Y1154_ARATH
ID Y1154_ARATH Reviewed; 472 AA.
AC Q3EDL4; O23699; Q94KD9; Q9LMM7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable serine/threonine-protein kinase At1g01540;
DE EC=2.7.11.1;
GN OrderedLocusNames=At1g01540; ORFNames=F22L4.8;
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].
RX PubMed=9666060; DOI=10.1016/s0378-1119(98)00286-8;
RA Terryn N., Gielen J., De Keyser A., Van Den Daele H., Ardiles W., Neyt P.,
RA De Clercq R., Coppieters J., Dehais P., Villarroel R., Rouze P.,
RA van Montagu M.;
RT "Sequence analysis of a 40-kb Arabidopsis thaliana genomic region located
RT at the top of chromosome 1.";
RL Gene 215:11-17(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-67, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q3EDL4-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK56254.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM16225.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y12776; CAA73303.1; -; Genomic_DNA.
DR EMBL; AC061957; AAF81312.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27302.1; -; Genomic_DNA.
DR EMBL; AF332429; AAG48792.1; -; mRNA.
DR EMBL; AF367265; AAK56254.1; ALT_SEQ; mRNA.
DR EMBL; AY093964; AAM16225.1; ALT_SEQ; mRNA.
DR PIR; A86146; A86146.
DR RefSeq; NP_171661.1; NM_100036.5. [Q3EDL4-1]
DR AlphaFoldDB; Q3EDL4; -.
DR SMR; Q3EDL4; -.
DR BioGRID; 24768; 1.
DR STRING; 3702.AT1G01540.2; -.
DR iPTMnet; Q3EDL4; -.
DR PaxDb; Q3EDL4; -.
DR PRIDE; Q3EDL4; -.
DR ProteomicsDB; 242500; -. [Q3EDL4-1]
DR EnsemblPlants; AT1G01540.2; AT1G01540.2; AT1G01540. [Q3EDL4-1]
DR GeneID; 839533; -.
DR Gramene; AT1G01540.2; AT1G01540.2; AT1G01540. [Q3EDL4-1]
DR KEGG; ath:AT1G01540; -.
DR Araport; AT1G01540; -.
DR TAIR; locus:2025396; AT1G01540.
DR eggNOG; KOG1187; Eukaryota.
DR InParanoid; Q3EDL4; -.
DR OMA; PITWDIR; -.
DR PhylomeDB; Q3EDL4; -.
DR PRO; PR:Q3EDL4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q3EDL4; baseline and differential.
DR Genevisible; Q3EDL4; 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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; HDA:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..472
FT /note="Probable serine/threonine-protein kinase At1g01540"
FT /id="PRO_0000302048"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 154..431
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 437..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 160..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 67
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 143
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 227
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 314
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 319
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 327
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
SQ SEQUENCE 472 AA; 52325 MW; FA5E5AED90C5862D CRC64;
MSVYDAAFLN TELSKPTSIF GLRLWVVIGI LLGSLIVIAL FLLSLCLTSR RKNRKPRADF
ASAAIATPPI SKEIKEIVPA QNQSVPAEIQ VDIGKIEHRV VFSDRVSSGE SRGTASASET
ASYSGSGNCG PEVSHLGWGR WYTLRELEAA TNGLCEENVI GEGGYGIVYR GILTDGTKVA
VKNLLNNRGQ AEKEFKVEVE VIGRVRHKNL VRLLGYCVEG AYRMLVYDFV DNGNLEQWIH
GDVGDVSPLT WDIRMNIILG MAKGLAYLHE GLEPKVVHRD IKSSNILLDR QWNAKVSDFG
LAKLLGSESS YVTTRVMGTF GYVAPEYACT GMLNEKSDIY SFGILIMEII TGRNPVDYSR
PQGETNLVDW LKSMVGNRRS EEVVDPKIPE PPSSKALKRV LLVALRCVDP DANKRPKMGH
IIHMLEAEDL LYRDERRTTR DHGSRERQET AVVAAGSESG ESGSRHHQQK QR
