Y5185_ARATH
ID Y5185_ARATH Reviewed; 484 AA.
AC Q8LEB6;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable receptor-like protein kinase At5g18500;
DE EC=2.7.11.1;
GN OrderedLocusNames=At5g18500; ORFNames=T28N17.1;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF Clone.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 membrane
CC protein {ECO:0000250}.
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; AC051626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92571.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92572.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71166.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71167.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71168.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71169.1; -; Genomic_DNA.
DR EMBL; BT029165; ABJ17100.1; -; mRNA.
DR EMBL; AY085517; AAM62741.1; -; mRNA.
DR RefSeq; NP_001031898.1; NM_001036821.3.
DR RefSeq; NP_001332714.1; NM_001343548.1.
DR RefSeq; NP_001332715.1; NM_001343549.1.
DR RefSeq; NP_001332716.1; NM_001343550.1.
DR RefSeq; NP_001332717.1; NM_001343547.1.
DR RefSeq; NP_197351.1; NM_121855.3.
DR AlphaFoldDB; Q8LEB6; -.
DR SMR; Q8LEB6; -.
DR STRING; 3702.AT5G18500.2; -.
DR iPTMnet; Q8LEB6; -.
DR PaxDb; Q8LEB6; -.
DR PRIDE; Q8LEB6; -.
DR ProteomicsDB; 243134; -.
DR EnsemblPlants; AT5G18500.1; AT5G18500.1; AT5G18500.
DR EnsemblPlants; AT5G18500.2; AT5G18500.2; AT5G18500.
DR EnsemblPlants; AT5G18500.3; AT5G18500.3; AT5G18500.
DR EnsemblPlants; AT5G18500.4; AT5G18500.4; AT5G18500.
DR EnsemblPlants; AT5G18500.5; AT5G18500.5; AT5G18500.
DR EnsemblPlants; AT5G18500.6; AT5G18500.6; AT5G18500.
DR GeneID; 831968; -.
DR Gramene; AT5G18500.1; AT5G18500.1; AT5G18500.
DR Gramene; AT5G18500.2; AT5G18500.2; AT5G18500.
DR Gramene; AT5G18500.3; AT5G18500.3; AT5G18500.
DR Gramene; AT5G18500.4; AT5G18500.4; AT5G18500.
DR Gramene; AT5G18500.5; AT5G18500.5; AT5G18500.
DR Gramene; AT5G18500.6; AT5G18500.6; AT5G18500.
DR KEGG; ath:AT5G18500; -.
DR Araport; AT5G18500; -.
DR TAIR; locus:2146203; AT5G18500.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_4_1_1; -.
DR InParanoid; Q8LEB6; -.
DR OMA; DQFSAND; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q8LEB6; -.
DR PRO; PR:Q8LEB6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LEB6; baseline and differential.
DR Genevisible; Q8LEB6; 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: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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..484
FT /note="Probable receptor-like protein kinase At5g18500"
FT /id="PRO_0000401339"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 166..445
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 72..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 292
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 172..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 155
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 239
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 331
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 339
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
SQ SEQUENCE 484 AA; 54213 MW; FEEFD03196439389 CRC64;
MGSGLNDTLS RNYNGLELWE IIVIVLSAIF VVVLAISLWL TFRRKTSRSS SNLIPVSRQI
PPSVPEEIKE IRVDEVSSSN GGNGYPSISE KFGDKEPEKG IKAESENGDS SRSGSFNHLE
KKDGSSVSSA NPLTAPSPLS GLPEFSHLGW GHWFTLRDLQ MATNQFSRDN IIGDGGYGVV
YRGNLVNGTP VAVKKLLNNL GQADKDFRVE VEAIGHVRHK NLVRLLGYCM EGTQRMLVYE
YVNNGNLEQW LRGDNQNHEY LTWEARVKIL IGTAKALAYL HEAIEPKVVH RDIKSSNILI
DDKFNSKISD FGLAKLLGAD KSFITTRVMG TFGYVAPEYA NSGLLNEKSD VYSFGVVLLE
AITGRYPVDY ARPPPEVHLV EWLKMMVQQR RSEEVVDPNL ETKPSTSALK RTLLTALRCV
DPMSEKRPRM SQVARMLESE EYPIAREDRR RRRSQNGTTR DSDPPRNSTD TDKSEYHDLK
PEGG
