ID A0A3B6FN69_WHEAT Unreviewed; 811 AA.
AC A0A3B6FN69;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
GN ORFNames=CFC21_041688 {ECO:0000313|EMBL:KAF7030073.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS3B02G273000.1.cds1};
RN [1] {ECO:0000313|EMBL:KAF7030073.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7030073.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS3B02G273000.1.cds1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS3B02G273000.1.cds1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS3B02G273000.1.cds1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7030073.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7030073.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) 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 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; CM022218; KAF7030073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6FN69; -.
DR SMR; A0A3B6FN69; -.
DR STRING; 4565.A0A3B6FN69; -.
DR PaxDb; 4565-Traes_3B_64DFEB19C-1; -.
DR EnsemblPlants; TraesCS3B02G273000.1; TraesCS3B02G273000.1.cds1; TraesCS3B02G273000.
DR Gramene; TraesCAD_scaffold_002336_01G000100.1; TraesCAD_scaffold_002336_01G000100.1; TraesCAD_scaffold_002336_01G000100.
DR Gramene; TraesCLE_scaffold_003060_01G000100.1; TraesCLE_scaffold_003060_01G000100.1; TraesCLE_scaffold_003060_01G000100.
DR Gramene; TraesCS3B02G273000.1; TraesCS3B02G273000.1.cds1; TraesCS3B02G273000.
DR Gramene; TraesCS3B03G0705600.1; TraesCS3B03G0705600.1.CDS1; TraesCS3B03G0705600.
DR Gramene; TraesKAR3B01G0299150.1; cds.TraesKAR3B01G0299150.1; TraesKAR3B01G0299150.
DR Gramene; TraesPAR_scaffold_000032_01G000400.1; TraesPAR_scaffold_000032_01G000400.1; TraesPAR_scaffold_000032_01G000400.
DR Gramene; TraesROB_scaffold_001829_01G000100.1; TraesROB_scaffold_001829_01G000100.1; TraesROB_scaffold_001829_01G000100.
DR OMA; CGFYPIG; -.
DR OrthoDB; 463273at2759; -.
DR Proteomes; UP000019116; Chromosome 3B.
DR Proteomes; UP000815260; Chromosome 3B.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR CDD; cd00028; B_lectin; 1.
DR CDD; cd00053; EGF; 1.
DR CDD; cd01098; PAN_AP_plant; 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; IPR000742; EGF-like_dom.
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; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR47974; OS07G0415500 PROTEIN; 1.
DR PANTHER; PTHR47974:SF7; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00954; S_locus_glycop; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR SUPFAM; SSF57414; Hairpin loop containing domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000641}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000641};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..811
FT /note="Receptor-like serine/threonine-protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040070436"
FT TRANSMEM 450..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..150
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 277..315
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 329..411
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 508..810
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 811 AA; 91310 MW; 4A5D99FCD4B813B7 CRC64;
MPRLFFYPVA LLLPLLSTLL CSCASPWQRS TGTSLQVDRE KVLLVSPDTT FSCGFYPSGN
GTNAFYFSIW FTHATDKTVV WTANPRFPVN AQGSRISLNR EGNLVLTDFN DSTAWESKTG
WGKHTTVALL DTGNLVINDS AGKTVWQSFD LPTNTLLPTQ HLTRANKLVS QSDSYHVLYF
DNDNVLRLLY NGPDITSIYW PSPDYNALQN GRTRFNSSKL AVLDREGKFL SSDGFKMIAS
DSGLGIQRRI TIDYDGNFRM YSLNASSGNW SITGQGVQQM CYVHGLCGKN GICEYSPAGR
PRCTCPPGYK MVDPENWDRG CKPTFSIQCG QPQEDFQFVK VPHGDFYGFD LTSNKSISLE
ECRRICLESC MCISFTYKAG EGLCYTKNVL YNGQVYPYFL GDNYFKLPKS VSSTSPAANH
PGITCSPERS KVMVVSADAY IKNSDHISWA YLYIFAAILG AVELFFIMTG WYVLFKMHNI
PKSMEEGYKM ITSQFRRFTY RELVEATGKF KEELGKGGNG VVYRGILGDK KVVAVKKLTD
VRKGEEEFWA EVTLIGRINH MNLVRMYGFC SEGQHRLLVY EFVENESLDR YLFDGRGTER
LLSWGQRFKI ALGTARGLAY LHHECLEWIV HCDVKPENIL LTREFEAKIA DFGLSKLSQR
DSSSLNFTQM RGTTGYMAPE WVMNLPIDAK VDVYSFGVVL LEIVTGSRVS SGVTAYEDEM
GLMQIPSGAT EGGEEMGFMQ FVQAVKQMLA NGADLDIVDA RLKGHFNHKQ ATVMVKIAIS
CLDERSKRPT MEQIARNLME CDDEDYHPAY F
//
