HERK_ARATH
ID HERK_ARATH Reviewed; 830 AA.
AC Q9LX66; Q9SNA7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Receptor-like protein kinase HERK 1;
DE EC=2.7.11.-;
DE AltName: Full=Protein HERCULES RECEPTOR KINASE 1;
DE Flags: Precursor;
GN Name=HERK1; OrderedLocusNames=At3g46290; ORFNames=F12M12.260, F18L15.10;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
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).
RN [6]
RP GENE FAMILY.
RX PubMed=19529822; DOI=10.1093/mp/ssn083;
RA Chae L., Sudat S., Dudoit S., Zhu T., Luan S.;
RT "Diverse transcriptional programs associated with environmental stress and
RT hormones in the Arabidopsis receptor-like kinase gene family.";
RL Mol. Plant 2:84-107(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AUTOPHOSPHORYLATION, MUTAGENESIS OF
RP LYS-513, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION BY
RP BRASSINOSTEROIDS.
RX PubMed=19383785; DOI=10.1073/pnas.0812346106;
RA Guo H., Li L., Ye H., Yu X., Algreen A., Yin Y.;
RT "Three related receptor-like kinases are required for optimal cell
RT elongation in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:7648-7653(2009).
CC -!- FUNCTION: Receptor-like protein kinase required for cell elongation
CC during vegetative growth, mostly in a brassinosteroid-(BR-) independent
CC manner. {ECO:0000269|PubMed:19383785}.
CC -!- INTERACTION:
CC Q9LX66; Q9FN92: At5g59700; NbExp=4; IntAct=EBI-22028097, EBI-17071988;
CC Q9LX66; Q9SCZ4: FER; NbExp=5; IntAct=EBI-22028097, EBI-15880405;
CC Q9LX66; B3GS44: LRE; NbExp=2; IntAct=EBI-22028097, EBI-21914693;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19383785,
CC ECO:0000305|PubMed:17644812}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:19383785, ECO:0000305|PubMed:17644812}.
CC -!- TISSUE SPECIFICITY: Expressed in most vegetative tissues, including
CC leaves, stems and roots, especially in cell elongation regions.
CC {ECO:0000269|PubMed:19383785}.
CC -!- INDUCTION: By brassinosteroids (BR). {ECO:0000269|PubMed:19383785}.
CC -!- PTM: Autophosphorylated.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to redundancy with
CC THE1. Herk1 and the1 double mutants are stunted. In herk1-1, shorter
CC hypocotyls without brassinolide (BL) treatment than with BL treatment.
CC {ECO:0000269|PubMed:19383785}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB62020.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL133298; CAB62020.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL355775; CAB90956.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78143.1; -; Genomic_DNA.
DR PIR; T45686; T45686.
DR PIR; T49270; T49270.
DR RefSeq; NP_190214.1; NM_114497.4.
DR AlphaFoldDB; Q9LX66; -.
DR SMR; Q9LX66; -.
DR IntAct; Q9LX66; 3.
DR STRING; 3702.AT3G46290.1; -.
DR iPTMnet; Q9LX66; -.
DR PaxDb; Q9LX66; -.
DR PRIDE; Q9LX66; -.
DR ProteomicsDB; 230508; -.
DR EnsemblPlants; AT3G46290.1; AT3G46290.1; AT3G46290.
DR GeneID; 823774; -.
DR Gramene; AT3G46290.1; AT3G46290.1; AT3G46290.
DR KEGG; ath:AT3G46290; -.
DR Araport; AT3G46290; -.
DR TAIR; locus:2075346; AT3G46290.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_42_1_1; -.
DR InParanoid; Q9LX66; -.
DR OMA; CDDKSEM; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LX66; -.
DR PRO; PR:Q9LX66; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LX66; baseline and differential.
DR Genevisible; Q9LX66; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0009741; P:response to brassinosteroid; IGI:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IGI:TAIR.
DR InterPro; IPR045272; ANXUR1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024788; Malectin-like_Carb-bd_dom.
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 PANTHER; PTHR27003; PTHR27003; 1.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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 ATP-binding; Cell membrane; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..830
FT /note="Receptor-like protein kinase HERK 1"
FT /id="PRO_0000312029"
FT TOPO_DOM 25..405
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 485..758
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 609
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 491..499
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 513
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 513
FT /note="K->R: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:19383785"
SQ SEQUENCE 830 AA; 91468 MW; 9767A13857FE36BF CRC64;
MGIEKFETFI LISTISILLC ICHGFTPVDN YLINCGSPTN GTLMGRIFLS DKLSSKLLTS
SKEILASVGG NSGSDIYHTA RVFTEVSSYK FSVTRGRHWV RLYFNPFDYQ NFKMGSAKFA
VSSQSHVLLS DFTVTSSKVV KEYSLNVTTN DLVLTFTPSS GSFAFVNAIE VISIPDTLIT
GSPRFVGNPA QFPDMSMQGL ETIHRVNMGG PLVASNNDTL TRTWVPDSEF LLEKNLAKSM
SKFSTVNFVP GYATEDSAPR TVYGSCTEMN SADNPNSIFN VTWEFDVDPG FQYYFRFHFC
DIVSLSLNQL YFNLYVDSMV AATDIDLSTL VDNTLAGAYS MDFVTQTPKG SNKVRVSIGP
STVHTDYPNA IVNGLEIMKM NNSKGQLSTG TFVPGSSSSS KSNLGLIVGS AIGSLLAVVF
LGSCFVLYKK RKRGQDGHSK TWMPFSINGT SMGSKYSNGT TLTSITTNAN YRIPFAAVKD
ATNNFDESRN IGVGGFGKVY KGELNDGTKV AVKRGNPKSQ QGLAEFRTEI EMLSQFRHRH
LVSLIGYCDE NNEMILIYEY MENGTVKSHL YGSGLPSLTW KQRLEICIGA ARGLHYLHTG
DSKPVIHRDV KSANILLDEN FMAKVADFGL SKTGPELDQT HVSTAVKGSF GYLDPEYFRR
QQLTDKSDVY SFGVVLFEVL CARPVIDPTL PREMVNLAEW AMKWQKKGQL DQIIDQSLRG
NIRPDSLRKF AETGEKCLAD YGVDRPSMGD VLWNLEYALQ LQEAVIDGEP EDNSTNMIGE
LPPQINNFSQ GDTSVNVPGT AGRFEESSID DLSGVSMSKV FSQLVKSEGR
