CRK3_ARATH
ID CRK3_ARATH Reviewed; 646 AA.
AC Q9CAL2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cysteine-rich receptor-like protein kinase 3;
DE Short=Cysteine-rich RLK3;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=CRK3; OrderedLocusNames=At1g70530; ORFNames=F24J13.10;
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=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 [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 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC010796; AAG52470.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35075.1; -; Genomic_DNA.
DR PIR; C96729; C96729.
DR RefSeq; NP_177210.1; NM_105721.2.
DR AlphaFoldDB; Q9CAL2; -.
DR SMR; Q9CAL2; -.
DR STRING; 3702.AT1G70530.1; -.
DR iPTMnet; Q9CAL2; -.
DR PaxDb; Q9CAL2; -.
DR PRIDE; Q9CAL2; -.
DR ProteomicsDB; 222652; -.
DR EnsemblPlants; AT1G70530.1; AT1G70530.1; AT1G70530.
DR GeneID; 843390; -.
DR Gramene; AT1G70530.1; AT1G70530.1; AT1G70530.
DR KEGG; ath:AT1G70530; -.
DR Araport; AT1G70530; -.
DR TAIR; locus:2026785; AT1G70530.
DR eggNOG; ENOG502QVTV; Eukaryota.
DR HOGENOM; CLU_000288_35_6_1; -.
DR InParanoid; Q9CAL2; -.
DR OMA; IGSCPPK; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9CAL2; -.
DR SABIO-RK; Q9CAL2; -.
DR PRO; PR:Q9CAL2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAL2; baseline and differential.
DR Genevisible; Q9CAL2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..646
FT /note="Cysteine-rich receptor-like protein kinase 3"
FT /id="PRO_0000295050"
FT TOPO_DOM 21..260
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..131
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 139..241
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 323..578
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 621..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 448
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 329..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 396
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 482
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 487
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 495
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 646 AA; 71611 MW; EA976D025A08FE58 CRC64;
MPILTLLLLI LGLFISPSVS DSRGDTVAQI CNNRTTTPQQ RSLFVTNFLA AMDAVSPLVE
AKGYGQVVNG TGNLTVYAYG ECIKDLDKKD CDLCFAQIKA KVPRCLPFQK GTRGGQVFSD
GCYIRYDDYN FYNETLSLQD RTVCAPKEIT GVNRTVFRDN AAELVKNMSV EAVRNGGFYA
GFVDRHNVTV HGLAQCWETL NRSGCVECLS KASVRIGSCL VNEEGRVLSA GCYMRFSTQK
FYNNSGNSTS DGNGGHNHLG VILAVTSSVV AFVLLVSAAG FLLKKRHAKK QREKKQLGSL
FMLANKSNLC FSYENLERAT DYFSDKNKLG QGGSGSVYKG VLTNGKTVAV KRLFFNTKQW
VDHFFNEVNL ISQVDHKNLV KLLGCSITGP ESLLVYEYIA NQSLHDYLFV RKDVQPLNWA
KRFKIILGTA EGMAYLHEES NLRIIHRDIK LSNILLEDDF TPRIADFGLA RLFPEDKTHI
STAIAGTLGY MAPEYVVRGK LTEKADVYSF GVLMIEVITG KRNNAFVQDA GSILQSVWSL
YRTSNVEEAV DPILGDNFNK IEASRLLQIG LLCVQAAFDQ RPAMSVVVKM MKGSLEIHTP
TQPPFLNPGS VVEMRKMMMT PTTNQSNSSG SRSDYITEGS SFFEPR
