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
