ID M1CJP1_SOLTU Unreviewed; 759 AA.
AC M1CJP1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
GN Name=102596659 {ECO:0000313|EnsemblPlants:PGSC0003DMT400068929};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400068929, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400068929}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400068929};
RG EnsemblPlants;
RL Submitted (JUN-2015) 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|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|PIRNR:PIRNR000641};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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DR RefSeq; XP_006349562.1; XM_006349500.2.
DR RefSeq; XP_006349564.1; XM_006349502.2.
DR AlphaFoldDB; M1CJP1; -.
DR PaxDb; 4113-PGSC0003DMT400068929; -.
DR EnsemblPlants; PGSC0003DMT400068928; PGSC0003DMT400068928; PGSC0003DMG400026810.
DR EnsemblPlants; PGSC0003DMT400068929; PGSC0003DMT400068929; PGSC0003DMG400026810.
DR GeneID; 102596659; -.
DR Gramene; PGSC0003DMT400068928; PGSC0003DMT400068928; PGSC0003DMG400026810.
DR Gramene; PGSC0003DMT400068929; PGSC0003DMT400068929; PGSC0003DMG400026810.
DR KEGG; sot:102596659; -.
DR eggNOG; ENOG502QW3Z; Eukaryota.
DR HOGENOM; CLU_000288_116_2_1; -.
DR InParanoid; M1CJP1; -.
DR OMA; QKICVAC; -.
DR OrthoDB; 1210474at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1CJP1; baseline.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0048544; P:recognition of pollen; IEA:InterPro.
DR CDD; cd00028; B_lectin; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 2.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
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; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR47974:SF13; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE SD3-1; 1.
DR PANTHER; PTHR47974; OS07G0415500 PROTEIN; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00954; S_locus_glycop; 1.
DR PIRSF; PIRSF000641; SRK; 2.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00473; PAN_AP; 1.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50927; BULB_LECTIN; 2.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000641};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|PIRNR:PIRNR000641}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000641};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000641}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|PIRNR:PIRNR000641};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..153
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 156..274
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 326..406
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 482..759
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 733..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 759 AA; 84875 MW; 5847E53B6F679486 CRC64;
MDRGDRIIAC YSNLLLSVSI GFLLFSVVSS QIPLGSKLTV EENNYWFSSN KDYAIGFLNF
SDQYSFGVRF NAIYIPSSEQ AAIWTAGWNV KVSSKAYFEL SLTGEMILFD PAKGKIVWQS
KTGNTSVESA VLLDDGNFVL LNRNKSAVWQ SFESPSDTML SGQSLSVGQS LRASSRGSLT
SYYSLHMNVS GEMQLRWETS IIYWTVGGPK SAVRAILGSD GILQLLDQQS QAVWSVYGED
HNDSDVKFRF LRLDSDGNLR IYSWENNATS WRTVWQAIIN QCDVFATCAT NGICTLNASD
SYVCWCPFRS TRDSNSECLI PYKPSCESGS SMILHEHMYL YGIYPPNNTV VQTNLQQCRT
LCQKDPSCHA ASFINNGTPQ CHMMNSRYVG GQSDPSLGSV TFVKTCSDPI AVLPPPVPAP
RKVSQKICVA CLLEVAAASI VVFVMLQFSI GVYLFRRRKH MMQKSALPHI VPNATGCIVF
SYSEIKDLTD NFKQQIGQNV FKGLLPDNRL VAVKDLNASI DERRFRAAVL KIGSIYHKNL
LRLDGYCCES GRRLLVYELA KYGSVDKCLE EPRMCKRLTW RKRMDICLSV ARAISYLHTG
CREFISHGNL KCENVVLDDE LEAKVSEFGL RTIQAEASSS GGLAETDVRD FGKVMVVLIT
GCQNADEACY WSYEKWVKAE KEMAMDQRIV VGTDSEELER ALRIAFWCLQ GDERMRPSMG
EVIKVLEGTL TVDPPPPPFA HNQQWPPDDE SPSESYSAL
//
