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Calmodulin-binding receptor kinase CaMRLK (EC 2.7.11.1) (Calmodulin-binding receptor-like kinase) (AtCaMRLK) (Protein MATERNAL EFFECT EMBRYO ARREST 62)

 CARLK_ARATH             Reviewed;         666 AA.
Q9FK63; A0A1P8BFN9; Q56ZY8; Q6QNV0;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
31-JAN-2018, entry version 138.
RecName: Full=Calmodulin-binding receptor kinase CaMRLK {ECO:0000305};
EC=2.7.11.1 {ECO:0000269|PubMed:14720124};
AltName: Full=Calmodulin-binding receptor-like kinase {ECO:0000303|PubMed:14720124};
Short=AtCaMRLK {ECO:0000303|PubMed:14720124};
AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 62 {ECO:0000303|PubMed:15634699};
Flags: Precursor;
Name=CAMRLK {ECO:0000303|PubMed:14720124};
Synonyms=MEE62 {ECO:0000303|PubMed:15634699};
OrderedLocusNames=At5g45800 {ECO:0000312|Araport:AT5G45800};
ORFNames=MRA19.24 {ECO:0000312|EMBL:BAB09223.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF
LYS-423, COFACTOR, INTERACTION WITH CAM1, AUTOPHOSPHORYLATION,
CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=14720124; DOI=10.1042/BJ20031045;
Charpenteau M., Jaworski K., Ramirez B.C., Tretyn A., Ranjeva R.,
Ranty B.;
"A receptor-like kinase from Arabidopsis thaliana is a calmodulin-
binding protein.";
Biochem. J. 379:841-848(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND GENE FAMILY.
STRAIN=cv. Columbia;
PubMed=20064227; DOI=10.1186/1471-2164-11-19;
Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
"Genome-wide cloning and sequence analysis of leucine-rich repeat
receptor-like protein kinase genes in Arabidopsis thaliana.";
BMC Genomics 11:19-19(2010).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9734815; DOI=10.1093/dnares/5.3.203;
Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. VI.
Sequence features of the regions of 1,367,185 bp covered by 19
physically assigned P1 and TAC clones.";
DNA Res. 5:203-216(1998).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 578-666 (ISOFORM 1).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
ENZYME REGULATION.
PubMed=15292241; DOI=10.1074/jbc.M402830200;
Yang T., Chaudhuri S., Yang L., Chen Y., Poovaiah B.W.;
"Calcium/calmodulin up-regulates a cytoplasmic receptor-like kinase in
plants.";
J. Biol. Chem. 279:42552-42559(2004).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15634699; DOI=10.1242/dev.01595;
Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S.,
Johnson C.S., Capron A., Xie L.-F., Ye D., Sundaresan V.;
"Genetic and molecular identification of genes required for female
gametophyte development and function in Arabidopsis.";
Development 132:603-614(2005).
[9]
INDUCTION BY P.BRASSICAE OVIPOSITION.
PubMed=17142483; DOI=10.1104/pp.106.090837;
Little D., Gouhier-Darimont C., Bruessow F., Reymond P.;
"Oviposition by pierid butterflies triggers defense responses in
Arabidopsis.";
Plant Physiol. 143:784-800(2007).
[10]
DISRUPTION PHENOTYPE.
PubMed=21431781; DOI=10.1007/s11103-011-9769-x;
ten Hove C.A., Bochdanovits Z., Jansweijer V.M., Koning F.G.,
Berke L., Sanchez-Perez G.F., Scheres B., Heidstra R.;
"Probing the roles of LRR RLK genes in Arabidopsis thaliana roots
using a custom T-DNA insertion set.";
Plant Mol. Biol. 76:69-83(2011).
-!- FUNCTION: Can phosphorylate the myelin basic protein in vitro
(PubMed:14720124). Required for endosperm development in embryos
(PubMed:15634699). Maybe involved in auxin and osmotic stress
responses (PubMed:21431781). {ECO:0000269|PubMed:14720124,
ECO:0000269|PubMed:15634699, ECO:0000269|PubMed:21431781}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:14720124}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:14720124};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:14720124};
Note=Uses manganese ion preferentially to magnesium ion.
{ECO:0000269|PubMed:14720124};
-!- ENZYME REGULATION: Not stimulated by calmodulin (CaM).
{ECO:0000303|PubMed:15292241}.
-!- SUBUNIT: Binds calmodulin (CaM) in a calcium-dependent manner.
Interacts with CAM1, but not with CAM8.
{ECO:0000269|PubMed:14720124}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
membrane protein {ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9FK63-1; Sequence=Displayed;
Name=2;
IsoId=Q9FK63-2; Sequence=VSP_058921, VSP_058922;
Note=No experimental confirmation available.
{ECO:0000312|EMBL:ANM70401.1};
-!- TISSUE SPECIFICITY: Expressed in reproductive and vegetative
tissues, with higher levels in seedlings and flowers, but not in
leaves. {ECO:0000269|PubMed:14720124}.
-!- INDUCTION: Induced after P.brassicae oviposition.
{ECO:0000269|PubMed:17142483}.
-!- PTM: Calmodulin (CaM)-independent autophosphorylation.
{ECO:0000269|PubMed:14720124}.
-!- DISRUPTION PHENOTYPE: Endosperm development arrested at one-cell
zygotic stage (PubMed:15634699). Increased resistance to auxin
(e.g. IAA and NPA) and osmotic stress (e.g. mannitol)
(PubMed:21431781). {ECO:0000269|PubMed:15634699,
ECO:0000269|PubMed:21431781}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AY531551; AAS21681.1; -; mRNA.
EMBL; FJ708790; ACN59381.1; -; mRNA.
EMBL; AB012245; BAB09223.1; -; Genomic_DNA.
EMBL; CP002688; AED95301.1; -; Genomic_DNA.
EMBL; CP002688; ANM70401.1; -; Genomic_DNA.
EMBL; AY072097; AAL59919.1; -; mRNA.
EMBL; AY096584; AAM20234.1; -; mRNA.
EMBL; AK220822; BAD94117.1; -; mRNA.
RefSeq; NP_001332015.1; NM_001344640.1. [Q9FK63-2]
RefSeq; NP_199392.1; NM_123948.5. [Q9FK63-1]
UniGene; At.29993; -.
STRING; 3702.AT5G45800.1; -.
PaxDb; Q9FK63; -.
EnsemblPlants; AT5G45800.1; AT5G45800.1; AT5G45800. [Q9FK63-1]
EnsemblPlants; AT5G45800.2; AT5G45800.2; AT5G45800. [Q9FK63-2]
GeneID; 834620; -.
Gramene; AT5G45800.1; AT5G45800.1; AT5G45800. [Q9FK63-1]
Gramene; AT5G45800.2; AT5G45800.2; AT5G45800. [Q9FK63-2]
KEGG; ath:AT5G45800; -.
Araport; AT5G45800; -.
TAIR; locus:2171988; AT5G45800.
eggNOG; ENOG410IJ8Y; Eukaryota.
eggNOG; ENOG410XUCB; LUCA.
HOGENOM; HOG000238936; -.
OMA; NAMQGRF; -.
OrthoDB; EOG093604AR; -.
PRO; PR:Q9FK63; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FK63; baseline and differential.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0009733; P:response to auxin; IMP:UniProtKB.
GO; GO:0009625; P:response to insect; IEP:UniProtKB.
GO; GO:0006970; P:response to osmotic stress; IMP:UniProtKB.
Gene3D; 3.80.10.10; -; 2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR025875; Leu-rich_rpt_4.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
Pfam; PF12799; LRR_4; 1.
Pfam; PF13855; LRR_8; 2.
Pfam; PF07714; Pkinase_Tyr; 2.
SMART; SM00369; LRR_TYP; 3.
SUPFAM; SSF52058; SSF52058; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51450; LRR; 6.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Calmodulin-binding; Cell membrane;
Complete proteome; Glycoprotein; Kinase; Leucine-rich repeat;
Magnesium; Manganese; Membrane; Nucleotide-binding; Phosphoprotein;
Receptor; Reference proteome; Repeat; Signal; Transferase;
Transmembrane; Transmembrane helix.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 666 Calmodulin-binding receptor kinase
CaMRLK.
/FTId=PRO_5009973812.
TOPO_DOM 18 297 Extracellular. {ECO:0000305}.
TRANSMEM 298 318 Helical. {ECO:0000255}.
TOPO_DOM 319 666 Cytoplasmic. {ECO:0000305}.
REPEAT 79 103 LRR 1. {ECO:0000255}.
REPEAT 105 127 LRR 2. {ECO:0000255}.
REPEAT 130 152 LRR 3. {ECO:0000255}.
REPEAT 153 177 LRR 4. {ECO:0000255}.
REPEAT 178 197 LRR 5. {ECO:0000255}.
REPEAT 198 224 LRR 6. {ECO:0000255}.
REPEAT 226 246 LRR 7. {ECO:0000255}.
DOMAIN 395 661 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 401 409 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 319 337 Calmodulin binding.
{ECO:0000269|PubMed:14720124}.
BINDING 423 423 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CARBOHYD 27 27 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 52 52 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 137 137 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 148 148 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 154 154 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 189 189 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 261 261 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
VAR_SEQ 462 490 KEKLILYEFMANGDLHRWLHELPAGETNV -> LFHLVFLL
VDDWDDFKICADKSHPLLWDS (in isoform 2).
/FTId=VSP_058921.
VAR_SEQ 491 666 Missing (in isoform 2).
/FTId=VSP_058922.
MUTAGEN 423 423 K->A: Complete loss of kinase activity.
{ECO:0000269|PubMed:14720124}.
CONFLICT 303 303 S -> F (in Ref. 1; AAS21681).
{ECO:0000305}.
CONFLICT 580 580 S -> R (in Ref. 6; BAD94117).
{ECO:0000305}.
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


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