Y5248_ARATH
ID Y5248_ARATH Reviewed; 872 AA.
AC Q9FLV4; F4KFQ0;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At5g24080;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At5g24080; ORFNames=MZF18.3;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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] OF 367-872.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AY056241; Type=Frameshift; Evidence={ECO:0000305};
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; AB009056; BAB08731.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69103.1; -; Genomic_DNA.
DR EMBL; AY056241; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001330805.1; NM_001343839.1.
DR AlphaFoldDB; Q9FLV4; -.
DR SMR; Q9FLV4; -.
DR BioGRID; 17748; 7.
DR IntAct; Q9FLV4; 7.
DR PaxDb; Q9FLV4; -.
DR PRIDE; Q9FLV4; -.
DR EnsemblPlants; AT5G24080.2; AT5G24080.2; AT5G24080.
DR GeneID; 832473; -.
DR Gramene; AT5G24080.2; AT5G24080.2; AT5G24080.
DR KEGG; ath:AT5G24080; -.
DR Araport; AT5G24080; -.
DR eggNOG; ENOG502QTC9; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q9FLV4; -.
DR OMA; QFRISTV; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9FLV4; -.
DR PRO; PR:Q9FLV4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLV4; baseline and differential.
DR Genevisible; Q9FLV4; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0031625; F:ubiquitin protein ligase binding; IEA:UniProt.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00954; S_locus_glycop; 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; 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; Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein;
KW Kinase; Lectin; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..872
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase At5g24080"
FT /id="PRO_0000401330"
FT TOPO_DOM 26..472
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..872
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..149
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 306..344
FT /note="EGF-like; atypical"
FT DOMAIN 360..447
FT /note="PAN"
FT DOMAIN 530..810
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 619..637
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 656
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 536..544
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 558
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 521
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 603
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 690
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 695
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 310..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DISULFID 316..332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DISULFID 400..424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DISULFID 404..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
SQ SEQUENCE 872 AA; 97311 MW; 01DA1501971E0024 CRC64;
MSSFHFYFPS VGLFSFFCFF LVSLATEPHI GLGSKLKASE PNRAWVSANG TFAIGFTRFK
PTDRFLLSIW FAQLPGDPTI VWSPNRNSPV TKEAVLELEA TGNLVLSDQN TVVWTSNTSN
HGVESAVMSE SGNFLLLGTE VTAGPTIWQS FSQPSDTLLP NQPLTVSLEL TSNPSPSRHG
HYSLKMLQQH TSLSLGLTYN INLDPHANYS YWSGPDISNV TGDVTAVLDD TGSFKIVYGE
SSIGAVYVYK NPVDDNRNYN NSSNLGLTKN PVLRRLVLEN NGNLRLYRWD NDMNGSSQWV
PEWAAVSNPC DIAGICGNGV CNLDRTKKNA DCLCLPGSVK LPDQENAKLC SDNSSLVQEC
ESNINRNGSF KISTVQETNY YFSERSVIEN ISDISNVRKC GEMCLSDCKC VASVYGLDDE
KPYCWILKSL NFGGFRDPGS TLFVKTRANE SYPSNSNNND SKSRKSHGLR QKVLVIPIVV
GMLVLVALLG MLLYYNLDRK RTLKRAAKNS LILCDSPVSF TYRDLQNCTN NFSQLLGSGG
FGTVYKGTVA GETLVAVKRL DRALSHGERE FITEVNTIGS MHHMNLVRLC GYCSEDSHRL
LVYEYMINGS LDKWIFSSEQ TANLLDWRTR FEIAVATAQG IAYFHEQCRN RIIHCDIKPE
NILLDDNFCP KVSDFGLAKM MGREHSHVVT MIRGTRGYLA PEWVSNRPIT VKADVYSYGM
LLLEIVGGRR NLDMSYDAED FFYPGWAYKE LTNGTSLKAV DKRLQGVAEE EEVVKALKVA
FWCIQDEVSM RPSMGEVVKL LEGTSDEINL PPMPQTILEL IEEGLEDVYR AMRREFNNQL
SSLTVNTITT SQSYRSSSRS HATCSYSSMS PR
