07180.1; AT5G07180.
DR GeneID; 830609; -.
DR Gramene; AT5G07180.1; AT5G07180.1; AT5G07180.
DR KEGG; ath:AT5G07180; -.
DR Araport; AT5G07180; -.
DR TAIR; locus:2182855; AT5G07180.
DR eggNOG; ENOG502QTEP; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q6XAT2; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q6XAT2; -.
DR PRO; PR:Q6XAT2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6XAT2; baseline and differential.
DR Genevisible; Q6XAT2; 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: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; IEA:UniProtKB-KW.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IBA:GO_Central.
DR GO; GO:0009553; P:embryo sac development; IGI:TAIR.
DR GO; GO:0048481; P:plant ovule development; IGI:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010103; P:stomatal complex morphogenesis; IGI:TAIR.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
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; PF12799; LRR_4; 1.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 14.
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; 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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..967
FT /note="LRR receptor-like serine/threonine-protein kinase
FT ERL2"
FT /id="PRO_0000387510"
FT TOPO_DOM 28..585
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 586..606
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 607..967
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 74..97
FT /note="LRR 1"
FT REPEAT 98..120
FT /note="LRR 2"
FT REPEAT 122..145
FT /note="LRR 3"
FT REPEAT 146..166
FT /note="LRR 4"
FT REPEAT 170..192
FT /note="LRR 5"
FT REPEAT 194..216
FT /note="LRR 6"
FT REPEAT 218..240
FT /note="LRR 7"
FT REPEAT 242..261
FT /note="LRR 8"
FT REPEAT 265..287
FT /note="LRR 9"
FT REPEAT 289..311
FT /note="LRR 10"
FT REPEAT 313..335
FT /note="LRR 11"
FT REPEAT 337..359
FT /note="LRR 12"
FT REPEAT 361..382
FT /note="LRR 13"
FT REPEAT 385..406
FT /note="LRR 14"
FT REPEAT 409..431
FT /note="LRR 15"
FT REPEAT 433..456
FT /note="LRR 16"
FT REPEAT 457..479
FT /note="LRR 17"
FT REPEAT 481..503
FT /note="LRR 18"
FT REPEAT 505..527
FT /note="LRR 19"
FT REPEAT 529..550
FT /note="LRR 20"
FT DOMAIN 651..921
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 921..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 776
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 657..665
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 679
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 640
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 648
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 724
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 763
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 818
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 826
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 967 AA; 106680 MW; 90096C7B67CE852C CRC64;
MRRIETMKGL FFCLGMVVFM LLGSVSPMNN EGKALMAIKA SFSNVANMLL DWDDVHNHDF
CSWRGVFCDN VSLNVVSLNL SNLNLGGEIS SALGDLMNLQ SIDLQGNKLG GQIPDEIGNC
VSLAYVDFST NLLFGDIPFS ISKLKQLEFL NLKNNQLTGP IPATLTQIPN LKTLDLARNQ
LTGEIPRLLY WNEVLQYLGL RGNMLTGTLS PDMCQLTGLW YFDVRGNNLT GTIPESIGNC
TSFEILDVSY NQITGVIPYN IGFLQVATLS LQGNKLTGRI PEVIGLMQAL AVLDLSDNEL
TGPIPPILGN LSFTGKLYLH GNKLTGQIPP ELGNMSRLSY LQLNDNELVG KIPPELGKLE
QLFELNLANN NLVGLIPSNI SSCAALNQFN VHGNFLSGAV PLEFRNLGSL TYLNLSSNSF
KGKIPAELGH IINLDTLDLS GNNFSGSIPL TLGDLEHLLI LNLSRNHLNG TLPAEFGNLR
SIQIIDVSFN FLAGVIPTEL GQLQNINSLI LNNNKIHGKI PDQLTNCFSL ANLNISFNNL
SGIIPPMKNF TRFSPASFFG NPFLCGNWVG SICGPSLPKS QVFTRVAVIC MVLGFITLIC
MIFIAVYKSK QQKPVLKGSS KQPEGSTKLV ILHMDMAIHT FDDIMRVTEN LDEKYIIGYG
ASSTVYKCTS KTSRPIAIKR IYNQYPSNFR EFETELETIG SIRHRNIVSL HGYALSPFGN
LLFYDYMENG SLWDLLHGPG KKVKLDWETR LKIAVGAAQG LAYLHHDCTP RIIHRDIKSS
NILLDGNFEA RLSDFGIAKS IPATKTYAST YVLGTIGYID PEYARTSRLN EKSDIYSFGI
VLLELLTGKK AVDNEANLHQ MILSKADDNT VMEAVDAEVS VTCMDSGHIK KTFQLALLCT
KRNPLERPTM QEVSRVLLSL VPSPPPKKLP SPAKVQEGEE RRESHSSDTT TPQWFVQFRE
DISKSSL
