Y5241_ARATH
ID Y5241_ARATH Reviewed; 824 AA.
AC Q9FLW0; Q8RXW4;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Probable receptor-like protein kinase At5g24010;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN OrderedLocusNames=At5g24010; ORFNames=MZF18.11;
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 493-824.
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200;
RA Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA Barbier-Brygoo H., Ephritikhine G.;
RT "A high content in lipid-modified peripheral proteins and integral receptor
RT kinases features in the arabidopsis plasma membrane proteome.";
RL Mol. Cell. Proteomics 6:1980-1996(2007).
RN [7]
RP GENE FAMILY.
RX PubMed=19529822; DOI=10.1093/mp/ssn083;
RA Chae L., Sudat S., Dudoit S., Zhu T., Luan S.;
RT "Diverse transcriptional programs associated with environmental stress and
RT hormones in the Arabidopsis receptor-like kinase gene family.";
RL Mol. Plant 2:84-107(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:17644812}; Single-
CC pass type I membrane protein {ECO:0000305|PubMed:17644812}.
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; AB009056; BAB08724.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93245.1; -; Genomic_DNA.
DR EMBL; AY080639; AAL85985.1; -; mRNA.
DR RefSeq; NP_197789.1; NM_122306.3.
DR AlphaFoldDB; Q9FLW0; -.
DR SMR; Q9FLW0; -.
DR BioGRID; 17741; 28.
DR IntAct; Q9FLW0; 28.
DR STRING; 3702.AT5G24010.1; -.
DR iPTMnet; Q9FLW0; -.
DR PaxDb; Q9FLW0; -.
DR PRIDE; Q9FLW0; -.
DR ProteomicsDB; 243132; -.
DR EnsemblPlants; AT5G24010.1; AT5G24010.1; AT5G24010.
DR GeneID; 832466; -.
DR Gramene; AT5G24010.1; AT5G24010.1; AT5G24010.
DR KEGG; ath:AT5G24010; -.
DR Araport; AT5G24010; -.
DR TAIR; locus:2178707; AT5G24010.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_42_1_1; -.
DR InParanoid; Q9FLW0; -.
DR OMA; GQRIPFA; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9FLW0; -.
DR PRO; PR:Q9FLW0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLW0; baseline and differential.
DR Genevisible; Q9FLW0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR InterPro; IPR045272; ANXUR1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024788; Malectin-like_Carb-bd_dom.
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 PANTHER; PTHR27003; PTHR27003; 1.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..824
FT /note="Probable receptor-like protein kinase At5g24010"
FT /id="PRO_0000386558"
FT TOPO_DOM 25..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..824
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 489..764
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 440..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 613
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 495..503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 640
FT /note="C -> Y (in Ref. 3; AAL85985)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 824 AA; 91823 MW; 5150D0CF3E05393B CRC64;
MAFPINLTQT LLFFFCPLLH LSFAAFTPTD NYLINSGSNT NTSFFTTRSF LSDSSEPGSS
FLSTDRSISI SDTNPSPDSP VLYNTARVFP VGGSYKFQVT TKGTHFIRLH FAPFKASRFN
LRSAKFRVLI NGFSVINSFS TSSVVVKEFI LKIDDPVLEI SFLPFKASGF GFVNAVEVFS
APKDYIMDQG TKLVIPNSAQ IFSNLSSQVL ETVHRINVGG SKLTPFNDTL WRTWVVDDNY
LLLRAAARRA WTTHSPNYQN GGATREIAPD NVYMTAQEMD RDNQELQARF NISWGFQVDE
KRVLHLVRLH FCDIVSSSLN QLYFNVFINE YLAFKDVDLS TLTFHVLASP LYIDFVAESD
RSGMLRISVG PSDLSNPARV NALLNGVEIM RILSPVSSEV VSGKRNVVWI VVGSVLGGFV
FLSLFFLSVL CLCRRKNNKT RSSESTGWTP LRRFRGSSNS RTTERTVSSS GYHTLRISFA
ELQSGTNNFD RSLVIGVGGF GMVFRGSLKD NTKVAVKRGS PGSRQGLPEF LSEITILSKI
RHRHLVSLVG YCEEQSEMIL VYEYMDKGPL KSHLYGSTNP PLSWKQRLEV CIGAARGLHY
LHTGSSQGII HRDIKSTNIL LDNNYVAKVA DFGLSRSGPC IDETHVSTGV KGSFGYLDPE
YFRRQQLTDK SDVYSFGVVL FEVLCARPAV DPLLVREQVN LAEWAIEWQR KGMLDQIVDP
NIADEIKPCS LKKFAETAEK CCADYGVDRP TIGDVLWNLE HVLQLQESGP LNIPEEDYGD
VTDPRTARQG LSNGSNIERD YGDGTSGIIS STQVFSQLMT NAGR
