PEK10_ARATH
ID PEK10_ARATH Reviewed; 762 AA.
AC Q9C660;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Proline-rich receptor-like protein kinase PERK10;
DE EC=2.7.11.1;
DE AltName: Full=Proline-rich extensin-like receptor kinase 10;
DE Short=AtPERK10;
GN Name=PERK10; OrderedLocusNames=At1g26150; ORFNames=F28B23.17;
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 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 [4]
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 [5]
RP INTERACTION WITH KIPK1 AND KIPK2, AND FUNCTION.
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: Could be involved in the negative regulation of root growth.
CC {ECO:0000269|PubMed:25262228}.
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:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in inflorescence bolts and flower
CC buds, and, to a lower extent, in roots, seedlings, leaves and siliques.
CC {ECO:0000269|PubMed:15653807}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50687.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC079829; AAG50687.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30655.1; -; Genomic_DNA.
DR PIR; F86387; F86387.
DR RefSeq; NP_173940.2; NM_102380.4.
DR AlphaFoldDB; Q9C660; -.
DR SMR; Q9C660; -.
DR BioGRID; 24393; 1.
DR IntAct; Q9C660; 2.
DR STRING; 3702.AT1G26150.1; -.
DR iPTMnet; Q9C660; -.
DR PaxDb; Q9C660; -.
DR PRIDE; Q9C660; -.
DR ProteomicsDB; 236149; -.
DR EnsemblPlants; AT1G26150.1; AT1G26150.1; AT1G26150.
DR GeneID; 839156; -.
DR Gramene; AT1G26150.1; AT1G26150.1; AT1G26150.
DR KEGG; ath:AT1G26150; -.
DR Araport; AT1G26150; -.
DR TAIR; locus:2028756; AT1G26150.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_106_3_1; -.
DR InParanoid; Q9C660; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9C660; -.
DR PRO; PR:Q9C660; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C660; baseline and differential.
DR Genevisible; Q9C660; 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: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; IBA:GO_Central.
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; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..762
FT /note="Proline-rich receptor-like protein kinase PERK10"
FT /id="PRO_0000400062"
FT TOPO_DOM 1..328
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..762
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 430..706
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..312
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 554
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 436..444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 458
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 762 AA; 80856 MW; DC15B446CEAC80D1 CRC64;
MTTPAQAPRE EVSLSPSLAS PPLMALPPPQ PSFPGDNATS PTREPTNGNP PETTNTPAQS
SPPPETPLSS PPPEPSPPSP SLTGPPPTTI PVSPPPEPSP PPPLPTEAPP PANPVSSPPP
ESSPPPPPPT EAPPTTPITS PSPPTNPPPP PESPPSLPAP DPPSNPLPPP KLVPPSHSPP
RHLPSPPASE IPPPPRHLPS PPASERPSTP PSDSEHPSPP PPGHPKRREQ PPPPGSKRPT
PSPPSPSDSK RPVHPSPPSP PEETLPPPKP SPDPLPSNSS SPPTLLPPSS VVSPPSPPRK
SVSGPDNPSP NNPTPVTDNS SSSGISIAAV VGVSIGVALV LLTLIGVVVC CLKKRKKRLS
TIGGGYVMPT PMESSSPRSD SALLKTQSSA PLVGNRSSNR TYLSQSEPGG FGQSRELFSY
EELVIATNGF SDENLLGEGG FGRVYKGVLP DERVVAVKQL KIGGGQGDRE FKAEVDTISR
VHHRNLLSMV GYCISENRRL LIYDYVPNNN LYFHLHAAGT PGLDWATRVK IAAGAARGLA
YLHEDCHPRI IHRDIKSSNI LLENNFHALV SDFGLAKLAL DCNTHITTRV MGTFGYMAPE
YASSGKLTEK SDVFSFGVVL LELITGRKPV DASQPLGDES LVEWARPLLS NATETEEFTA
LADPKLGRNY VGVEMFRMIE AAAACIRHSA TKRPRMSQIV RAFDSLAEED LTNGMRLGES
EIINSAQQSA EIRLFRRMAF GSQNYSTDSL TRNSYISKDE NL
