Y1112_ARATH
ID Y1112_ARATH Reviewed; 820 AA.
AC Q9SXB3; Q3EDE4; Q8H7E6; Q93ZU9;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At1g11280;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g11280; ORFNames=T28P6.7;
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 [MRNA] (ISOFORM 3).
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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=3;
CC Name=1;
CC IsoId=Q9SXB3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SXB3-2; Sequence=VSP_040152;
CC Name=3;
CC IsoId=Q9SXB3-3; Sequence=VSP_040153;
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; AF083714; AAN60272.1; -; mRNA.
DR EMBL; AC007259; AAD49994.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28709.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28710.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28711.1; -; Genomic_DNA.
DR EMBL; AY056250; AAL07099.1; -; mRNA.
DR EMBL; AY062482; AAL32560.1; -; mRNA.
DR PIR; G86246; G86246.
DR RefSeq; NP_563887.1; NM_101001.3. [Q9SXB3-2]
DR RefSeq; NP_849636.1; NM_179305.3. [Q9SXB3-1]
DR RefSeq; NP_849637.1; NM_179306.2. [Q9SXB3-3]
DR AlphaFoldDB; Q9SXB3; -.
DR SMR; Q9SXB3; -.
DR PaxDb; Q9SXB3; -.
DR PRIDE; Q9SXB3; -.
DR ProteomicsDB; 242414; -. [Q9SXB3-1]
DR EnsemblPlants; AT1G11280.1; AT1G11280.1; AT1G11280. [Q9SXB3-2]
DR EnsemblPlants; AT1G11280.2; AT1G11280.2; AT1G11280. [Q9SXB3-1]
DR EnsemblPlants; AT1G11280.3; AT1G11280.3; AT1G11280. [Q9SXB3-3]
DR GeneID; 837670; -.
DR Gramene; AT1G11280.1; AT1G11280.1; AT1G11280. [Q9SXB3-2]
DR Gramene; AT1G11280.2; AT1G11280.2; AT1G11280. [Q9SXB3-1]
DR Gramene; AT1G11280.3; AT1G11280.3; AT1G11280. [Q9SXB3-3]
DR KEGG; ath:AT1G11280; -.
DR Araport; AT1G11280; -.
DR TAIR; locus:2202089; AT1G11280.
DR InParanoid; Q9SXB3; -.
DR OrthoDB; 407794at2759; -.
DR PhylomeDB; Q9SXB3; -.
DR PRO; PR:Q9SXB3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SXB3; baseline and differential.
DR Genevisible; Q9SXB3; 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; IPR021820; S-locus_recpt_kinase_C.
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; PF11883; DUF3403; 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; PS50948; PAN; 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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..820
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase At1g11280"
FT /id="PRO_0000401306"
FT TOPO_DOM 29..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..820
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..148
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 283..319
FT /note="EGF-like"
FT DOMAIN 338..422
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 505..792
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 594..611
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 630
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 511..519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 533
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 664
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 815
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 287..299
FT /evidence="ECO:0000250"
FT DISULFID 293..307
FT /evidence="ECO:0000250"
FT DISULFID 377..398
FT /evidence="ECO:0000250"
FT DISULFID 381..387
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MDLKENSFEHM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_040152"
FT VAR_SEQ 464..475
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_040153"
FT CONFLICT 15
FT /note="W -> C (in Ref. 1; AAN60272)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="Q -> H (in Ref. 1; AAN60272)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="T -> N (in Ref. 1; AAN60272)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="I -> V (in Ref. 1; AAN60272)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="S -> N (in Ref. 1; AAN60272)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="A -> T (in Ref. 1; AAN60272)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="T -> A (in Ref. 4; AAL07099)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="D -> E (in Ref. 1; AAN60272)"
FT /evidence="ECO:0000305"
FT CONFLICT 661..666
FT /note="QDNTRK -> KTTLVR (in Ref. 1; AAN60272)"
FT /evidence="ECO:0000305"
FT CONFLICT 766
FT /note="V -> I (in Ref. 1; AAN60272)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 820 AA; 91337 MW; C91D361C956EDFBE CRC64;
MGIHLGEIGI VLFPWFLWLS LFLSCGYAAI TISSPLTLGQ TLSSPGGFYE LGFFSPNNSQ
NQYVGIWFKK ITPRVVVWVA NREKPITTPV ANLTISRNGS LILLDSSKNV VWSTRRPSIS
NKCHAKLLDT GNLVIVDDVS ENLLWQSFEN PGDTMLPYSS LMYNLATGEK RVLSSWKSHT
DPSPGDFVVR LTPQVPAQIV TMRGSSVYKR SGPWAKTGFT GVPLMDESYT SPFSLSQDVG
NGTGLFSYLQ RSSELTRVII TSEGYLKTFR YNGTGWVLDF ITPANLCDLY GACGPFGLCV
TSNPTKCKCM KGFVPKYKEE WKRGNMTSGC MRRTELSCQA NLSTKTQGKG VDVFYRLANV
KPPDLYEYAS FVDADQCHQG CLSNCSCSAF AYITGIGCLL WNHELIDTIR YSVGGEFLSI
RLASSELAGS RRTKIIVGSI SLSIFVILAF GSYKYWRYRA KQNVGPTWAF FNNSQDSWKN
GLEPQEISGL TFFEMNTIRA ATNNFNVSNK LGQGGFGPVY KGTLSDKKDI AVKRLSSSSG
QGTEEFMNEI KLISKLQHRN LVRLLGCCID GEEKLLIYEF LVNKSLDTFL FDLTLKLQID
WPKRFNIIQG VSRGLLYLHR DSCMRVIHRD LKVSNILLDD KMNPKISDFG LARMFQGTQH
QDNTRKVVGT LGYMSPEYAW TGMFSEKSDI YAFGVLLLEI ISGKKISSFC CGEEGKTLLG
HAWECWLETG GVDLLDEDIS SSCSPVEVEV ARCVQIGLLC IQQQAVDRPN IAQVVTMMTS
ATDLPRPKQP LFALQIQDQE SVVSVSKSVN HVTQTEIYGR
