Y1155_ARATH
ID Y1155_ARATH Reviewed; 802 AA.
AC Q9SY95;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At1g61550;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g61550; ORFNames=T25B24.10;
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; AAD25553.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33850.1; -; Genomic_DNA.
DR PIR; G96640; G96640.
DR RefSeq; NP_176349.1; NM_104835.3.
DR AlphaFoldDB; Q9SY95; -.
DR SMR; Q9SY95; -.
DR PaxDb; Q9SY95; -.
DR PRIDE; Q9SY95; -.
DR ProteomicsDB; 242501; -.
DR EnsemblPlants; AT1G61550.1; AT1G61550.1; AT1G61550.
DR GeneID; 842449; -.
DR Gramene; AT1G61550.1; AT1G61550.1; AT1G61550.
DR KEGG; ath:AT1G61550; -.
DR Araport; AT1G61550; -.
DR TAIR; locus:2200923; AT1G61550.
DR HOGENOM; CLU_000288_116_1_1; -.
DR InParanoid; Q9SY95; -.
DR OMA; FIMRGSK; -.
DR OrthoDB; 407794at2759; -.
DR PhylomeDB; Q9SY95; -.
DR PRO; PR:Q9SY95; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SY95; baseline and differential.
DR Genevisible; Q9SY95; 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; IPR000742; EGF-like_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50026; EGF_3; 1.
DR PROSITE; PS50948; PAN; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..802
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase At1g61550"
FT /id="PRO_0000401318"
FT TOPO_DOM 20..421
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..802
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..139
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 273..309
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 328..410
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 489..774
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 578..595
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 614
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 495..503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 648
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 277..289
FT /evidence="ECO:0000250"
FT DISULFID 283..297
FT /evidence="ECO:0000250"
FT DISULFID 363..384
FT /evidence="ECO:0000250"
FT DISULFID 367..373
FT /evidence="ECO:0000250"
SQ SEQUENCE 802 AA; 89398 MW; AEB1FE82E4B89298 CRC64;
MTRFACFLFS TLLLSFSYAA ITPTSPLSIG QTLSSPNGIF ELGFFSPNNS RNLYVGIWFK
GIIPRTVVWV ANRENSVTDA TADLAISSNG SLLLFDGKHS TVWSTGETFA SNGSSAELSD
SGNLLVIDKV SGITLWQSFE HLGDTMLPYS SLMYNPGTGE KRVLSSWKSY TDPLPGEFVG
YITTQVPPQG FIMRGSKPYW RSGPWAKTRF TGVPLTDESY THPFSVQQDA NGSVYFSHLQ
RNFKRSLLVL TSEGSLKVTH HNGTDWVLNI DVPANTCDFY GVCGPFGLCV MSIPPKCKCF
KGFVPQFSEE WKRGNWTGGC VRRTELLCQG NSTGRHVNVF HPVANIKPPD FYEFVSSGSA
EECYQSCLHN CSCLAFAYIN GIGCLIWNQE LMDVMQFSVG GELLSIRLAS SEMGGNQRKK
TIIASIVSIS LFVTLASAAF GFWRYRLKHN AIVSKVSLQG AWRNDLKSED VSGLYFFEMK
TIEIATNNFS LVNKLGQGGF GPVYKGKLQD GKEIAVKRLS SSSGQGKEEF MNEILLISKL
QHINLVRILG CCIEGEERLL VYEFMVNKSL DTFIFDSRKR VEIDWPKRFS IIQGIARGLL
YLHRDSRLRI IHRDVKVSNI LLDDKMNPKI SDFGLARMYE GTKYQDNTRR IVGTLGYMSP
EYAWTGVFSE KSDTYSFGVL LLEVISGEKI SRFSYDKERK NLLAYAWESW CENGGVGFLD
KDATDSCHPS EVGRCVQIGL LCVQHQPADR PNTLELLSML TTTSDLPLPK EPTFAVHTSD
DGSRTSDLIT VNEVTQSVVL GR
