Y4119_ARATH
ID Y4119_ARATH Reviewed; 849 AA.
AC Q9T058; Q682D0;
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 At4g11900;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At4g11900; ORFNames=T26M18.110;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] (ISOFORM 2).
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 (SEP-2004) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9T058-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9T058-2; Sequence=VSP_040157, VSP_040158;
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; AL078606; CAB44328.1; -; Genomic_DNA.
DR EMBL; AL161533; CAB78233.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83067.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67245.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67251.1; -; Genomic_DNA.
DR EMBL; AK175437; BAD43200.1; -; mRNA.
DR PIR; T09349; T09349.
DR RefSeq; NP_001329085.1; NM_001340743.1. [Q9T058-2]
DR RefSeq; NP_001329091.1; NM_001340747.1. [Q9T058-2]
DR RefSeq; NP_192927.5; NM_117260.8. [Q9T058-1]
DR AlphaFoldDB; Q9T058; -.
DR SMR; Q9T058; -.
DR STRING; 3702.AT4G11900.1; -.
DR PaxDb; Q9T058; -.
DR PRIDE; Q9T058; -.
DR ProteomicsDB; 243190; -. [Q9T058-1]
DR EnsemblPlants; AT4G11900.1; AT4G11900.1; AT4G11900. [Q9T058-1]
DR EnsemblPlants; AT4G11900.10; AT4G11900.10; AT4G11900. [Q9T058-2]
DR EnsemblPlants; AT4G11900.5; AT4G11900.5; AT4G11900. [Q9T058-2]
DR GeneID; 826797; -.
DR Gramene; AT4G11900.1; AT4G11900.1; AT4G11900. [Q9T058-1]
DR Gramene; AT4G11900.10; AT4G11900.10; AT4G11900. [Q9T058-2]
DR Gramene; AT4G11900.5; AT4G11900.5; AT4G11900. [Q9T058-2]
DR KEGG; ath:AT4G11900; -.
DR Araport; AT4G11900; -.
DR TAIR; locus:2137010; AT4G11900.
DR eggNOG; ENOG502RCRG; Eukaryota.
DR HOGENOM; CLU_000288_116_4_1; -.
DR InParanoid; Q9T058; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9T058; -.
DR PRO; PR:Q9T058; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T058; baseline and differential.
DR Genevisible; Q9T058; 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: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; 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; 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; 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..849
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase At4g11900"
FT /id="PRO_0000401327"
FT TOPO_DOM 27..466
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..849
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..180
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 311..348
FT /note="EGF-like"
FT DOMAIN 368..447
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 537..822
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 626..643
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 662
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 543..551
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 565
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 696
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 844
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 315..327
FT /evidence="ECO:0000250"
FT DISULFID 321..336
FT /evidence="ECO:0000250"
FT DISULFID 401..421
FT /evidence="ECO:0000250"
FT DISULFID 405..411
FT /evidence="ECO:0000250"
FT VAR_SEQ 624..626
FT /note="DSL -> GEW (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_040157"
FT VAR_SEQ 627..849
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_040158"
SQ SEQUENCE 849 AA; 95816 MW; E7D3DA5D0CA5D3DE CRC64;
MQICKKNVFL LYYGVLVFLS FQVSSSTDTI STNQPLSGFE TIVSSGDIFE LGLFTPTPDT
YDHRNYYIGM WYRHVSPQTI VWVANRESPL GGDASTYLLK ILDGNLILHD NISATRKSHT
EGTSRRSPQK ISEGNLLFHE TVWSTGVNSS MSKDVQAVLF DSGNLVLRDG PNSSAAVLWQ
SFDHPSDTWL PGGKIRLGSQ LFTSWESLID PSPGRYSLEF DPKLHSLVTV WNRSKSYWSS
GPLYDWLQSF KGFPELQGTK LSFTLNMDES YITFSVDPQS RYRLVMGVSG QFMLQVWHVD
LQSWRVILSQ PDNRCDVYNS CGSFGICNEN REPPPCRCVP GFKREFSQGS DDSNDYSGGC
KRETYLHCYK RNDEFLPIEN MKLATDPTTA SVLTSGTFRT CASRCVADCS CQAYANDGNK
CLVWTKDAFN LQQLDANKGH TFFLRLASSN ISTANNRKTE HSKGKSIVLP LVLASLVATA
ACFVGLYCCI SSRIRRKKKQ RDEKHSRELL EGGLIDDAGE NMCYLNLHDI MVATNSFSRK
KKLGEGGFGP VYKGKLPNGM EVAIKRLSKK SSQGLTEFKN EVVLIIKLQH KNLVRLLGYC
VEGDEKLLIY EYMSNKSLDG LLFDSLKSRE LDWETRMKIV NGTTRGLQYL HEYSRLRIIH
RDLKASNILL DDEMNPKISD FGTARIFGCK QIDDSTQRIV GTFGYMSPEY ALGGVISEKS
DIYSFGVLLL EIISGKKATR FVHNDQKHSL IAYEWESWCE TKGVSIIDEP MCCSYSLEEA
MRCIHIALLC VQDHPKDRPM ISQIVYMLSN DNTLPIPKQP TFSNVLNGDQ QLDYVFSINE
ATQTELEAR
