PEK13_ARATH
ID PEK13_ARATH Reviewed; 710 AA.
AC Q9CAL8;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Proline-rich receptor-like protein kinase PERK13;
DE EC=2.7.11.1;
DE AltName: Full=Proline-rich extensin-like receptor kinase 13;
DE Short=AtPERK13;
DE AltName: Full=Protein ROOT HAIR SPECIFIC 10;
GN Name=PERK13; Synonyms=RHS10; OrderedLocusNames=At1g70460;
GN ORFNames=F24J13.3;
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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP GENE FAMILY.
RX PubMed=12374299; DOI=10.1023/a:1019951120788;
RA Silva N.F., Goring D.R.;
RT "The proline-rich, extensin-like receptor kinase-1 (PERK1) gene is rapidly
RT induced by wounding.";
RL Plant Mol. Biol. 50:667-685(2002).
RN [5]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15653807; DOI=10.1093/pcp/pch206;
RA Nakhamchik A., Zhao Z., Provart N.J., Shiu S.-H., Keatley S.K.,
RA Cameron R.K., Goring D.R.;
RT "A comprehensive expression analysis of the Arabidopsis proline-rich
RT extensin-like receptor kinase gene family using bioinformatic and
RT experimental approaches.";
RL Plant Cell Physiol. 45:1875-1881(2004).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19448035; DOI=10.1104/pp.109.140905;
RA Won S.-K., Lee Y.-J., Lee H.-Y., Heo Y.-K., Cho M., Cho H.-T.;
RT "Cis-element- and transcriptome-based screening of root hair-specific genes
RT and their functional characterization in Arabidopsis.";
RL Plant Physiol. 150:1459-1473(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RA Lin C., Cho H.-T.;
RT "A pro-rich extensin-like receptor kinase regulates Arabidopsis root hair
RT growth.";
RL (In) Proceedings of the 21st international conference on Arabidopsis
RL research, abstract#08086, Yokohama (2010).
RN [8]
RP INTERACTION WITH KIPK1 AND KIPK2.
RX PubMed=25262228; DOI=10.1093/jxb/eru390;
RA Humphrey T.V., Haasen K.E., Aldea-Brydges M.G., Sun H., Zayed Y.,
RA Indriolo E., Goring D.R.;
RT "PERK-KIPK-KCBP signalling negatively regulates root growth in Arabidopsis
RT thaliana.";
RL J. Exp. Bot. 66:71-83(2015).
CC -!- FUNCTION: Regulates negatively root hairs elongation.
CC {ECO:0000269|PubMed:19448035, ECO:0000269|Ref.7}.
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 -!- SUBUNIT: Interacts with KIPK1 AND KIPK2 (via its cytosolic domain).
CC {ECO:0000269|PubMed:25262228}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|Ref.7}; Single-pass
CC membrane protein {ECO:0000269|Ref.7}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, especially in root
CC hairs. {ECO:0000269|PubMed:15653807, ECO:0000269|PubMed:19448035}.
CC -!- DISRUPTION PHENOTYPE: Longer root hairs. {ECO:0000269|PubMed:19448035,
CC ECO:0000269|Ref.7}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX816903; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC010796; AAG52479.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35064.1; -; Genomic_DNA.
DR EMBL; BX816903; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; D96728; D96728.
DR RefSeq; NP_177203.1; NM_105714.4.
DR AlphaFoldDB; Q9CAL8; -.
DR SMR; Q9CAL8; -.
DR BioGRID; 28602; 1.
DR IntAct; Q9CAL8; 2.
DR STRING; 3702.AT1G70460.1; -.
DR PaxDb; Q9CAL8; -.
DR PRIDE; Q9CAL8; -.
DR ProteomicsDB; 235090; -.
DR EnsemblPlants; AT1G70460.1; AT1G70460.1; AT1G70460.
DR GeneID; 843382; -.
DR Gramene; AT1G70460.1; AT1G70460.1; AT1G70460.
DR KEGG; ath:AT1G70460; -.
DR Araport; AT1G70460; -.
DR TAIR; locus:2026846; AT1G70460.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_106_3_1; -.
DR InParanoid; Q9CAL8; -.
DR OMA; NDQKGHA; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9CAL8; -.
DR PRO; PR:Q9CAL8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAL8; baseline and differential.
DR Genevisible; Q9CAL8; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
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 InterPro; IPR011009; Kinase-like_dom_sf.
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 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; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..710
FT /note="Proline-rich receptor-like protein kinase PERK13"
FT /id="PRO_0000400065"
FT TOPO_DOM 1..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..710
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 353..619
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..192
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 477
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 359..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 426
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 511
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 516
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 524
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 67
FT /note="S -> A (in Ref. 3; BX816903)"
FT /evidence="ECO:0000305"
FT CONFLICT 83..84
FT /note="LT -> FC (in Ref. 3; BX816903)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="P -> L (in Ref. 3; BX816903)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 710 AA; 75372 MW; 8B4420A8DD8F3AA6 CRC64;
MSDSPTSSPP APSADSAPPP DTSSDGSAAP PPTDSAPPPS PPADSSPPPA LPSLPPAVFS
PPPTVSSPPP PPLDSSPPPP PDLTPPPSSP PPPDAPPPIP IVFPPPIDSP PPESTNSPPP
PEVFEPPPPP ADEDESPPAP PPPEQLPPPA SSPQGGPKKP KKHHPGPATS PPAPSAPATS
PPAPPNAPPR NSSHALPPKS TAAGGPLTSP SRGVPSSGNS VPPPANSGGG YQGKTMAGFA
IAGFAVIALM AVVFLVRRKK KRNIDAYSDS QYLPPSNFSI KSDGFLYGQN PTKGYSGPGG
YNSQQQSNSG NSFGSQRGGG GYTRSGSAPD SAVMGSGQTH FTYEELTDIT EGFSKHNILG
EGGFGCVYKG KLNDGKLVAV KQLKVGSGQG DREFKAEVEI ISRVHHRHLV SLVGYCIADS
ERLLIYEYVP NQTLEHHLHG KGRPVLEWAR RVRIAIGSAK GLAYLHEDCH PKIIHRDIKS
ANILLDDEFE AQVADFGLAK LNDSTQTHVS TRVMGTFGYL APEYAQSGKL TDRSDVFSFG
VVLLELITGR KPVDQYQPLG EESLVEWARP LLHKAIETGD FSELVDRRLE KHYVENEVFR
MIETAAACVR HSGPKRPRMV QVVRALDSEG DMGDISNGNK VGQSSAYDSG QYNNDTMKFR
KMAFGFDDSS DSGMYSGDYS VQDSRKGSNG ASSEFTRNET ENRNFNNRRY
