CE101_ARATH
ID CE101_ARATH Reviewed; 850 AA.
AC Q9LW83;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase CES101;
DE EC=2.7.11.1;
DE AltName: Full=Protein CALLUS EXPRESSION OF RBCS 101;
DE Flags: Precursor;
GN Name=CES101; OrderedLocusNames=At3g16030; ORFNames=MSL1.2;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=16597626; DOI=10.1093/pcp/pci242;
RA Niwa Y., Goto S., Nakano T., Sakaiya M., Hirano T., Tsukaya H., Komeda Y.,
RA Kobayashi H.;
RT "Arabidopsis mutants by activation tagging in which photosynthesis genes
RT are expressed in dedifferentiated calli.";
RL Plant Cell Physiol. 47:319-331(2006).
CC -!- FUNCTION: Promotes the expression of genes involved in photosynthesis
CC at least in dedifferentiated calli. {ECO:0000269|PubMed:16597626}.
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 type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves, and, to a lower extent,
CC in roots and flowers. {ECO:0000269|PubMed:16597626}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02668.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB012247; BAB02668.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75764.1; -; Genomic_DNA.
DR RefSeq; NP_188224.1; NM_112473.2.
DR AlphaFoldDB; Q9LW83; -.
DR SMR; Q9LW83; -.
DR STRING; 3702.AT3G16030.1; -.
DR PaxDb; Q9LW83; -.
DR PRIDE; Q9LW83; -.
DR ProteomicsDB; 222605; -.
DR EnsemblPlants; AT3G16030.1; AT3G16030.1; AT3G16030.
DR GeneID; 820848; -.
DR Gramene; AT3G16030.1; AT3G16030.1; AT3G16030.
DR KEGG; ath:AT3G16030; -.
DR Araport; AT3G16030; -.
DR TAIR; locus:2093397; AT3G16030.
DR eggNOG; ENOG502QTRQ; Eukaryota.
DR HOGENOM; CLU_000288_116_7_1; -.
DR PRO; PR:Q9LW83; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LW83; baseline and differential.
DR Genevisible; Q9LW83; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate 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; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009620; P:response to fungus; IMP:TAIR.
DR CDD; cd00028; B_lectin; 1.
DR Gene3D; 2.90.10.10; -; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF08276; PAN_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; SSF51110; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein; Kinase; Lectin;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..850
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase CES101"
FT /id="PRO_0000401298"
FT TOPO_DOM 23..423
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..850
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..144
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 334..416
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 527..816
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 616..633
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 652
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 533..541
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 555
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 686
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 845
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 367..390
FT /evidence="ECO:0000250"
FT DISULFID 371..377
FT /evidence="ECO:0000250"
SQ SEQUENCE 850 AA; 96285 MW; 3F6B5435E5B0447F CRC64;
MWSNCIFLTL FTFYLFLGQS CCQTDTLLQG QYLKDGQELV SAFNIFKLKF FNFENSSNWY
LGIWYNNFYL SGAVWIANRN NPVLGRSGSL TVDSLGRLRI LRGASSLLEL SSTETTGNTT
LKLLDSGNLQ LQEMDSDGSM KRTLWQSFDY PTDTLLPGMK LGFNVKTGKR WELTSWLGDT
LPASGSFVFG MDDNITNRLT ILWLGNVYWA SGLWFKGGFS LEKLNTNGFI FSFVSTESEH
YFMYSGDENY GGPLFPRIRI DQQGSLQKIN LDGVKKHVHC SPSVFGEELE YGCYQQNFRN
CVPARYKEVT GSWDCSPFGF GYTYTRKTYD LSYCSRFGYT FRETVSPSAE NGFVFNEIGR
RLSSYDCYVK CLQNCSCVAY ASTNGDGTGC EIWNTDPTNE NSASHHPRTI YIRIKGSKLA
ATWLVVVASL FLIIPVTWLI IYLVLRKFKI KGTNFVSESL KMISSQSCSL TNKRLSTLRV
GSTIDQEMLL LELGIERRRR GKRSARNNNN ELQIFSFESV AFATDYFSDA NKLGEGGFGP
VYKGRLIDGE EVAIKRLSLA SGQGLVEFKN EAMLIAKLQH TNLVKLLGCC VEKDEKMLIY
EYMPNKSLDY FLFDPLRKIV LDWKLRFRIM EGIIQGLLYL HKYSRLKVIH RDIKAGNILL
DEDMNPKISD FGMARIFGAQ ESKANTKRVA GTFGYMSPEY FREGLFSAKS DVFSFGVLML
EIICGRKNNS FHHDSEGPLN LIVHVWNLFK ENRVREVIDP SLGDSAVENP QVLRCVQVAL
LCVQQNADDR PSMLDVVSMI YGDGNNALSL PKEPAFYDGP PRSSPEMEVE PPEMENVSAN
RVTITVMEAR
