Y1146_ARATH
ID Y1146_ARATH Reviewed; 749 AA.
AC O64774; F4HTL5; Q0WQD4;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 4.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At1g61460;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g61460; ORFNames=T1F9.5;
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC13895.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF00665.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AC004255; AAC13895.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33840.2; -; Genomic_DNA.
DR EMBL; AK228765; BAF00665.1; ALT_SEQ; mRNA.
DR RefSeq; NP_176341.3; NM_104827.3.
DR AlphaFoldDB; O64774; -.
DR SMR; O64774; -.
DR PaxDb; O64774; -.
DR PRIDE; O64774; -.
DR EnsemblPlants; AT1G61460.1; AT1G61460.1; AT1G61460.
DR GeneID; 842440; -.
DR Gramene; AT1G61460.1; AT1G61460.1; AT1G61460.
DR KEGG; ath:AT1G61460; -.
DR Araport; AT1G61460; -.
DR HOGENOM; CLU_000288_116_5_1; -.
DR InParanoid; O64774; -.
DR OMA; HCQENST; -.
DR OrthoDB; 479847at2759; -.
DR PRO; PR:O64774; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O64774; baseline and differential.
DR Genevisible; O64774; 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; 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; 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 ATP-binding; Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein;
KW Kinase; Lectin; Membrane; Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..749
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase At1g61460"
FT /id="PRO_0000401313"
FT TOPO_DOM 26..392
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..749
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..145
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 247..280
FT /note="EGF-like; atypical"
FT DOMAIN 299..381
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 454..721
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 543..560
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 579
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 460..468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
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 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 251..263
FT /evidence="ECO:0000250"
FT DISULFID 257..268
FT /evidence="ECO:0000250"
FT DISULFID 334..355
FT /evidence="ECO:0000250"
FT DISULFID 338..344
FT /evidence="ECO:0000250"
FT CONFLICT 472
FT /note="K -> E (in Ref. 3; BAF00665)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 749 AA; 84086 MW; 29944AD15D4570D5 CRC64;
MRITFFASLL LFTNTIFISF SFAIAGINKE SPLSIGQTLS SSNGVYELGF FSFNNSENHY
LGIWFKGIIP RVVVWVANRE NPVTDSTANL AISSNASLLL YNGKHGVAWS SGETLASNGS
RAELSDTGNL IVIDNFSGRT LWQSFDHLGD TMLPFSALMY NLATGEKQVL TSWKSYTNPA
VGDFVLQITT QVPTQALTMR GSKPYWRSGP WAKTRNFKLP RIVITSKGSL EISRHSGTDW
VLNFVAPAHS CDYYGVCGPF GICVKSVCKC FKGFIPKYIE EWKRGNWTDG CVRRTKLHCQ
ENSTKKDANF FHPVANIKPP DFYEFASAVD AEGCYKICLH NCSCLAFSYI HGIGCLIWNQ
DFMDTVQFSA GGEILSIRLA RSELGGNKRK KTITASIVSL SLFLILGSTA FGFWRYRVKH
NASQDAPKYD LEPQDVSGSY LFEMNTIQTA TNNFSLSNKL GQGGFGSVYK GKLQDGKEIA
VKRLSSSSGQ GKEEFMNEIV LISKLQHKNL VRILGCCIEG EERLLIYEFM LNKSLDTFLF
DSRKRLEIDW PKRFDIIQGI ARGIHYLHRD SCLKVIHRDL KVSNILLDEK MNPKISDFGL
ARMYQGTEYQ DNTRRVVGTL GYMSPEDILE IISGEKISRF SYGKEEKTLI AYAWESWCET
GGVDLLDKDV ADSCRPLEVE RCIQIGLLCV QHQPADRPNT LELMSMLTTT SDLPSPKQPT
FVVHWRDDES SSKDLITVNE MTKSVILGR
