Y1343_ARATH
ID Y1343_ARATH Reviewed; 829 AA.
AC Q9XID3;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At1g34300;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g34300; ORFNames=F23M19.5;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200;
RA Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA Barbier-Brygoo H., Ephritikhine G.;
RT "A high content in lipid-modified peripheral proteins and integral receptor
RT kinases features in the arabidopsis plasma membrane proteome.";
RL Mol. Cell. Proteomics 6:1980-1996(2007).
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:0000305|PubMed:17644812};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:17644812}.
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; AC007454; AAD39605.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31694.1; -; Genomic_DNA.
DR EMBL; AY090246; AAL90909.1; -; mRNA.
DR EMBL; BT001084; AAN46865.1; -; mRNA.
DR PIR; B86467; B86467.
DR RefSeq; NP_174690.1; NM_103152.4.
DR AlphaFoldDB; Q9XID3; -.
DR SMR; Q9XID3; -.
DR IntAct; Q9XID3; 2.
DR STRING; 3702.AT1G34300.1; -.
DR iPTMnet; Q9XID3; -.
DR PaxDb; Q9XID3; -.
DR PRIDE; Q9XID3; -.
DR ProteomicsDB; 242417; -.
DR EnsemblPlants; AT1G34300.1; AT1G34300.1; AT1G34300.
DR GeneID; 840330; -.
DR Gramene; AT1G34300.1; AT1G34300.1; AT1G34300.
DR KEGG; ath:AT1G34300; -.
DR Araport; AT1G34300; -.
DR TAIR; locus:2026155; AT1G34300.
DR eggNOG; ENOG502QRWA; Eukaryota.
DR HOGENOM; CLU_000288_116_2_1; -.
DR InParanoid; Q9XID3; -.
DR OMA; PWPTRFA; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9XID3; -.
DR PRO; PR:Q9XID3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XID3; baseline and differential.
DR Genevisible; Q9XID3; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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; IEA:InterPro.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR Gene3D; 2.90.10.10; -; 2.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR045874; LRK10-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR27009; PTHR27009; 1.
DR Pfam; PF01453; B_lectin; 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; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; SSF51110; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein;
KW Kinase; Lectin; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..829
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase At1g34300"
FT /id="PRO_0000401314"
FT TOPO_DOM 26..421
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..829
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..140
FT /note="Bulb-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 143..260
FT /note="Bulb-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 264..301
FT /note="EGF-like"
FT DOMAIN 317..399
FT /note="Apple"
FT DOMAIN 484..759
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 572..589
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 608
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 490..498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 532
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 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 46
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 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
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 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 268..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DISULFID 274..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DISULFID 317..399
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DISULFID 350..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DISULFID 354..360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
SQ SEQUENCE 829 AA; 91293 MW; 908A5438F177D197 CRC64;
MAVKTPFLKL LPLLLLLLHF PFSFSTIPLG SVIYASGSNQ NWPSPNSTFS VSFVPSPSPN
SFLAAVSFAG SVPIWSAGTV DSRGSLRLHT SGSLRLTNGS GTTVWDSKTD RLGVTSGSIE
DTGEFILLNN RSVPVWSSFD NPTDTIVQSQ NFTAGKILRS GLYSFQLERS GNLTLRWNTS
AIYWNHGLNS SFSSNLSSPR LSLQTNGVVS IFESNLLGGA EIVYSGDYGD SNTFRFLKLD
DDGNLRIYSS ASRNSGPVNA HWSAVDQCLV YGYCGNFGIC SYNDTNPICS CPSRNFDFVD
VNDRRKGCKR KVELSDCSGN TTMLDLVHTR LFTYEDDPNS ESFFAGSSPC RANCLSSVLC
LASVSMSDGS GNCWQKHPGS FFTGYQWPSV PSTSYVKVCG PVVANTLERA TKGDDNNSKV
HLWIVAVAVI AGLLGLVAVE IGLWWCCCRK NPRFGTLSSH YTLLEYASGA PVQFTYKELQ
RCTKSFKEKL GAGGFGTVYR GVLTNRTVVA VKQLEGIEQG EKQFRMEVAT ISSTHHLNLV
RLIGFCSQGR HRLLVYEFMR NGSLDNFLFT TDSAKFLTWE YRFNIALGTA KGITYLHEEC
RDCIVHCDIK PENILVDDNF AAKVSDFGLA KLLNPKDNRY NMSSVRGTRG YLAPEWLANL
PITSKSDVYS YGMVLLELVS GKRNFDVSEK TNHKKFSIWA YEEFEKGNTK AILDTRLSED
QTVDMEQVMR MVKTSFWCIQ EQPLQRPTMG KVVQMLEGIT EIKNPLCPKT ISEVSFSGNS
MSTSHASMFV ASGPTRSSSF SATRSFQTMG ITSSGPASTR ISEGSMLGS
