ID Y1661_ARATH Reviewed; 842 AA.
AC Q9SY89;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 158.
DE RecName: Full=Putative G-type lectin S-receptor-like serine/threonine-protein kinase At1g61610;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g61610; ORFNames=T25B24.4;
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).
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: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC005850; AAD25549.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33862.1; -; Genomic_DNA.
DR PIR; E96641; E96641.
DR RefSeq; NP_176355.1; NM_104843.2.
DR AlphaFoldDB; Q9SY89; -.
DR SMR; Q9SY89; -.
DR BioGRID; 27680; 21.
DR IntAct; Q9SY89; 21.
DR STRING; 3702.Q9SY89; -.
DR iPTMnet; Q9SY89; -.
DR PaxDb; 3702-AT1G61610-1; -.
DR ProteomicsDB; 243184; -.
DR EnsemblPlants; AT1G61610.1; AT1G61610.1; AT1G61610.
DR GeneID; 842457; -.
DR Gramene; AT1G61610.1; AT1G61610.1; AT1G61610.
DR KEGG; ath:AT1G61610; -.
DR Araport; AT1G61610; -.
DR TAIR; AT1G61610; -.
DR eggNOG; ENOG502QSUU; Eukaryota.
DR HOGENOM; CLU_000288_116_7_1; -.
DR InParanoid; Q9SY89; -.
DR OMA; WRKRWEI; -.
DR OrthoDB; 2101463at2759; -.
DR PhylomeDB; Q9SY89; -.
DR PRO; PR:Q9SY89; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SY89; baseline and differential.
DR Genevisible; Q9SY89; AT.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate 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; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:UniProt.
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; 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; 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:SF248; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 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; PS50026; EGF_3; 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; Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein;
KW Kinase; Lectin; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..842
FT /note="Putative G-type lectin S-receptor-like
FT serine/threonine-protein kinase At1g61610"
FT /id="PRO_0000401324"
FT TOPO_DOM 23..443
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..842
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..150
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 292..331
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 350..431
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 525..814
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 614..631
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 650
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 531..539
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 553
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 684
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 837
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 296..308
FT /evidence="ECO:0000250"
FT DISULFID 302..319
FT /evidence="ECO:0000250"
FT DISULFID 385..406
FT /evidence="ECO:0000250"
FT DISULFID 389..395
FT /evidence="ECO:0000250"
SQ SEQUENCE 842 AA; 95382 MW; 62FB352040117111 CRC64;
MAGFNRNLTL VTTLLIFHQL CSNVSCSTSN SFTRNHTIRE GDSLISEDES FELGFFTPKN
STLRYVGIWY KNIEPQTVVW VANREKPLLD HKGALKIADD GNLVIVNGQN ETIWSTNVEP
ESNNTVAVLF KTGDLVLCSD SDRRKWYWES FNNPTDTFLP GMRVRVNPSL GENRAFIPWK
SESDPSPGKY SMGIDPVGAL EIVIWEGEKR KWRSGPWNSA IFTGIPDMLR FTNYIYGFKL
SSPPDRDGSV YFTYVASDSS DFLRFWIRPD GVEEQFRWNK DIRNWNLLQW KPSTECEKYN
RCGNYSVCDD SKEFDSGKCS CIDGFEPVHQ DQWNNRDFSG GCQRRVPLNC NQSLVAGQED
GFTVLKGIKV PDFGSVVLHN NSETCKDVCA RDCSCKAYAL VVGIGCMIWT RDLIDMEHFE
RGGNSINIRL AGSKLGGGKE NSTLWIIVFS VIGAFLLGLC IWILWKFKKS LKAFLWKKKD
ITVSDIIENR DYSSSPIKVL VGDQVDTPDL PIFSFDSVAS ATGDFAEENK LGQGGFGTVY
KGNFSEGREI AVKRLSGKSK QGLEEFKNEI LLIAKLQHRN LVRLLGCCIE DNEKMLLYEY
MPNKSLDRFL FDESKQGSLD WRKRWEVIGG IARGLLYLHR DSRLKIIHRD LKASNILLDT
EMNPKISDFG MARIFNYRQD HANTIRVVGT YGYMAPEYAM EGIFSEKSDV YSFGVLILEI
VSGRKNVSFR GTDHGSLIGY AWHLWSQGKT KEMIDPIVKD TRDVTEAMRC IHVGMLCTQD
SVIHRPNMGS VLLMLESQTS QLPPPRQPTF HSFLNSGDIE LNFDGHDVAS VNDVTFTTIV
GR
//
