CRLK2_ARATH
ID CRLK2_ARATH Reviewed; 436 AA.
AC Q9LFV3; Q570M6; Q8LCL1;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Calcium/calmodulin-regulated receptor-like kinase 2 {ECO:0000303|PubMed:21056039};
DE Short=AtCRLK2 {ECO:0000303|PubMed:21056039};
DE EC=2.7.11.1;
GN Name=CRLK2 {ECO:0000303|PubMed:21056039}; OrderedLocusNames=At5g15730;
GN ORFNames=F14F8.110;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY.
RX PubMed=21056039; DOI=10.1016/j.febslet.2010.10.059;
RA DeFalco T.A., Chiasson D., Munro K., Kaiser B.N., Snedden W.A.;
RT "Characterization of GmCaMK1, a member of a soybean calmodulin-binding
RT receptor-like kinase family.";
RL FEBS Lett. 584:4717-4724(2010).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LFV3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LFV3-2; Sequence=VSP_040159;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AL391144; CAC01772.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92198.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92199.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69538.1; -; Genomic_DNA.
DR EMBL; AK220682; BAD93743.1; -; mRNA.
DR EMBL; AY086538; AAM63603.1; -; mRNA.
DR PIR; T51402; T51402.
DR RefSeq; NP_001078591.1; NM_001085122.3. [Q9LFV3-1]
DR RefSeq; NP_001331208.1; NM_001343420.1. [Q9LFV3-1]
DR RefSeq; NP_568320.1; NM_121578.4. [Q9LFV3-2]
DR AlphaFoldDB; Q9LFV3; -.
DR SMR; Q9LFV3; -.
DR IntAct; Q9LFV3; 1.
DR MINT; Q9LFV3; -.
DR STRING; 3702.AT5G15730.2; -.
DR PaxDb; Q9LFV3; -.
DR PRIDE; Q9LFV3; -.
DR ProteomicsDB; 220341; -. [Q9LFV3-1]
DR EnsemblPlants; AT5G15730.1; AT5G15730.1; AT5G15730. [Q9LFV3-2]
DR EnsemblPlants; AT5G15730.2; AT5G15730.2; AT5G15730. [Q9LFV3-1]
DR EnsemblPlants; AT5G15730.3; AT5G15730.3; AT5G15730. [Q9LFV3-1]
DR GeneID; 831429; -.
DR Gramene; AT5G15730.1; AT5G15730.1; AT5G15730. [Q9LFV3-2]
DR Gramene; AT5G15730.2; AT5G15730.2; AT5G15730. [Q9LFV3-1]
DR Gramene; AT5G15730.3; AT5G15730.3; AT5G15730. [Q9LFV3-1]
DR KEGG; ath:AT5G15730; -.
DR Araport; AT5G15730; -.
DR TAIR; locus:2143166; AT5G15730.
DR eggNOG; KOG1187; Eukaryota.
DR InParanoid; Q9LFV3; -.
DR OMA; VDKGQHM; -.
DR PhylomeDB; Q9LFV3; -.
DR PRO; PR:Q9LFV3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFV3; baseline and differential.
DR Genevisible; Q9LFV3; 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:0009536; C:plastid; HDA:TAIR.
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; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..436
FT /note="Calcium/calmodulin-regulated receptor-like kinase 2"
FT /id="PRO_0000401332"
FT TRANSMEM 7..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 114..375
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 65..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 120..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 187
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 276
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 284
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT VAR_SEQ 202..203
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_040159"
FT CONFLICT 39
FT /note="L -> P (in Ref. 3; BAD93743)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 48761 MW; 54CE48B32B4CCACC CRC64;
MVNRSDLVVI GISVGLALGL LLALLLFFAI KWYYGRSHLR RCANEQNSPT LPVHTAKRGV
VIPDDRANTE SSQPPENGAP TQHQPWWNNH TKDLTVSASG IPRYNYKDIQ KATQNFTTVL
GQGSFGPVYK AVMPNGELAA AKVHGSNSSQ GDREFQTEVS LLGRLHHRNL VNLTGYCVDK
SHRMLIYEFM SNGSLENLLY GGEGMQVLNW EERLQIALDI SHGIEYLHEG AVPPVIHRDL
KSANILLDHS MRAKVADFGL SKEMVLDRMT SGLKGTHGYM DPTYISTNKY TMKSDIYSFG
VIILELITAI HPQQNLMEYI NLASMSPDGI DEILDQKLVG NASIEEVRLL AKIANRCVHK
TPRKRPSIGE VTQFILKIKQ SRSRGRRQDT MSSSFGVGYE EDLSRVMSRI KDQHVELGLL
AGVKEENHQE RNIATT
