Y5720_ARATH
ID Y5720_ARATH Reviewed; 669 AA.
AC Q93Y06; Q9FH93;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable inactive receptor kinase At5g67200;
DE Flags: Precursor;
GN OrderedLocusNames=At5g67200; ORFNames=K21H1.16;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND IDENTIFICATION BY
RP 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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10954.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB020742; BAB10954.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED98313.1; -; Genomic_DNA.
DR EMBL; AY059897; AAL24379.1; -; mRNA.
DR EMBL; BT003370; AAO30018.1; -; mRNA.
DR RefSeq; NP_569046.1; NM_126120.3.
DR AlphaFoldDB; Q93Y06; -.
DR SMR; Q93Y06; -.
DR STRING; 3702.AT5G67200.1; -.
DR iPTMnet; Q93Y06; -.
DR PaxDb; Q93Y06; -.
DR PRIDE; Q93Y06; -.
DR ProteomicsDB; 242839; -.
DR EnsemblPlants; AT5G67200.1; AT5G67200.1; AT5G67200.
DR GeneID; 836855; -.
DR Gramene; AT5G67200.1; AT5G67200.1; AT5G67200.
DR KEGG; ath:AT5G67200; -.
DR Araport; AT5G67200; -.
DR TAIR; locus:2155508; AT5G67200.
DR eggNOG; ENOG502QR4S; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; Q93Y06; -.
DR OMA; IINRACA; -.
DR OrthoDB; 498625at2759; -.
DR PhylomeDB; Q93Y06; -.
DR PRO; PR:Q93Y06; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93Y06; baseline and differential.
DR Genevisible; Q93Y06; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..669
FT /note="Probable inactive receptor kinase At5g67200"
FT /id="PRO_0000315403"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 98..120
FT /note="LRR 1"
FT REPEAT 121..142
FT /note="LRR 2"
FT REPEAT 145..167
FT /note="LRR 3"
FT REPEAT 169..191
FT /note="LRR 4"
FT REPEAT 192..212
FT /note="LRR 5"
FT DOMAIN 393..669
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 318..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 399..407
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 421
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 669 AA; 74006 MW; F6CD668713DC1811 CRC64;
MTLNFFLPFF FFFILLRVSA GAEPNYFNSL LPSDAVALLS FKSTADLDNK LLYSLTERYD
YCQWRGVKCA QGRIVRLVLS GVGLRGYFSS ATLSRLDQLR VLSLENNSLF GPIPDLSHLV
NLKSLFLSRN QFSGAFPPSI LSLHRLMILS ISHNNFSGSI PSEINALDRL TSLNLDFNRF
NGTLPSLNQS FLTSFNVSGN NLTGVIPVTP TLSRFDASSF RSNPGLCGEI INRACASRSP
FFGSTNKTTS SEAPLGQSAQ AQNGGAVVIP PVVTKKKGKE SGLVLGFTAG LASLIVLGLC
LVVFSLVIKK RNDDGIYEPN PKGEASLSQQ QQSQNQTPRT RAVPVLNSDT ESQKREKEVQ
FQETEQRIPN SGNLVFCGES RSQGMYTMEQ LMRASAELLG RGSVGITYKA VLDNQLIVTV
KRLDAAKTAV TSEEAFENHM EIVGGLRHTN LVPIRSYFQS NGERLIIYDY HPNGSLFNLI
HGSRSSRAKP LHWTSCLKIA EDVAQGLYYI HQTSSALVHG NLKSTNILLG QDFEACLTDY
CLSVLTDSSS ASPDDPDSSS YKAPEIRKSS RRPTSKCDVY SFGVLIFELL TGKNASRHPF
MAPHDMLDWV RAMREEEEGT EDNRLGMMTE TACLCRVTSP EQRPTMRQVI KMIQEIKESV
MAEENDPFR
