ID M0Y2Q7_HORVV Unreviewed; 796 AA.
AC M0Y2Q7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
OS Hordeum vulgare subsp. vulgare (Domesticated barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=112509 {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.2HG0214510.1.CDS1, ECO:0000313|Proteomes:UP000011116};
RN [1] {ECO:0000313|Proteomes:UP000011116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Morex {ECO:0000313|Proteomes:UP000011116};
RX PubMed=23075845; DOI=10.1038/nature11543;
RG The International Barley Genome Sequencing Consortium;
RA Mayer K.F., Waugh R., Brown J.W., Schulman A., Langridge P., Platzer M.,
RA Fincher G.B., Muehlbauer G.J., Sato K., Close T.J., Wise R.P., Stein N.;
RT "A physical, genetic and functional sequence assembly of the barley
RT genome.";
RL Nature 491:711-716(2012).
RN [2] {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.2HG0214510.1.CDS1}
RP IDENTIFICATION.
RC STRAIN=subsp. vulgare
RC {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.2HG0214510.1.CDS1};
RG EnsemblPlants;
RL Submitted (JAN-2022) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001433,
CC ECO:0000256|PIRNR:PIRNR000641};
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; Evidence={ECO:0000256|ARBA:ARBA00000775,
CC ECO:0000256|PIRNR:PIRNR000641};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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DR AlphaFoldDB; M0Y2Q7; -.
DR STRING; 112509.M0Y2Q7; -.
DR PaxDb; 4513-MLOC_65195-1; -.
DR EnsemblPlants; HORVU.MOREX.r3.2HG0214510.1; HORVU.MOREX.r3.2HG0214510.1.CDS1; HORVU.MOREX.r3.2HG0214510.
DR Gramene; HORVU.MOREX.r2.2HG0178320.1; HORVU.MOREX.r2.2HG0178320.1.CDS.1; HORVU.MOREX.r2.2HG0178320.
DR Gramene; HORVU.MOREX.r3.2HG0214510.1; HORVU.MOREX.r3.2HG0214510.1.CDS1; HORVU.MOREX.r3.2HG0214510.
DR InParanoid; M0Y2Q7; -.
DR OMA; SHMEEVM; -.
DR OrthoDB; 344059at2759; -.
DR Proteomes; UP000011116; Chromosome 2H.
DR ExpressionAtlas; M0Y2Q7; baseline.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR CDD; cd00028; B_lectin; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR47976; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD2-5; 1.
DR PANTHER; PTHR47976:SF42; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000641};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000641}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000011116};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000641}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT BINDING 512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 796 AA; 88039 MW; 422E638988F330BC CRC64;
MIMQNLNMLG SIILLLVFPI LLLPTVVAYP STTSHSNLWN ISSMQSRVAM ARNSSALVIL
ESGSASYQLY FGFYSKDGHA FTLSVLLIGP QDPVIWSANP DDHVSQNAVL NFTDNGNMLL
SDGDGTVIWS TATKNKSVAG FRLDVSGNLV LFDQSNSPVW QSFHHPTDTL VLGQSLCRGM
NISVKPSNTK WPSARIYLSA EFEGLRYSYQ PASYSQLFTE VASTTSNCYV FVNGSFGFPN
QVFSLPLARS LQFMRLESDG HLRLYKMQGY SSPQLLSDVL STTMKFCDYP FACGDYGVCS
GGQCSCPSLS YFRSNNERHP EAGCTLLTSI SCNRAHNHQL LPLDNVSYFS DNMFRSSAAS
SPSEEVCKQA CLMDCACRVA IFQYSGVSKY SNGGYCLLLS EQKLISLAEG SSDGLSAYIK
IQGTRSIKKR ITTIVCSVIA GLSALGILFS AIIWKMCKKE EEELFDSIPG TPKRFSFREL
KVATGNFSVK LGSGGFGSVF KGKIGRETIA VKRLESVEQG TEEFLAEVMT IGRMHHHNLV
RLIGFCAEKS HRLLVYEYLC NSSLDKWIFH ACSVFTLSWK TRRNIIIAIA RGLSYLHEEC
KEKIAHLDIK PQNILLDDRF NAKLSDFGLS KMINRDQSKI MTRMRGTRGY LAPEWLGSKI
TEKADIYSFG IVVMEIICGR ENLDESLPEE SIHLISLLEE KARSGHLVDL VDSGSNDMQF
HMEEVMEAMR LAMWCLQVDS SRRPLMSTVA KVLEGVTSLE AAPDYSFVPS FASNGAGVAG
PTSSYVPSES HLSGPR
//
