Y1649_ARATH
ID Y1649_ARATH Reviewed; 804 AA.
AC O64770;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At1g61490;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g61490; ORFNames=T1F9.1;
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; AC004255; AAC13891.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33844.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60681.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60682.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60685.1; -; Genomic_DNA.
DR RefSeq; NP_001322951.1; NM_001333978.1.
DR RefSeq; NP_001322952.1; NM_001333975.1.
DR RefSeq; NP_001322955.1; NM_001333977.1.
DR RefSeq; NP_176344.1; NM_104830.2.
DR AlphaFoldDB; O64770; -.
DR SMR; O64770; -.
DR BioGRID; 27666; 1.
DR IntAct; O64770; 1.
DR STRING; 3702.AT1G61490.1; -.
DR PaxDb; O64770; -.
DR PRIDE; O64770; -.
DR EnsemblPlants; AT1G61490.1; AT1G61490.1; AT1G61490.
DR EnsemblPlants; AT1G61490.2; AT1G61490.2; AT1G61490.
DR EnsemblPlants; AT1G61490.4; AT1G61490.4; AT1G61490.
DR EnsemblPlants; AT1G61490.5; AT1G61490.5; AT1G61490.
DR GeneID; 842443; -.
DR Gramene; AT1G61490.1; AT1G61490.1; AT1G61490.
DR Gramene; AT1G61490.2; AT1G61490.2; AT1G61490.
DR Gramene; AT1G61490.4; AT1G61490.4; AT1G61490.
DR Gramene; AT1G61490.5; AT1G61490.5; AT1G61490.
DR KEGG; ath:AT1G61490; -.
DR Araport; AT1G61490; -.
DR TAIR; locus:2197664; AT1G61490.
DR eggNOG; ENOG502QSUU; Eukaryota.
DR HOGENOM; CLU_000288_116_1_1; -.
DR InParanoid; O64770; -.
DR OMA; EDSWRKG; -.
DR OrthoDB; 407794at2759; -.
DR PhylomeDB; O64770; -.
DR PRO; PR:O64770; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O64770; baseline and differential.
DR Genevisible; O64770; 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 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..804
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase At1g61490"
FT /id="PRO_0000401323"
FT TOPO_DOM 25..425
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..804
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..144
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 278..314
FT /note="EGF-like"
FT DOMAIN 333..415
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 490..775
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 579..596
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 615
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 496..504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 518
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 649
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 282..294
FT /evidence="ECO:0000250"
FT DISULFID 288..302
FT /evidence="ECO:0000250"
FT DISULFID 368..389
FT /evidence="ECO:0000250"
FT DISULFID 372..378
FT /evidence="ECO:0000250"
SQ SEQUENCE 804 AA; 89935 MW; C8EAD5F6CAD85AB9 CRC64;
MGKKRIVFFA CLLLFTVLLR FSYAGITTES PLSVEQTLSS SNGIYELGFF SPNNSQNLYV
GIWFKGIIPR VVVWVANRET PTTDTSANLA ISSNGSLLLF NGKHGVVWSI GENFASNGSR
AELTDNGNLV VIDNASGRTL WESFEHFGDT MLPFSSLMYN LATGEKRVLT SWKTDTDPSP
GVFVGQITPQ VPSQVLIMRG STRYYRTGPW AKTRFTGIPL MDDTYASPFS LQQDANGSGF
FTYFDRSFKL SRIIISSEGS MKRFRHNGTD WELSYMAPAN SCDIYGVCGP FGLCIVSVPL
KCKCLKGFVP HSTEEWKRGN WTGGCARLTE LHCQGNSTGK DVNIFHPVTN VKLPDFYEYE
SSVDAEECHQ SCLHNCSCLA FAYIHGIGCL IWNQNLMDAV QFSAGGEILS IRLAHSELGG
NKRNKIIVAS TVSLSLFVIL TSAAFGFWRY RVKHKAYTLK DAWRNDLKSK EVPGLEFFEM
NTIQTATNNF SLSNKLGQGG FGSVYKGKLQ DGKEIAVKQL SSSSGQGKEE FMNEIVLISK
LQHRNLVRVL GCCIEGEEKL LIYEFMLNKS LDTFVFDARK KLEVDWPKRF DIVQGIARGL
LYLHRDSRLK VIHRDLKVSN ILLDEKMNPK ISDFGLARMY EGTQCQDKTR RVVGTLGYMS
PEYAWTGVFS EKSDIYSFGV LLLEIIIGEK ISRFSYGEEG KTLLAYAWES WGETKGIDLL
DQDLADSCRP LEVGRCVQIG LLCVQHQPAD RPNTLELLAM LTTTSDLPSP KQPTFVVHSR
DDESSLSKDL FTVNEMTQSM ILGR
