HSL1_ARATH
ID HSL1_ARATH Reviewed; 996 AA.
AC Q9SGP2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Receptor-like protein kinase HSL1;
DE EC=2.7.11.1;
DE AltName: Full=Protein HAESA-LIKE1;
DE Flags: Precursor;
GN Name=HSL1; OrderedLocusNames=At1g28440; ORFNames=F3M18.12;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Morosawa T.,
RA Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K.,
RA Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K.,
RA Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA Hayashizaki Y., Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP IDENTIFICATION, AND DEVELOPMENTAL STAGE.
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).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Decreased expression shortly before the onset of
CC abscission. {ECO:0000269|PubMed:18660431}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC010155; AAF16764.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30977.1; -; Genomic_DNA.
DR EMBL; AY093235; AAM13234.1; -; mRNA.
DR EMBL; BT008808; AAP68247.1; -; mRNA.
DR EMBL; AK227198; BAE99237.1; -; mRNA.
DR EMBL; FJ708639; ACN59235.1; -; mRNA.
DR PIR; F86410; F86410.
DR RefSeq; NP_174166.1; NM_102612.4.
DR PDB; 7ODK; X-ray; 1.83 A; AAA/BBB=17-618.
DR PDB; 7ODV; X-ray; 2.31 A; AAA/DDD=17-618.
DR PDB; 7OGO; X-ray; 2.38 A; AAA/DDD=17-618.
DR PDB; 7OGQ; X-ray; 2.20 A; AAA=17-618.
DR PDB; 7OGU; X-ray; 2.87 A; AAA/DDD/GGG/JJJ=17-618.
DR PDB; 7OGZ; X-ray; 2.70 A; AAA/DDD=17-618.
DR PDBsum; 7ODK; -.
DR PDBsum; 7ODV; -.
DR PDBsum; 7OGO; -.
DR PDBsum; 7OGQ; -.
DR PDBsum; 7OGU; -.
DR PDBsum; 7OGZ; -.
DR AlphaFoldDB; Q9SGP2; -.
DR SMR; Q9SGP2; -.
DR STRING; 3702.AT1G28440.1; -.
DR iPTMnet; Q9SGP2; -.
DR PaxDb; Q9SGP2; -.
DR PRIDE; Q9SGP2; -.
DR ProteomicsDB; 232131; -.
DR EnsemblPlants; AT1G28440.1; AT1G28440.1; AT1G28440.
DR GeneID; 839742; -.
DR Gramene; AT1G28440.1; AT1G28440.1; AT1G28440.
DR KEGG; ath:AT1G28440; -.
DR Araport; AT1G28440; -.
DR TAIR; locus:2032553; AT1G28440.
DR eggNOG; ENOG502QQFB; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9SGP2; -.
DR OMA; EVMWLTE; -.
DR OrthoDB; 145621at2759; -.
DR PhylomeDB; Q9SGP2; -.
DR PRO; PR:Q9SGP2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SGP2; baseline and differential.
DR Genevisible; Q9SGP2; 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:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 4.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
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 3D-structure; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..996
FT /note="Receptor-like protein kinase HSL1"
FT /id="PRO_0000383586"
FT TOPO_DOM 16..618
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 640..996
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 59..83
FT /note="LRR 1"
FT REPEAT 84..107
FT /note="LRR 2"
FT REPEAT 109..131
FT /note="LRR 3"
FT REPEAT 133..154
FT /note="LRR 4"
FT REPEAT 155..178
FT /note="LRR 5"
FT REPEAT 179..203
FT /note="LRR 6"
FT REPEAT 205..228
FT /note="LRR 7"
FT REPEAT 229..252
FT /note="LRR 8"
FT REPEAT 253..276
FT /note="LRR 9"
FT REPEAT 278..299
FT /note="LRR 10"
FT REPEAT 300..323
FT /note="LRR 11"
FT REPEAT 325..347
FT /note="LRR 12"
FT REPEAT 348..371
FT /note="LRR 13"
FT REPEAT 373..395
FT /note="LRR 14"
FT REPEAT 396..419
FT /note="LRR 15"
FT REPEAT 421..443
FT /note="LRR 16"
FT REPEAT 444..467
FT /note="LRR 17"
FT REPEAT 468..491
FT /note="LRR 18"
FT REPEAT 493..515
FT /note="LRR 19"
FT REPEAT 516..539
FT /note="LRR 20"
FT REPEAT 541..562
FT /note="LRR 21"
FT REPEAT 563..586
FT /note="LRR 22"
FT DOMAIN 676..962
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 967..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 815
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 682..690
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 704
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 764
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 802
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 859
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 866
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 867
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 996 AA; 108929 MW; 9C9A6A708A1F933A CRC64;
MYLLFLFLLF PTVFSLNQDG FILQQVKLSL DDPDSYLSSW NSNDASPCRW SGVSCAGDFS
SVTSVDLSSA NLAGPFPSVI CRLSNLAHLS LYNNSINSTL PLNIAACKSL QTLDLSQNLL
TGELPQTLAD IPTLVHLDLT GNNFSGDIPA SFGKFENLEV LSLVYNLLDG TIPPFLGNIS
TLKMLNLSYN PFSPSRIPPE FGNLTNLEVM WLTECHLVGQ IPDSLGQLSK LVDLDLALND
LVGHIPPSLG GLTNVVQIEL YNNSLTGEIP PELGNLKSLR LLDASMNQLT GKIPDELCRV
PLESLNLYEN NLEGELPASI ALSPNLYEIR IFGNRLTGGL PKDLGLNSPL RWLDVSENEF
SGDLPADLCA KGELEELLII HNSFSGVIPE SLADCRSLTR IRLAYNRFSG SVPTGFWGLP
HVNLLELVNN SFSGEISKSI GGASNLSLLI LSNNEFTGSL PEEIGSLDNL NQLSASGNKF
SGSLPDSLMS LGELGTLDLH GNQFSGELTS GIKSWKKLNE LNLADNEFTG KIPDEIGSLS
VLNYLDLSGN MFSGKIPVSL QSLKLNQLNL SYNRLSGDLP PSLAKDMYKN SFIGNPGLCG
DIKGLCGSEN EAKKRGYVWL LRSIFVLAAM VLLAGVAWFY FKYRTFKKAR AMERSKWTLM
SFHKLGFSEH EILESLDEDN VIGAGASGKV YKVVLTNGET VAVKRLWTGS VKETGDCDPE
KGYKPGVQDE AFEAEVETLG KIRHKNIVKL WCCCSTRDCK LLVYEYMPNG SLGDLLHSSK
GGMLGWQTRF KIILDAAEGL SYLHHDSVPP IVHRDIKSNN ILIDGDYGAR VADFGVAKAV
DLTGKAPKSM SVIAGSCGYI APEYAYTLRV NEKSDIYSFG VVILEIVTRK RPVDPELGEK
DLVKWVCSTL DQKGIEHVID PKLDSCFKEE ISKILNVGLL CTSPLPINRP SMRRVVKMLQ
EIGGGDEDSL HKIRDDKDGK LTPYYNEDTS DQGSIA
