CRK42_ARATH
ID CRK42_ARATH Reviewed; 651 AA.
AC Q9FNE1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cysteine-rich receptor-like protein kinase 42;
DE Short=Cysteine-rich RLK42;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=CRK42; OrderedLocusNames=At5g40380; ORFNames=MPO12.90;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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] OF 10-642.
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 ORGANIZATION, AND NOMENCLATURE.
RX PubMed=11402176; DOI=10.1104/pp.126.2.473;
RA Chen Z.;
RT "A superfamily of proteins with novel cysteine-rich repeats.";
RL Plant Physiol. 126:473-476(2001).
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;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CRK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX829950; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB006702; BAB11593.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94540.1; -; Genomic_DNA.
DR EMBL; BX829950; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_198854.3; NM_123402.5.
DR AlphaFoldDB; Q9FNE1; -.
DR SMR; Q9FNE1; -.
DR BioGRID; 19287; 1.
DR IntAct; Q9FNE1; 1.
DR STRING; 3702.AT5G40380.1; -.
DR PaxDb; Q9FNE1; -.
DR PRIDE; Q9FNE1; -.
DR ProteomicsDB; 220347; -.
DR EnsemblPlants; AT5G40380.1; AT5G40380.1; AT5G40380.
DR GeneID; 834036; -.
DR Gramene; AT5G40380.1; AT5G40380.1; AT5G40380.
DR KEGG; ath:AT5G40380; -.
DR Araport; AT5G40380; -.
DR TAIR; locus:2170598; AT5G40380.
DR eggNOG; ENOG502QRU4; Eukaryota.
DR HOGENOM; CLU_000288_35_6_1; -.
DR InParanoid; Q9FNE1; -.
DR OMA; YGFAQCF; -.
DR OrthoDB; 295093at2759; -.
DR PhylomeDB; Q9FNE1; -.
DR PRO; PR:Q9FNE1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNE1; baseline and differential.
DR Genevisible; Q9FNE1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 3.30.430.20; -; 2.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01657; Stress-antifung; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51473; GNK2; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..651
FT /note="Cysteine-rich receptor-like protein kinase 42"
FT /id="PRO_0000295089"
FT TOPO_DOM 29..251
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..135
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 137..236
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 315..604
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 440
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 321..329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 388
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 474
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 479
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 487
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 340
FT /note="V -> L (in Ref. 3; BX829950)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="V -> F (in Ref. 3; BX829950)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="A -> E (in Ref. 3; BX829950)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="G -> V (in Ref. 3; BX829950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 651 AA; 72706 MW; 6E4CC556E66FDCB9 CRC64;
MRCLTKTRSF HYVIIFYSFF FLPFLSSSSD DQRTTVSGLF CGGRSKSSAD PNYIPTFVED
MHSLSLKLTT RRFATESLNS TTSIYALIQC HDDLSPSDCQ LCYAIARTRI PRCLPSSSAR
IFLDGCFLRY ETYEFYDESV SDASDSFSCS NDTVLDPRFG FQVSETAARV AVRKGGFGVA
GENGVHALAQ CWESLGKEDC RVCLEKAVKE VKRCVSRREG RAMNTGCYLR YSDHKFYNGD
GHHKFHVLFN KGVIVAIVLT TSAFVMLILL ATYVIMTKVS KTKQEKRNLG LVSRKFNNSK
TKFKYETLEK ATDYFSHKKM LGQGGNGTVF LGILPNGKNV AVKRLVFNTR DWVEEFFNEV
NLISGIQHKN LVKLLGCSIE GPESLLVYEY VPNKSLDQFL FDESQSKVLN WSQRLNIILG
TAEGLAYLHG GSPVRIIHRD IKTSNVLLDD QLNPKIADFG LARCFGLDKT HLSTGIAGTL
GYMAPEYVVR GQLTEKADVY SFGVLVLEIA CGTRINAFVP ETGHLLQRVW NLYTLNRLVE
ALDPCLKDEF LQVQGSEAEA CKVLRVGLLC TQASPSLRPS MEEVIRMLTE RDYPIPSPTS
PPFLRVSSLT TDLEGSSTIS HSTNSTTTFN TMVKTDQASY TSSESSTTRT I
