Y1136_ARATH
ID Y1136_ARATH Reviewed; 821 AA.
AC O64784; Q0WPR0;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At1g61360;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g61360; ORFNames=T1F9.15;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) 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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O64784-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O64784-2; Sequence=VSP_040155;
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; AAC13905.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33826.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33827.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59343.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59344.1; -; Genomic_DNA.
DR EMBL; AK229002; BAF00889.1; -; mRNA.
DR RefSeq; NP_001154438.1; NM_001160966.1. [O64784-2]
DR RefSeq; NP_001321708.1; NM_001333952.1. [O64784-2]
DR RefSeq; NP_001321709.1; NM_001333951.1. [O64784-2]
DR RefSeq; NP_176331.1; NM_104817.3. [O64784-1]
DR AlphaFoldDB; O64784; -.
DR SMR; O64784; -.
DR STRING; 3702.AT1G61360.1; -.
DR PaxDb; O64784; -.
DR PRIDE; O64784; -.
DR ProteomicsDB; 242518; -. [O64784-1]
DR EnsemblPlants; AT1G61360.1; AT1G61360.1; AT1G61360. [O64784-1]
DR EnsemblPlants; AT1G61360.2; AT1G61360.2; AT1G61360. [O64784-2]
DR EnsemblPlants; AT1G61360.3; AT1G61360.3; AT1G61360. [O64784-2]
DR EnsemblPlants; AT1G61360.4; AT1G61360.4; AT1G61360. [O64784-2]
DR GeneID; 842430; -.
DR Gramene; AT1G61360.1; AT1G61360.1; AT1G61360. [O64784-1]
DR Gramene; AT1G61360.2; AT1G61360.2; AT1G61360. [O64784-2]
DR Gramene; AT1G61360.3; AT1G61360.3; AT1G61360. [O64784-2]
DR Gramene; AT1G61360.4; AT1G61360.4; AT1G61360. [O64784-2]
DR KEGG; ath:AT1G61360; -.
DR Araport; AT1G61360; -.
DR TAIR; locus:2197649; AT1G61360.
DR eggNOG; ENOG502QQPW; Eukaryota.
DR HOGENOM; CLU_000288_116_1_1; -.
DR InParanoid; O64784; -.
DR OMA; FIDYAWH; -.
DR PhylomeDB; O64784; -.
DR PRO; PR:O64784; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O64784; baseline and differential.
DR Genevisible; O64784; 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; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF08276; PAN_2; 1.
DR Pfam; PF00069; Pkinase; 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 Alternative splicing; ATP-binding; Cell membrane; Disulfide bond;
KW EGF-like domain; Glycoprotein; Kinase; Lectin; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..821
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase At1g61360"
FT /id="PRO_0000401315"
FT TOPO_DOM 21..427
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..821
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..140
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 276..312
FT /note="EGF-like"
FT DOMAIN 331..417
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 498..785
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 587..604
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT REGION 774..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 623
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 504..512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 657
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 807
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 280..292
FT /evidence="ECO:0000250"
FT DISULFID 286..300
FT /evidence="ECO:0000250"
FT DISULFID 370..391
FT /evidence="ECO:0000250"
FT DISULFID 374..380
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..81
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040155"
FT CONFLICT 209
FT /note="T -> A (in Ref. 3; BAF00889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 821 AA; 90934 MW; 425CA39FCCF6A348 CRC64;
MRIVACLLLI TALFSSYGYA AITTSSPLSI GVTLSSPGGS YELGFFSSNN SGNQYVGIWF
KKVTPRVIVW VANREKPVSS TMANLTISSN GSLILLDSKK DLVWSSGGDP TSNKCRAELL
DTGNLVVVDN VTGNYLWQSF EHLGDTMLPL TSLMYDIPNN KKRVLTSWKS ETDPSPGEFV
AEITPQVPSQ GLIRKGSSPY WRSGPWAGTR FTGIPEMDAS YVNPLGMVQD EVNGTGVFAF
CVLRNFNLSY IKLTPEGSLR ITRNNGTDWI KHFEGPLTSC DLYGRCGPFG LCVRSGTPMC
QCLKGFEPKS DEEWRSGNWS RGCVRRTNLS CQGNSSVETQ GKDRDVFYHV SNIKPPDSYE
LASFSNEEQC HQGCLRNCSC TAFSYVSGIG CLVWNQELLD TVKFIGGGET LSLRLAHSEL
TGRKRIKIIT VATLSLSVCL ILVLVACGCW RYRVKQNGSS LVSKDNVEGA WKSDLQSQDV
SGLNFFEIHD LQTATNNFSV LNKLGQGGFG TVYKGKLQDG KEIAVKRLTS SSVQGTEEFM
NEIKLISKLQ HRNLLRLLGC CIDGEEKLLV YEYMVNKSLD IFIFDLKKKL EIDWATRFNI
IQGIARGLLY LHRDSFLRVV HRDLKVSNIL LDEKMNPKIS DFGLARLFHG NQHQDSTGSV
VGTLGYMSPE YAWTGTFSEK SDIYSFGVLM LEIITGKEIS SFSYGKDNKN LLSYAWDSWS
ENGGVNLLDQ DLDDSDSVNS VEAGRCVHIG LLCVQHQAID RPNIKQVMSM LTSTTDLPKP
TQPMFVLETS DEDSSLSHSQ RSNDLSSVDE NKSSEELNAS S
