CARLK_ARATH
ID CARLK_ARATH Reviewed; 666 AA.
AC Q9FK63; A0A1P8BFN9; Q56ZY8; Q6QNV0;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Calmodulin-binding receptor kinase CaMRLK {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:14720124};
DE AltName: Full=Calmodulin-binding receptor-like kinase {ECO:0000303|PubMed:14720124};
DE Short=AtCaMRLK {ECO:0000303|PubMed:14720124};
DE AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 62 {ECO:0000303|PubMed:15634699};
DE Flags: Precursor;
GN Name=CAMRLK {ECO:0000303|PubMed:14720124};
GN Synonyms=MEE62 {ECO:0000303|PubMed:15634699};
GN OrderedLocusNames=At5g45800 {ECO:0000312|Araport:AT5G45800};
GN ORFNames=MRA19.24 {ECO:0000312|EMBL:BAB09223.1};
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] (ISOFORM 1), FUNCTION, MUTAGENESIS OF LYS-423,
RP COFACTOR, INTERACTION WITH CAM1, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY,
RP AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=14720124; DOI=10.1042/bj20031045;
RA Charpenteau M., Jaworski K., Ramirez B.C., Tretyn A., Ranjeva R., Ranty B.;
RT "A receptor-like kinase from Arabidopsis thaliana is a calmodulin-binding
RT protein.";
RL Biochem. J. 379:841-848(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 578-666 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=15292241; DOI=10.1074/jbc.m402830200;
RA Yang T., Chaudhuri S., Yang L., Chen Y., Poovaiah B.W.;
RT "Calcium/calmodulin up-regulates a cytoplasmic receptor-like kinase in
RT plants.";
RL J. Biol. Chem. 279:42552-42559(2004).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15634699; DOI=10.1242/dev.01595;
RA Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT "Genetic and molecular identification of genes required for female
RT gametophyte development and function in Arabidopsis.";
RL Development 132:603-614(2005).
RN [9]
RP INDUCTION BY P.BRASSICAE OVIPOSITION.
RX PubMed=17142483; DOI=10.1104/pp.106.090837;
RA Little D., Gouhier-Darimont C., Bruessow F., Reymond P.;
RT "Oviposition by pierid butterflies triggers defense responses in
RT Arabidopsis.";
RL Plant Physiol. 143:784-800(2007).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=21431781; DOI=10.1007/s11103-011-9769-x;
RA ten Hove C.A., Bochdanovits Z., Jansweijer V.M., Koning F.G., Berke L.,
RA Sanchez-Perez G.F., Scheres B., Heidstra R.;
RT "Probing the roles of LRR RLK genes in Arabidopsis thaliana roots using a
RT custom T-DNA insertion set.";
RL Plant Mol. Biol. 76:69-83(2011).
CC -!- FUNCTION: Can phosphorylate the myelin basic protein in vitro
CC (PubMed:14720124). Required for endosperm development in embryos
CC (PubMed:15634699). Maybe involved in auxin and osmotic stress responses
CC (PubMed:21431781). {ECO:0000269|PubMed:14720124,
CC ECO:0000269|PubMed:15634699, ECO:0000269|PubMed:21431781}.
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:14720124};
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:14720124};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:14720124};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:14720124};
CC Note=Uses manganese ion preferentially to magnesium ion.
CC {ECO:0000269|PubMed:14720124};
CC -!- ACTIVITY REGULATION: Not stimulated by calmodulin (CaM).
CC {ECO:0000303|PubMed:15292241}.
CC -!- SUBUNIT: Binds calmodulin (CaM) in a calcium-dependent manner.
CC Interacts with CAM1, but not with CAM8. {ECO:0000269|PubMed:14720124}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FK63-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FK63-2; Sequence=VSP_058921, VSP_058922;
CC -!- TISSUE SPECIFICITY: Expressed in reproductive and vegetative tissues,
CC with higher levels in seedlings and flowers, but not in leaves.
CC {ECO:0000269|PubMed:14720124}.
CC -!- INDUCTION: Induced after P.brassicae oviposition.
CC {ECO:0000269|PubMed:17142483}.
CC -!- PTM: Calmodulin (CaM)-independent autophosphorylation.
CC {ECO:0000269|PubMed:14720124}.
CC -!- DISRUPTION PHENOTYPE: Endosperm development arrested at one-cell
CC zygotic stage (PubMed:15634699). Increased resistance to auxin (e.g.
CC IAA and NPA) and osmotic stress (e.g. mannitol) (PubMed:21431781).
CC {ECO:0000269|PubMed:15634699, ECO:0000269|PubMed:21431781}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AY531551; AAS21681.1; -; mRNA.
DR EMBL; FJ708790; ACN59381.1; -; mRNA.
DR EMBL; AB012245; BAB09223.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95301.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70401.1; -; Genomic_DNA.
DR EMBL; AY072097; AAL59919.1; -; mRNA.
DR EMBL; AY096584; AAM20234.1; -; mRNA.
DR EMBL; AK220822; BAD94117.1; -; mRNA.
DR RefSeq; NP_001332015.1; NM_001344640.1. [Q9FK63-2]
DR RefSeq; NP_199392.1; NM_123948.5. [Q9FK63-1]
DR AlphaFoldDB; Q9FK63; -.
DR SMR; Q9FK63; -.
DR IntAct; Q9FK63; 4.
DR STRING; 3702.AT5G45800.1; -.
DR PaxDb; Q9FK63; -.
DR PRIDE; Q9FK63; -.
DR ProteomicsDB; 240251; -. [Q9FK63-1]
DR EnsemblPlants; AT5G45800.1; AT5G45800.1; AT5G45800. [Q9FK63-1]
DR EnsemblPlants; AT5G45800.2; AT5G45800.2; AT5G45800. [Q9FK63-2]
DR GeneID; 834620; -.
DR Gramene; AT5G45800.1; AT5G45800.1; AT5G45800. [Q9FK63-1]
DR Gramene; AT5G45800.2; AT5G45800.2; AT5G45800. [Q9FK63-2]
DR KEGG; ath:AT5G45800; -.
DR Araport; AT5G45800; -.
DR TAIR; locus:2171988; AT5G45800.
DR eggNOG; ENOG502QSF1; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; Q9FK63; -.
DR OMA; NAMQGRF; -.
DR PhylomeDB; Q9FK63; -.
DR PRO; PR:Q9FK63; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK63; baseline and differential.
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:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IMP:UniProtKB.
DR GO; GO:0009625; P:response to insect; IEP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 6.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Calmodulin-binding; Cell membrane;
KW Glycoprotein; Kinase; Leucine-rich repeat; Magnesium; Manganese; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..666
FT /note="Calmodulin-binding receptor kinase CaMRLK"
FT /id="PRO_5009973812"
FT TOPO_DOM 18..297
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..666
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 79..103
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 105..127
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 130..152
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 153..177
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 178..197
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 198..224
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 226..246
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT DOMAIN 395..661
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 319..337
FT /note="Calmodulin binding"
FT /evidence="ECO:0000269|PubMed:14720124"
FT BINDING 401..409
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 462..490
FT /note="KEKLILYEFMANGDLHRWLHELPAGETNV -> LFHLVFLLVDDWDDFKICA
FT DKSHPLLWDS (in isoform 2)"
FT /id="VSP_058921"
FT VAR_SEQ 491..666
FT /note="Missing (in isoform 2)"
FT /id="VSP_058922"
FT MUTAGEN 423
FT /note="K->A: Complete loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:14720124"
FT CONFLICT 303
FT /note="S -> F (in Ref. 1; AAS21681)"
FT /evidence="ECO:0000305"
FT CONFLICT 580
FT /note="S -> R (in Ref. 6; BAD94117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 666 AA; 73893 MW; 54365411909D1159 CRC64;
MFLKLFLLLS LVSFSHSDSS STVSCPNGTD FHQLTTVFRY VSGFNSSWFS SNCSAVITHV
VLPSRKLNGT VSWNPIRNLT RLRVLDLSNN SLDGSLPTWL WSMPGLVSVN LSRNRFGGSI
RVIPVNGSVL SAVKELNLSF NRFKHAVNFT GFTNLTTLDL SHNSLGVLPL GLGSLSGLRH
LDISRCKING SVKPISGLKS LDYLDLSENS MNGSFPVDFP NLNHLQFLNL SANRFSGSVG
FDKYRKFGKS AFLHGGDFVF NDSKIPYHHR IHRLPHRHPP PVRQRNVKTH RTNHTPLVIG
LSSSLGALII VIFAAAIILI RRRMKSARTK SRWAISNPTP LDFKMEKSGP FEFGTESGSS
WVADIKEPTA APVVMASKPL MNLTFKDLIV ATSHFGTESV ISDGTCGPLY RAVLPGDLHV
AIKVLERIRD VDQNDAVTAF EALTRLKHPN LLTLSGYCIA GKEKLILYEF MANGDLHRWL
HELPAGETNV EDWSADTWES HVGDSSPEKT NWLIRHRIAI GVARGLAYLH HVGTTHGHLV
ATNILLTETL EPRISDFGIN NIARTGDDTN KNNVEFDVYS FGVILFELLT GKQGSDENVK
SVRRLVKERR GEEALDSRLR LAAGESVNEM VESLRIGYFC TAETPVKRPT MQQVLGLLKD
IRTVSR
