Y1150_ARATH
ID Y1150_ARATH Reviewed; 804 AA.
AC Q9SYA0;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At1g61500;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g61500; ORFNames=T25B24.15;
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; AAD25558.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33845.1; -; Genomic_DNA.
DR PIR; B96640; B96640.
DR RefSeq; NP_564777.1; NM_104831.3.
DR AlphaFoldDB; Q9SYA0; -.
DR SMR; Q9SYA0; -.
DR STRING; 3702.AT1G61500.1; -.
DR PaxDb; Q9SYA0; -.
DR PRIDE; Q9SYA0; -.
DR EnsemblPlants; AT1G61500.1; AT1G61500.1; AT1G61500.
DR GeneID; 842444; -.
DR Gramene; AT1G61500.1; AT1G61500.1; AT1G61500.
DR KEGG; ath:AT1G61500; -.
DR Araport; AT1G61500; -.
DR TAIR; locus:2200888; AT1G61500.
DR eggNOG; ENOG502QT06; Eukaryota.
DR HOGENOM; CLU_000288_116_7_1; -.
DR InParanoid; Q9SYA0; -.
DR PhylomeDB; Q9SYA0; -.
DR PRO; PR:Q9SYA0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYA0; baseline and differential.
DR Genevisible; Q9SYA0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR CDD; cd00028; B_lectin; 1.
DR Gene3D; 2.90.10.10; -; 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 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; SSF51110; 1.
DR SUPFAM; SSF56112; SSF56112; 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 2: Evidence at transcript level;
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..804
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase At1g61500"
FT /id="PRO_0000401319"
FT TOPO_DOM 25..427
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..804
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..145
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 279..315
FT /note="EGF-like; atypical"
FT DOMAIN 334..416
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 491..776
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 580..597
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 616
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 497..505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 650
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 283..295
FT /evidence="ECO:0000250"
FT DISULFID 289..303
FT /evidence="ECO:0000250"
FT DISULFID 369..390
FT /evidence="ECO:0000250"
FT DISULFID 373..379
FT /evidence="ECO:0000250"
SQ SEQUENCE 804 AA; 90331 MW; D6ACE4309C185BB0 CRC64;
MMTRFACLHL FTMFLFTLLS GSSSAVITTE SPLSMGQTLS SANEVYELGF FSPNNTQDQY
VGIWFKDTIP RVVVWVANRE KPVTDSTAYL AISSSGSLLL LNGKHGTVWS SGVTFSSSGC
RAELSDSGNL KVIDNVSERA LWQSFDHLGD TLLHTSSLTY NLATAEKRVL TSWKSYTDPS
PGDFLGQITP QVPSQGFVMR GSTPYWRSGP WAKTRFTGIP FMDESYTGPF TLHQDVNGSG
YLTYFQRDYK LSRITLTSEG SIKMFRDNGM GWELYYEAPK KLCDFYGACG PFGLCVMSPS
PMCKCFRGFV PKSVEEWKRG NWTGGCVRHT ELDCLGNSTG EDADDFHQIA NIKPPDFYEF
ASSVNAEECH QRCVHNCSCL AFAYIKGIGC LVWNQDLMDA VQFSATGELL SIRLARSELD
GNKRKKTIVA SIVSLTLFMI LGFTAFGVWR CRVEHIAHIS KDAWKNDLKP QDVPGLDFFD
MHTIQNATNN FSLSNKLGQG GFGSVYKGKL QDGKEIAVKR LSSSSGQGKE EFMNEIVLIS
KLQHRNLVRV LGCCIEEEEK LLIYEFMVNK SLDTFLFDSR KRLEIDWPKR FDIIQGIARG
LLYLHHDSRL RVIHRDLKVS NILLDEKMNP KISDFGLARM YQGTEYQDNT RRVVGTLGYM
SPEYAWTGMF SEKSDIYSFG VLMLEIISGE KISRFSYGVE GKTLIAYAWE SWSEYRGIDL
LDQDLADSCH PLEVGRCIQI GLLCVQHQPA DRPNTLELLA MLTTTSDLPS PKQPTFAFHT
RDDESLSNDL ITVNGMTQSV ILGR
