ID A0A2K1YF58_POPTR Unreviewed; 811 AA.
AC A0A2K1YF58;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=POPTR_011G036400 {ECO:0000313|EMBL:PNT11661.1};
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694 {ECO:0000313|EMBL:PNT11661.1, ECO:0000313|Proteomes:UP000006729};
RN [1] {ECO:0000313|EMBL:PNT11661.1, ECO:0000313|Proteomes:UP000006729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729}, and
RC Nisqually-1 {ECO:0000313|EMBL:PNT11661.1};
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
RN [2] {ECO:0000313|EMBL:PNT11661.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nisqually-1 {ECO:0000313|EMBL:PNT11661.1};
RA Tuskan G., Difazio S., Jansson S., Bohlmann J., Grigoriev I., Hellsten U.,
RA Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., Sterck L.,
RA Aerts A., Bhalerao R., Bhalerao R., Blaudez D., Boerjan W., Brun A.,
RA Brunner A., Busov V., Campbell M., Carlson J., Chalot M., Chapman J.,
RA Chen G., Cooper D., Coutinho P., Couturier J., Covert S., Cronk Q.,
RA Cunningham R., Davis J., Degroeve S., Dejardin A., Depamphilis C.,
RA Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J., Ellis B.,
RA Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L.,
RA Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D., Holt R.,
RA Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M., Jorgensen R.,
RA Joshi C., Kangasjarvi J., Karlsson J., Kelleher C., Kirkpatrick R.,
RA Kirst M., Kohler A., Kalluri U., Larimer F., Leebens-Mack J., Leple J.,
RA Locascio P., Lou Y., Lucas S., Martin F., Montanini B., Napoli C.,
RA Nelson D., Nelson C., Nieminen K., Nilsson O., Pereda V., Peter G.,
RA Philippe R., Pilate G., Poliakov A., Razumovskaya J., Richardson P.,
RA Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J., Schrader J.,
RA Segerman B., Shin H., Siddiqui A., Sterky F., Terry A., Tsai C.,
RA Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S., Yang G.,
RA Yin T., Douglas C., Marra M., Sandberg G., Van De Peer Y., Rokhsar D.;
RT "WGS assembly of Populus trichocarpa.";
RL Submitted (JUL-2017) 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|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: 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 EMBL; CM009300; PNT11661.1; -; Genomic_DNA.
DR EMBL; CM009300; RQO97439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1YF58; -.
DR STRING; 3694.A0A2K1YF58; -.
DR EnsemblPlants; Potri.011G036400.4.v4.1; Potri.011G036400.4.v4.1; Potri.011G036400.v4.1.
DR Gramene; Potri.011G036400.4.v4.1; Potri.011G036400.4.v4.1; Potri.011G036400.v4.1.
DR InParanoid; A0A2K1YF58; -.
DR OrthoDB; 520203at2759; -.
DR Proteomes; UP000006729; Chromosome 11.
DR ExpressionAtlas; A0A2K1YF58; differential.
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 CDD; cd00028; B_lectin; 1.
DR CDD; cd01098; PAN_AP_plant; 1.
DR CDD; cd14066; STKc_IRAK; 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; IPR021820; S-locus_recpt_kinase_C.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR32444:SF130; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF11883; DUF3403; 1.
DR Pfam; PF08276; PAN_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000641};
KW Reference proteome {ECO:0000313|Proteomes:UP000006729};
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|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..811
FT /note="Receptor-like serine/threonine-protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033311365"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..147
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 335..417
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 493..778
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 811 AA; 91882 MW; DBB3DD35E11E7826 CRC64;
MEAEKLFLPF SLLMLHFSSC TSLDSLKTNQ TIKEGDVLIS KGNNFALGFF SPGSSSNRYL
GIWYHKVPEQ TVVWVANRND PIIGSSGFLF VDQYGNLVLY GNDDQKLPVW STNVSVEEND
TCAAQLLDSG NLILVRKRSR KTVWQSFDYP TNILLPGMKL GLDRKLGIDR FLTSWRSADD
PGIGDFSLMI NPNGSPQIIV YNGTEPISRS PPWPWRSQMG LYESTFVNDP DEIYWVYTVP
DDSYLLRIIV DHSGLLKVLT WRESDGQWKD YWKAPVFQCD YYGLCGAYST CELANLNEFG
CACLPGFEPK YPLEWSARDG SGGCVRKRLQ TSSFCQHGEG FVKVENVVLP ESSAAAWVDM
SKSRAACEVE CKRNCSCSAY AIIGIPGKNY GCLNWYKELV DIRYDRSNSY DLYVRVDAYE
LDDTKRKSND SREKTMQAVL APSIALSWFL ISLFAYLWFK KRAKKGSELQ VNSTSTELEY
FKLSTVTAAT NNFSPANKLG QGGFGSVYKG LLANGKEVAI KRLSRSSGQG TEEFKNEVMV
IAMLQHRNLV KLLGYCTQDG EQMLIYEYLP NKSLDSFLFD ESRRLLLDWR KRFDIIVGIA
RGILYLHQDS RLRIIHRDLK CSNILLDADM NPKISDFGMA KIFEGNRTED RTRRVVGTYG
YMPPEYVVFG NFSAKSDVFS FGVMLLEIAS GKKNNRFYQQ NPPLTLIGYV WELWREDKAL
EIVDPSLTEL YDPRDALKCI QIGLLCVQED ATDRPSMLAV VFMLSNETEI PSPKQPAFLF
RKSDNNPDIA LDVEDGQCSL NEVTITEIAC R
//
