HSL2_ARATH
ID HSL2_ARATH Reviewed; 993 AA.
AC C0LGX3; O49544;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase HSL2;
DE EC=2.7.11.1;
DE AltName: Full=Protein HAESA-LIKE2;
DE Flags: Precursor;
GN Name=HSL2; OrderedLocusNames=At5g65710; ORFNames=F6H11.160, MPA24.6;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 IDENTIFICATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=18660431; DOI=10.1105/tpc.108.059139;
RA Stenvik G.-E., Tandstad N.M., Guo Y., Shi C.-L., Kristiansen W.,
RA Holmgren A., Clark S.E., Aalen R.B., Butenko M.A.;
RT "The EPIP peptide of INFLORESCENCE DEFICIENT IN ABSCISSION is sufficient to
RT induce abscission in arabidopsis through the receptor-like kinases HAESA
RT and HAESA-LIKE2.";
RL Plant Cell 20:1805-1817(2008).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=18809915; DOI=10.1073/pnas.0805539105;
RA Cho S.K., Larue C.T., Chevalier D., Wang H., Jinn T.-L., Zhang S.,
RA Walker J.C.;
RT "Regulation of floral organ abscission in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15629-15634(2008).
CC -!- FUNCTION: Receptor-like serine/threonine-kinase acting on substrates
CC that controls floral organ abscission. Regulated by the 'INFLORESCENCE
CC DEFICIENT IN ABSCISSION' (IDA) family of ligands.
CC {ECO:0000269|PubMed:18809915}.
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 C0LGX3; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-16904927, EBI-16902452;
CC C0LGX3; Q94F62: BAK1; NbExp=2; IntAct=EBI-16904927, EBI-617138;
CC C0LGX3; Q9LJF3: BRL3; NbExp=2; IntAct=EBI-16904927, EBI-20651413;
CC C0LGX3; Q42371: ERECTA; NbExp=2; IntAct=EBI-16904927, EBI-16940407;
CC C0LGX3; Q9LFS4: NIK1; NbExp=2; IntAct=EBI-16904927, EBI-16146189;
CC C0LGX3; Q9ZRF9: RPK1; NbExp=2; IntAct=EBI-16904927, EBI-1238953;
CC C0LGX3; Q8LPS5: SERK5; NbExp=2; IntAct=EBI-16904927, EBI-16887868;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expression is restricted to the abscission zone.
CC {ECO:0000269|PubMed:18809915}.
CC -!- DEVELOPMENTAL STAGE: Expression increases shortly before the onset of
CC abscission. {ECO:0000269|PubMed:18660431, ECO:0000269|PubMed:18809915}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC RLK5/HAE. Hae and hsl2 double mutants have a strong abscission defect.
CC {ECO:0000269|PubMed:18660431}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10678.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA16687.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB010075; BAB10678.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL021684; CAA16687.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED98093.1; -; Genomic_DNA.
DR EMBL; FJ708817; ACN59408.1; -; mRNA.
DR PIR; T05897; T05897.
DR RefSeq; NP_201372.2; NM_125968.3.
DR AlphaFoldDB; C0LGX3; -.
DR SMR; C0LGX3; -.
DR BioGRID; 21942; 47.
DR IntAct; C0LGX3; 54.
DR STRING; 3702.AT5G65710.1; -.
DR PaxDb; C0LGX3; -.
DR PRIDE; C0LGX3; -.
DR ProteomicsDB; 230149; -.
DR EnsemblPlants; AT5G65710.1; AT5G65710.1; AT5G65710.
DR GeneID; 836700; -.
DR Gramene; AT5G65710.1; AT5G65710.1; AT5G65710.
DR KEGG; ath:AT5G65710; -.
DR Araport; AT5G65710; -.
DR TAIR; locus:2169975; AT5G65710.
DR eggNOG; ENOG502R5E1; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; C0LGX3; -.
DR OMA; CRISTLQ; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; C0LGX3; -.
DR PRO; PR:C0LGX3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; C0LGX3; baseline and differential.
DR Genevisible; C0LGX3; 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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:TAIR.
DR GO; GO:0010102; P:lateral root morphogenesis; IMP:TAIR.
DR GO; GO:0060866; P:leaf abscission; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010468; P:regulation of gene expression; IGI:TAIR.
DR Gene3D; 3.80.10.10; -; 3.
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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 5.
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 ATP-binding; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..993
FT /note="LRR receptor-like serine/threonine-protein kinase
FT HSL2"
FT /id="PRO_0000383587"
FT TOPO_DOM 29..632
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 633..653
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 654..993
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 75..96
FT /note="LRR 1"
FT REPEAT 99..120
FT /note="LRR 2"
FT REPEAT 124..146
FT /note="LRR 3"
FT REPEAT 148..170
FT /note="LRR 4"
FT REPEAT 172..192
FT /note="LRR 5"
FT REPEAT 196..217
FT /note="LRR 6"
FT REPEAT 221..243
FT /note="LRR 7"
FT REPEAT 245..267
FT /note="LRR 8"
FT REPEAT 269..291
FT /note="LRR 9"
FT REPEAT 293..315
FT /note="LRR 10"
FT REPEAT 316..338
FT /note="LRR 11"
FT REPEAT 364..386
FT /note="LRR 12"
FT REPEAT 388..410
FT /note="LRR 13"
FT REPEAT 412..433
FT /note="LRR 14"
FT REPEAT 435..458
FT /note="LRR 15"
FT REPEAT 460..481
FT /note="LRR 16"
FT REPEAT 484..507
FT /note="LRR 17"
FT REPEAT 508..530
FT /note="LRR 18"
FT REPEAT 532..555
FT /note="LRR 19"
FT REPEAT 556..579
FT /note="LRR 20"
FT REPEAT 580..601
FT /note="LRR 21"
FT DOMAIN 686..992
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 817
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 692..700
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 714
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 678
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 762
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 804
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 856
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 864
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 871
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 872
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 993 AA; 110710 MW; B91B856467B409D1 CRC64;
MLTNTNLFFF LSLLLLSCFL QVSSNGDAEI LSRVKKTRLF DPDGNLQDWV ITGDNRSPCN
WTGITCHIRK GSSLAVTTID LSGYNISGGF PYGFCRIRTL INITLSQNNL NGTIDSAPLS
LCSKLQNLIL NQNNFSGKLP EFSPEFRKLR VLELESNLFT GEIPQSYGRL TALQVLNLNG
NPLSGIVPAF LGYLTELTRL DLAYISFDPS PIPSTLGNLS NLTDLRLTHS NLVGEIPDSI
MNLVLLENLD LAMNSLTGEI PESIGRLESV YQIELYDNRL SGKLPESIGN LTELRNFDVS
QNNLTGELPE KIAALQLISF NLNDNFFTGG LPDVVALNPN LVEFKIFNNS FTGTLPRNLG
KFSEISEFDV STNRFSGELP PYLCYRRKLQ KIITFSNQLS GEIPESYGDC HSLNYIRMAD
NKLSGEVPAR FWELPLTRLE LANNNQLQGS IPPSISKARH LSQLEISANN FSGVIPVKLC
DLRDLRVIDL SRNSFLGSIP SCINKLKNLE RVEMQENMLD GEIPSSVSSC TELTELNLSN
NRLRGGIPPE LGDLPVLNYL DLSNNQLTGE IPAELLRLKL NQFNVSDNKL YGKIPSGFQQ
DIFRPSFLGN PNLCAPNLDP IRPCRSKRET RYILPISILC IVALTGALVW LFIKTKPLFK
RKPKRTNKIT IFQRVGFTEE DIYPQLTEDN IIGSGGSGLV YRVKLKSGQT LAVKKLWGET
GQKTESESVF RSEVETLGRV RHGNIVKLLM CCNGEEFRFL VYEFMENGSL GDVLHSEKEH
RAVSPLDWTT RFSIAVGAAQ GLSYLHHDSV PPIVHRDVKS NNILLDHEMK PRVADFGLAK
PLKREDNDGV SDVSMSCVAG SYGYIAPEYG YTSKVNEKSD VYSFGVVLLE LITGKRPNDS
SFGENKDIVK FAMEAALCYP SPSAEDGAMN QDSLGNYRDL SKLVDPKMKL STREYEEIEK
VLDVALLCTS SFPINRPTMR KVVELLKEKK SLE
