CRK1_ARATH
ID CRK1_ARATH Reviewed; 615 AA.
AC Q9LMB9; F4IE05; O22580;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Cysteine-rich receptor-like protein kinase 1 {ECO:0000305};
DE Short=Cysteine-rich RLK1 {ECO:0000303|PubMed:11402176};
DE EC=2.7.11.1;
DE AltName: Full=Receptor-like kinase in flowers 2 {ECO:0000303|PubMed:9687063};
DE Flags: Precursor;
GN Name=CRK1 {ECO:0000303|PubMed:11402176};
GN Synonyms=RKF2 {ECO:0000303|PubMed:9687063}; OrderedLocusNames=At1g19090;
GN ORFNames=F14D16.24;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9687063; DOI=10.1023/a:1005924817190;
RA Takahashi T., Mu J.-H., Gasch A., Chua N.-H.;
RT "Identification by PCR of receptor-like protein kinases from Arabidopsis
RT flowers.";
RL Plant Mol. Biol. 37:587-596(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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).
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; 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: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the whole plant at low levels.
CC {ECO:0000269|PubMed:9687063}.
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=AAC50044.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF79292.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF024649; AAC50044.1; ALT_FRAME; mRNA.
DR EMBL; AC068602; AAF79292.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP002684; AEE29801.2; -; Genomic_DNA.
DR RefSeq; NP_001319040.1; NM_001332384.1.
DR AlphaFoldDB; Q9LMB9; -.
DR SMR; Q9LMB9; -.
DR BioGRID; 23730; 2.
DR IntAct; Q9LMB9; 2.
DR STRING; 3702.AT1G19090.1; -.
DR PaxDb; Q9LMB9; -.
DR PRIDE; Q9LMB9; -.
DR GeneID; 838491; -.
DR KEGG; ath:AT1G19090; -.
DR Araport; AT1G19090; -.
DR eggNOG; ENOG502QRU4; Eukaryota.
DR HOGENOM; CLU_000288_35_6_1; -.
DR InParanoid; Q9LMB9; -.
DR OrthoDB; 295093at2759; -.
DR PhylomeDB; Q9LMB9; -.
DR PRO; PR:Q9LMB9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMB9; baseline and differential.
DR Genevisible; Q9LMB9; 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; 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; 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; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..615
FT /note="Cysteine-rich receptor-like protein kinase 1"
FT /id="PRO_0000295048"
FT TOPO_DOM 29..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..615
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..131
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 137..237
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 318..602
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 443
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 324..332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 346
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 240
FT /note="D -> DD (in Ref. 1; AAC50044)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="S -> SS (in Ref. 1; AAC50044)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 615 AA; 69176 MW; 062B0FE15744DA86 CRC64;
MQICASIAQF LAWVSFLVLL ATVGSSSSSE SLLNCQPLDH HLVNPSRLLG FLRAMSSVND
FITNDKLWVV SSITDVSPPI YVFLQCREDL SVSDCRHCFN ESRLELERKC SGSGGRIHSD
RCFLRFDDRD FSEEFVDPTF DKANCEETGT GFGEFWRFLD EALVNVTLKA VKNGGFGAAS
VIKTEAVYAL AQCWQTLDEN TCRECLVNAR SSLRACDGHE ARAFFTGCYL KYSTHKFFDD
AAEHKPDADQ RNFIRSSFFP HLSDRDVTRL AIAAISLSIL TSLGAFISYR RVSRKRKAQV
PSCVNFKYEM LEKATESFHD SMKLGQGGAG SVYKGILPDG RIVAVKKLFF NTREWADQFF
NEVNLISGVQ HKNLVRLLGC SIEGPKSLLV YEYVHNRSLD QILFMKNTVH ILSWKQRFNI
IIGISEGLEY LHRGSEVKII HRDIKTSNIL LDRNLSPKIA DFGLIRSMGT DKTQTNTGIA
GTLGYLAPEY LIKGQLTEKA DVYAFGVLII EIVTGKKNNA FTQGTSSVLY SVWEHFKANT
LDRSIDPRLK GSFVEEEALK VLQIGLLCVQ SSVELRPSMS EIVFMLQNKD SKFEYPKQPP
FLSASVLMPD EETRV
