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Y1571_ARATH
ID   Y1571_ARATH             Reviewed;        1120 AA.
AC   Q9LP24; C0LGF8; C0Z3K1; Q94B73;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Probable leucine-rich repeat receptor-like protein kinase At1g35710;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g35710; ORFNames=F14D7.1;
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] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=cv. Columbia;
RX   PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA   Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT   "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT   like protein kinase genes in Arabidopsis thaliana.";
RL   BMC Genomics 11:19-19(2010).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 294-708 (ISOFORM 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   -!- INTERACTION:
CC       Q9LP24-3; C0LGE0: At1g07650; NbExp=3; IntAct=EBI-20651291, EBI-16954597;
CC       Q9LP24-3; Q9LT96: At5g49770; NbExp=3; IntAct=EBI-20651291, EBI-17123993;
CC       Q9LP24-3; C0LGN2: LRR-RLK; NbExp=3; IntAct=EBI-20651291, EBI-20652801;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9LP24-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9LP24-2; Sequence=VSP_038434;
CC       Name=3;
CC         IsoId=Q9LP24-3; Sequence=VSP_038435;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF79881.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAK68748.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AC021198; AAF79881.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE31824.1; -; Genomic_DNA.
DR   EMBL; AK319165; BAH57280.1; -; mRNA.
DR   EMBL; FJ708647; ACN59243.1; -; mRNA.
DR   EMBL; AY042808; AAK68748.1; ALT_INIT; mRNA.
DR   PIR; B86479; B86479.
DR   RefSeq; NP_174809.1; NM_103273.2. [Q9LP24-1]
DR   AlphaFoldDB; Q9LP24; -.
DR   SMR; Q9LP24; -.
DR   BioGRID; 25707; 14.
DR   IntAct; Q9LP24; 17.
DR   STRING; 3702.AT1G35710.1; -.
DR   PaxDb; Q9LP24; -.
DR   PRIDE; Q9LP24; -.
DR   ProteomicsDB; 242438; -. [Q9LP24-1]
DR   EnsemblPlants; AT1G35710.1; AT1G35710.1; AT1G35710. [Q9LP24-1]
DR   GeneID; 840475; -.
DR   Gramene; AT1G35710.1; AT1G35710.1; AT1G35710. [Q9LP24-1]
DR   KEGG; ath:AT1G35710; -.
DR   Araport; AT1G35710; -.
DR   TAIR; locus:2011339; AT1G35710.
DR   eggNOG; ENOG502QQYD; Eukaryota.
DR   HOGENOM; CLU_000288_22_1_1; -.
DR   InParanoid; Q9LP24; -.
DR   OMA; SICANTF; -.
DR   OrthoDB; 179030at2759; -.
DR   PhylomeDB; Q9LP24; -.
DR   PRO; PR:Q9LP24; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LP24; baseline and differential.
DR   Genevisible; Q9LP24; 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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   Gene3D; 3.80.10.10; -; 5.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   Pfam; PF13855; LRR_8; 4.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00369; LRR_TYP; 13.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51450; LRR; 23.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Glycoprotein; Kinase;
KW   Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW   Signal; Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..1120
FT                   /note="Probable leucine-rich repeat receptor-like protein
FT                   kinase At1g35710"
FT                   /id="PRO_0000389461"
FT   TOPO_DOM        30..783
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        784..804
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        805..1120
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          78..100
FT                   /note="LRR 1"
FT   REPEAT          103..125
FT                   /note="LRR 2"
FT   REPEAT          127..150
FT                   /note="LRR 3"
FT   REPEAT          151..172
FT                   /note="LRR 4"
FT   REPEAT          175..198
FT                   /note="LRR 5"
FT   REPEAT          199..221
FT                   /note="LRR 6"
FT   REPEAT          223..246
FT                   /note="LRR 7"
FT   REPEAT          247..269
FT                   /note="LRR 8"
FT   REPEAT          271..294
FT                   /note="LRR 9"
FT   REPEAT          295..317
FT                   /note="LRR 10"
FT   REPEAT          319..342
FT                   /note="LRR 11"
FT   REPEAT          343..365
FT                   /note="LRR 12"
FT   REPEAT          367..389
FT                   /note="LRR 13"
FT   REPEAT          391..412
FT                   /note="LRR 14"
FT   REPEAT          415..437
FT                   /note="LRR 15"
FT   REPEAT          439..461
FT                   /note="LRR 16"
FT   REPEAT          463..484
FT                   /note="LRR 17"
FT   REPEAT          487..510
FT                   /note="LRR 18"
FT   REPEAT          535..557
FT                   /note="LRR 19"
FT   REPEAT          559..581
FT                   /note="LRR 20"
FT   REPEAT          583..605
FT                   /note="LRR 21"
FT   REPEAT          607..630
FT                   /note="LRR 22"
FT   REPEAT          631..652
FT                   /note="LRR 23"
FT   REPEAT          655..677
FT                   /note="LRR 24"
FT   REPEAT          678..701
FT                   /note="LRR 25"
FT   REPEAT          702..723
FT                   /note="LRR 26"
FT   REPEAT          726..748
FT                   /note="LRR 27"
FT   DOMAIN          851..1120
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        981
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         857..865
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         878
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         848
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O22476"
FT   MOD_RES         929
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O22476"
FT   MOD_RES         968
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT   MOD_RES         1014
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT   MOD_RES         1022
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT   MOD_RES         1029
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT   MOD_RES         1030
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
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        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        391
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        436
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        460
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        473
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        490
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        569
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        580
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        604
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        607
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        641
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        660
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        712
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..412
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172,
FT                   ECO:0000303|PubMed:19423640"
FT                   /id="VSP_038434"
FT   VAR_SEQ         825..1120
FT                   /note="ETGENMSIFSVDGKFKYQDIIESTNEFDPTHLIGTGGYSKVYRANLQDTIIA
FT                   VKRLHDTIDEEISKPVVKQEFLNEVKALTEIRHRNVVKLFGFCSHRRHTFLIYEYMEKG
FT                   SLNKLLANDEEAKRLTWTKRINVVKGVAHALSYMHHDRITPIVHRDISSGNILLDNDYT
FT                   AKISDFGTAKLLKTDSSNWSAVAGTYGYVAPEFAYTMKVTEKCDVYSFGVLILELIIGK
FT                   HPGDLVSSLSSSPGEALSLRSISDERVLEPRGQNREKLLKMVEMALLCLQANPESRPTM
FT                   LSISTTFS -> HRNRRIQQSLQSKPPRYNHSR (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:20064227"
FT                   /id="VSP_038435"
FT   CONFLICT        531
FT                   /note="G -> W (in Ref. 3; BAH57280)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        710
FT                   /note="H -> Y (in Ref. 4; ACN59243)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        Q9LP24-2:644
FT                   /note="G -> A (in Ref. 5; AAK68748)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        Q9LP24-2:655
FT                   /note="G -> A (in Ref. 5; AAK68748)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        Q9LP24-2:670
FT                   /note="E -> A (in Ref. 5; AAK68748)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        Q9LP24-2:677
FT                   /note="E -> Q (in Ref. 5; AAK68748)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1120 AA;  124104 MW;  DF5A5A0BA67B1357 CRC64;
     MGFAEKNLYD FRFLLFISII LSCSISASAT IAEANALLKW KSTFTNSSKL SSWVHDANTN
     TSFSCTSWYG VSCNSRGSIE ELNLTNTGIE GTFQDFPFIS LSNLAYVDLS MNLLSGTIPP
     QFGNLSKLIY FDLSTNHLTG EISPSLGNLK NLTVLYLHQN YLTSVIPSEL GNMESMTDLA
     LSQNKLTGSI PSSLGNLKNL MVLYLYENYL TGVIPPELGN MESMTDLALS QNKLTGSIPS
     TLGNLKNLMV LYLYENYLTG VIPPEIGNME SMTNLALSQN KLTGSIPSSL GNLKNLTLLS
     LFQNYLTGGI PPKLGNIESM IDLELSNNKL TGSIPSSLGN LKNLTILYLY ENYLTGVIPP
     ELGNMESMID LQLNNNKLTG SIPSSFGNLK NLTYLYLYLN YLTGVIPQEL GNMESMINLD
     LSQNKLTGSV PDSFGNFTKL ESLYLRVNHL SGAIPPGVAN SSHLTTLILD TNNFTGFFPE
     TVCKGRKLQN ISLDYNHLEG PIPKSLRDCK SLIRARFLGN KFTGDIFEAF GIYPDLNFID
     FSHNKFHGEI SSNWEKSPKL GALIMSNNNI TGAIPTEIWN MTQLVELDLS TNNLFGELPE
     AIGNLTNLSR LRLNGNQLSG RVPAGLSFLT NLESLDLSSN NFSSEIPQTF DSFLKLHDMN
     LSRNKFDGSI PRLSKLTQLT QLDLSHNQLD GEIPSQLSSL QSLDKLDLSH NNLSGLIPTT
     FEGMIALTNV DISNNKLEGP LPDTPTFRKA TADALEENIG LCSNIPKQRL KPCRELKKPK
     KNGNLVVWIL VPILGVLVIL SICANTFTYC IRKRKLQNGR NTDPETGENM SIFSVDGKFK
     YQDIIESTNE FDPTHLIGTG GYSKVYRANL QDTIIAVKRL HDTIDEEISK PVVKQEFLNE
     VKALTEIRHR NVVKLFGFCS HRRHTFLIYE YMEKGSLNKL LANDEEAKRL TWTKRINVVK
     GVAHALSYMH HDRITPIVHR DISSGNILLD NDYTAKISDF GTAKLLKTDS SNWSAVAGTY
     GYVAPEFAYT MKVTEKCDVY SFGVLILELI IGKHPGDLVS SLSSSPGEAL SLRSISDERV
     LEPRGQNREK LLKMVEMALL CLQANPESRP TMLSISTTFS
 
 
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