Y1105_ARATH
ID Y1105_ARATH Reviewed; 625 AA.
AC O04086; Q56YN4; Q8LPJ9;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Probable receptor-like protein kinase At1g11050;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g11050; ORFNames=T19D16.6;
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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 389-625.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) 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: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94000.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U95973; AAB65477.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28677.1; -; Genomic_DNA.
DR EMBL; AY099669; AAM20520.1; -; mRNA.
DR EMBL; BT003413; AAO30076.1; -; mRNA.
DR EMBL; AK221287; BAD94000.1; ALT_INIT; mRNA.
DR PIR; D86244; D86244.
DR RefSeq; NP_172572.1; NM_100978.2.
DR AlphaFoldDB; O04086; -.
DR SMR; O04086; -.
DR BioGRID; 22886; 5.
DR IntAct; O04086; 5.
DR STRING; 3702.AT1G11050.1; -.
DR iPTMnet; O04086; -.
DR PaxDb; O04086; -.
DR PRIDE; O04086; -.
DR ProteomicsDB; 242497; -.
DR EnsemblPlants; AT1G11050.1; AT1G11050.1; AT1G11050.
DR GeneID; 837646; -.
DR Gramene; AT1G11050.1; AT1G11050.1; AT1G11050.
DR KEGG; ath:AT1G11050; -.
DR Araport; AT1G11050; -.
DR TAIR; locus:2197414; AT1G11050.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_0_0_1; -.
DR InParanoid; O04086; -.
DR OMA; KLETFQF; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O04086; -.
DR PRO; PR:O04086; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04086; differential.
DR Genevisible; O04086; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; 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 InterPro; IPR043891; SPARK.
DR InterPro; IPR045271; SRF-like.
DR PANTHER; PTHR27001; PTHR27001; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF19160; SPARK; 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; Glycoprotein; Kinase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..625
FT /note="Probable receptor-like protein kinase At1g11050"
FT /id="PRO_0000389468"
FT TOPO_DOM 21..227
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 295..555
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 426
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 301..309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 424
FT /note="H -> R (in Ref. 4; BAD94000)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="A -> V (in Ref. 3; AAM20520/AAO30076)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 68521 MW; AD64DEDDF79A0665 CRC64;
MPNSILFLLL SFLYLTNCVA QSPSQTCPLD FSHVLTIPWN TTDCQKSDKS ADSKNSCCQS
LLTLIGIPLA HRLKQTSNFR LPNLATSISC LNNLQTKLSS LSLSSNLTSL CFDPNQFVIN
NETCAGIQTT QDWVSRLGPS TALDSACSSG LTDLTRCDAC VAAGFRVQKQ LITLDGNSSH
GVYCYHFVVT YAAGIVNKKG PESDDALSCL FSLSLRSPLN SKKKRHTVAL ALGITGAIFG
ALVIAGLICL YFRFGKAVKG GEVGWEDQGS RPKWRPNTGS IWFKIEELEK ATNNFSQKNF
IGRGGFGFVY KGVLPDGSVI AVKKVIESEF QGDAEFRNEV EIISNLKHRN LVPLRGCSMV
DDDSESQRYL VYDYMSNGNL DDHLFPRGET TKMPLSWPQR KSIILDVAKG LAYLHYGVKP
AIYHRDIKGT NILLDVDMRA RVADFGLAKQ SREGESHLTT RVAGTHGYLA PEYALYGQLT
EKSDVYSFGV VILEIMCGRK ALDLSTSGSP NTFLITDWAW SLVKAGKTEE ALEQSLLREE
GSGLSNPKGI MERFLQVGIL CAHVLVALRP TILDALKMLE GDIEVPPIPD RPVPLAHPSY
RMDGNGFTIS PALSGLQIHS GDMLR
