Y1675_ARATH
ID Y1675_ARATH Reviewed; 818 AA.
AC O64793; F4HTM7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At1g67520;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g67520; ORFNames=F12B7.7, T1F15.1;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC18783.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG52302.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE34658.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004393; AAC18783.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011020; AAG52302.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34658.1; ALT_SEQ; Genomic_DNA.
DR PIR; T02153; T02153.
DR RefSeq; NP_176919.2; NM_105419.2.
DR AlphaFoldDB; O64793; -.
DR SMR; O64793; -.
DR PaxDb; O64793; -.
DR PRIDE; O64793; -.
DR ProteomicsDB; 243035; -.
DR GeneID; 843073; -.
DR KEGG; ath:AT1G67520; -.
DR Araport; AT1G67520; -.
DR eggNOG; ENOG502QTRQ; Eukaryota.
DR InParanoid; O64793; -.
DR PRO; PR:O64793; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O64793; baseline and differential.
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:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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; 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; PF08276; PAN_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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; 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; Glycoprotein; Kinase; Lectin;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..818
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase At1g67520"
FT /id="PRO_0000401325"
FT TOPO_DOM 23..387
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..818
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..149
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 290..379
FT /note="PAN"
FT DOMAIN 496..785
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 585..602
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 621
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 502..510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 655
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 807
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 813
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 330..353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DISULFID 334..340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
SQ SEQUENCE 818 AA; 93072 MW; 5A9E0E88CE3AD838 CRC64;
MCSNGIFVSL LTLSLLLGKS CSETDTLHQG QFLKDGQELV SAFKIFKLKF FNFKNSENLY
LGIWFNNLYL NTDSQDRPVW IANRNNPISD RSGSLTVDSL GRLKILRGAS TMLELSSIET
TRNTTLQLLD SGNLQLQEMD ADGSMKRVLW QSFDYPTDTL LPGMKLGFDG KTRKRWELTS
WLGDTLPASG SFVFGMDTNI TNVLTILWRG NMYWSSGLWN KGRFSEEELN ECGFLFSFVS
TKSGQYFMYS GDQDDARTFF PTIMIDEQGI LRREQMHRQR NRQNYRNRNC LAAGYVVRDE
PYGFTSFRVT VSSSASNGFV LSGTFSSVDC SAICLQNSSC LAYASTEPDG TGCEIWNTYP
TNKGSASHSP RTIYIRGNEN KKVAAWHIVV ATLFLMTPII WFIIYLVLRK FNVKGRNCIR
ITHKTVLVSM VFLLTMIGFI RRRILSLRFG STIDQEMLLR ELGIDRSCIH KRNERKSNNE
LQIFSFESVV SATDDFSDEN KLGEGGFGPV YKGKLLNGEE VAIKRLSLAS GQGLVEFKNE
AILIAKLQHT NLVQVLGCCI EKDEKMLIYE YMQNKSLDYF LFDPLRKNVL DWTLRFRIME
GIIQGLLYLH KYSRLKVIHR DIKASNILLD EDMNPKISDF GLARIFGAEE TRANTKRVAG
TFGYMSPEYF REGLFSAKSD VFSFGVLMLE IICGRKNNSF HHDLEGPLNL IVHVWNLFKE
NKIREVIDLS LRDSALDYPQ VLRCVQVALL CVQENAEDRP SMLDVVSMIY GEGNNALSLP
KEPAFYDGPR RSFPEMKVEP QEPENVSASI TITVLEAR
