PR5K_ARATH
ID PR5K_ARATH Reviewed; 665 AA.
AC Q9FF29; Q38925;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=PR5-like receptor kinase {ECO:0000303|PubMed:8637920};
DE EC=2.7.11.1 {ECO:0000269|PubMed:8637920};
DE Flags: Precursor;
GN Name=PR5K {ECO:0000303|PubMed:8637920};
GN OrderedLocusNames=At5g38280 {ECO:0000312|Araport:AT5G38280};
GN ORFNames=MXA21.170 {ECO:0000312|EMBL:BAB11294.1};
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 [MRNA], FUNCTION, TISSUE SPECIFICITY,
RP AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-360.
RC STRAIN=cv. Columbia;
RX PubMed=8637920; DOI=10.1073/pnas.93.6.2598;
RA Wang X., Zafian P., Choudhary M., Lawton M.;
RT "The PR5K receptor protein kinase from Arabidopsis thaliana is structurally
RT related to a family of plant defense proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:2598-2602(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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).
CC -!- FUNCTION: Possesses kinase activity in vitro.
CC {ECO:0000269|PubMed:8637920}.
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 Evidence={ECO:0000269|PubMed:8637920};
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; Evidence={ECO:0000269|PubMed:8637920};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. Expressed at low levels in
CC stems. {ECO:0000269|PubMed:8637920}.
CC -!- PTM: Autophosphorylated in vitro. {ECO:0000269|PubMed:8637920}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the thaumatin family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Ser/Thr protein kinase family. {ECO:0000305}.
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DR EMBL; U48698; AAC49208.1; -; mRNA.
DR EMBL; AB005247; BAB11294.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94289.1; -; Genomic_DNA.
DR RefSeq; NP_198644.1; NM_123189.2.
DR AlphaFoldDB; Q9FF29; -.
DR SMR; Q9FF29; -.
DR STRING; 3702.AT5G38280.1; -.
DR PaxDb; Q9FF29; -.
DR PRIDE; Q9FF29; -.
DR ProteomicsDB; 225986; -.
DR EnsemblPlants; AT5G38280.1; AT5G38280.1; AT5G38280.
DR GeneID; 833810; -.
DR Gramene; AT5G38280.1; AT5G38280.1; AT5G38280.
DR KEGG; ath:AT5G38280; -.
DR Araport; AT5G38280; -.
DR TAIR; locus:2176737; AT5G38280.
DR eggNOG; ENOG502SK6K; Eukaryota.
DR HOGENOM; CLU_000288_170_0_1; -.
DR InParanoid; Q9FF29; -.
DR OMA; LACKAYG; -.
DR PhylomeDB; Q9FF29; -.
DR PRO; PR:Q9FF29; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FF29; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; ISS:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009620; P:response to fungus; ISS:TAIR.
DR Gene3D; 2.60.110.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR045874; LRK10-like.
DR InterPro; IPR037176; Osmotin/thaumatin-like_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001938; Thaumatin.
DR InterPro; IPR017949; Thaumatin_CS.
DR PANTHER; PTHR27009; PTHR27009; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00314; Thaumatin; 1.
DR PRINTS; PR00347; THAUMATIN.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00205; THN; 1.
DR SUPFAM; SSF49870; SSF49870; 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.
DR PROSITE; PS00316; THAUMATIN_1; 1.
DR PROSITE; PS51367; THAUMATIN_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..665
FT /note="PR5-like receptor kinase"
FT /id="PRO_5011950818"
FT TOPO_DOM 25..276
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..665
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 331..620
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 455
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 337..345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 33..249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 81..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 96..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 153..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 158..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 166..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 188..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 198..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT MUTAGEN 360
FT /note="K->R: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:8637920"
FT CONFLICT 25
FT /note="R -> T (in Ref. 1; AAC49208)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="G -> E (in Ref. 1; AAC49208)"
FT /evidence="ECO:0000305"
FT CONFLICT 567..576
FT /note="DSITDEEEKI -> NSITEEEEKF (in Ref. 1; AAC49208)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="I -> T (in Ref. 1; AAC49208)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="D -> A (in Ref. 1; AAC49208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 665 AA; 73952 MW; 9456BEC20C47B79E CRC64;
MVEGFSLSLM FLLVSHFFVS GVMSRNFTIE NKCDYTVWPG FLTMTTAVSL PTNGFSLKKG
ESRVINVPPS WSGRLWGRSF CSTSSTGNFS CATGDCGSGK IECSDSGARP PTTLIDFTLD
ATDGQDFYDV SVVDGYNLPL VVVPQRLGSG RTCSNVGCVV NLNKTCPSEL KVMGSSNKEH
PIACMNACQK FGLPEFCCYG EYGKPAKCQP TLYSTNFKNE CPLAYSYAYD NENNTFRCSN
SPNYVITFCP NDISSMSQPS KETNGGTKQK SSWKLKLIVG VSAALTLMIL IVVVIIVRTK
NMRNSEWNDQ NVEAVAMLKR YSYTRVKKMT NSFAHVLGKG GFGTVYKGKL ADSGRDVAVK
ILKVSEGNGE EFINEVASMS RTSHVNIVSL LGFCYEKNKR AIIYEFMPNG SLDKYISANM
STKMEWERLY DVAVGISRGL EYLHNRCVTR IVHFDIKPQN ILMDENLCPK ISDFGLAKLC
KNKESIISML HMRGTFGYIA PEMFSKNFGA VSHKSDVYSY GMVVLEMIGA KNIEKVEYSG
SNNGSMYFPE WVYKDFEKGE ITRIFGDSIT DEEEKIAKKL VLVALWCIQM NPSDRPPMIK
VIEMLEGNLE ALQVPPNPLL FSPEETVPDT LEDSDDTSTF FNPSHFERGT LLDSEDVLQH
GSRSS
