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Y1141_ARATH
ID   Y1141_ARATH             Reviewed;         845 AA.
AC   Q9LPZ3;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 3.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At1g11410;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g11410; ORFNames=T23J18.8;
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=AAF16627.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC011661; AAF16627.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE28733.1; -; Genomic_DNA.
DR   RefSeq; NP_001318981.1; NM_001331984.1.
DR   AlphaFoldDB; Q9LPZ3; -.
DR   SMR; Q9LPZ3; -.
DR   BioGRID; 22923; 1.
DR   IntAct; Q9LPZ3; 1.
DR   STRING; 3702.AT1G11410.1; -.
DR   PaxDb; Q9LPZ3; -.
DR   ProteomicsDB; 243180; -.
DR   EnsemblPlants; AT1G11410.1; AT1G11410.1; AT1G11410.
DR   GeneID; 837683; -.
DR   Gramene; AT1G11410.1; AT1G11410.1; AT1G11410.
DR   KEGG; ath:AT1G11410; -.
DR   Araport; AT1G11410; -.
DR   TAIR; locus:2200136; AT1G11410.
DR   eggNOG; ENOG502QUDG; Eukaryota.
DR   HOGENOM; CLU_000288_116_1_1; -.
DR   InParanoid; Q9LPZ3; -.
DR   PRO; PR:Q9LPZ3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LPZ3; baseline and differential.
DR   Genevisible; Q9LPZ3; 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: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; 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; 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   3: Inferred from homology;
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..845
FT                   /note="G-type lectin S-receptor-like serine/threonine-
FT                   protein kinase At1g11410"
FT                   /id="PRO_0000401310"
FT   TOPO_DOM        22..441
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        442..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        463..845
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          22..147
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DOMAIN          283..321
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          341..424
FT                   /note="PAN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT   DOMAIN          523..808
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          612..629
FT                   /note="CaM-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          803..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..845
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        648
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         529..537
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         551
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
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        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        379
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        287..299
FT                   /evidence="ECO:0000250"
FT   DISULFID        293..309
FT                   /evidence="ECO:0000250"
FT   DISULFID        372..399
FT                   /evidence="ECO:0000250"
FT   DISULFID        376..382
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   845 AA;  95862 MW;  2F9BDC7E4B655DFE CRC64;
     MKFFFIFFIF LFSFLIQSCY SDNTILRSQS LKDGDVIYSE GKRFAFGFFS LGNSKLRYVG
     IWYAQVSEQT IVWVANRDHP INDTSGLIKF STRGNLCVYA SGNGTEPIWS TDVIDMIQEP
     ALVAKLSDLG NLVLLDPVTG KSFWESFNHP TNTLLPFMKF GFTRQSGVDR IMTSWRSPGD
     PGSGNITYRI ERRGFPQMMM YKGLTLWWRT GSWTGQRWSG VPEMTNKFIF NISFVNNPDE
     VSITYGVLDA SVTTRMVLNE TGTLQRFRWN GRDKKWIGFW SAPEDKCDIY NHCGFNGYCD
     STSTEKFECS CLPGYEPKTP RDWFLRDASD GCTRIKADSI CNGKEGFAKL KRVKIPNTSA
     VNVDMNITLK ECEQRCLKNC SCVAYASAYH ESQDGAKGCL TWHGNMLDTR TYLSSGQDFY
     LRVDKSELAR WNGNGASGKK RLVLILISLI AVVMLLLISF HCYLRKRRQR TQSNRLRKAP
     SSFAPSSFDL EDSFILEELE DKSRSRELPL FELSTIATAT NNFAFQNKLG AGGFGPVYKG
     VLQNGMEIAV KRLSKSSGQG MEEFKNEVKL ISKLQHRNLV RILGCCVEFE EKMLVYEYLP
     NKSLDYFIFH EEQRAELDWP KRMGIIRGIG RGILYLHQDS RLRIIHRDLK ASNVLLDNEM
     IPKIADFGLA RIFGGNQIEG STNRVVGTYG YMSPEYAMDG QFSIKSDVYS FGVLILEIIT
     GKRNSAFYEE SLNLVKHIWD RWENGEAIEI IDKLMGEETY DEGEVMKCLH IGLLCVQENS
     SDRPDMSSVV FMLGHNAIDL PSPKHPAFTA GRRRNTKTGG SSDNWPSGET SSTINDVTLT
     DVQGR
 
 
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