Y1614_ARATH
ID Y1614_ARATH Reviewed; 814 AA.
AC O64780; F4HTK7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 4.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At1g61400;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g61400; ORFNames=T1F9.11;
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=AAC13901.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004255; AAC13901.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33832.2; -; Genomic_DNA.
DR RefSeq; NP_001319284.1; NM_001333955.1.
DR AlphaFoldDB; O64780; -.
DR SMR; O64780; -.
DR STRING; 3702.AT1G61400.1; -.
DR PaxDb; O64780; -.
DR PRIDE; O64780; -.
DR ProteomicsDB; 234338; -.
DR EnsemblPlants; AT1G61400.1; AT1G61400.1; AT1G61400.
DR GeneID; 842434; -.
DR Gramene; AT1G61400.1; AT1G61400.1; AT1G61400.
DR KEGG; ath:AT1G61400; -.
DR Araport; AT1G61400; -.
DR eggNOG; ENOG502QQPW; Eukaryota.
DR HOGENOM; CLU_000288_116_1_1; -.
DR InParanoid; O64780; -.
DR PRO; PR:O64780; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O64780; baseline and differential.
DR Genevisible; O64780; 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; IPR017441; Protein_kinase_ATP_BS.
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; PS00107; PROTEIN_KINASE_ATP; 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; Phosphoprotein; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..814
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase At1g61400"
FT /id="PRO_0000401317"
FT TOPO_DOM 35..436
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..814
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..154
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 288..324
FT /note="EGF-like; atypical"
FT DOMAIN 343..425
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 500..785
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 589..606
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 625
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 506..514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 659
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 796
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 292..304
FT /evidence="ECO:0000250"
FT DISULFID 298..312
FT /evidence="ECO:0000250"
FT DISULFID 378..399
FT /evidence="ECO:0000250"
FT DISULFID 382..388
FT /evidence="ECO:0000250"
SQ SEQUENCE 814 AA; 91382 MW; F8C872A89CE49009 CRC64;
MDFLFLLLER KNKHMGKKRV VLLWLSIFIS FSSAEITEES PLSIGQTLSS SNGVYELGFF
SFNNSQNQYV GISFKGIIPR VVVWVANREK PVTDSAANLV ISSNGSLQLF NGKHGVVWSS
GKALASNGSR VELLDSGNLV VIEKVSGRTL WESFEHLGDT LLPHSTIMYN VHTGEKRGLT
SWKSYTDPSP GDFVVLITPQ VPSQGFLMRG STPYFRSGPW AKTKFTGLPQ MDESYTSPFS
LTQDVNGSGY YSYFDRDNKR SRIRLTPDGS MKALRYNGMD WDTTYEGPAN SCDIYGVCGP
FGFCVISVPP KCKCFKGFIP KSIEEWKTGN WTSGCVRRSE LHCQGNSTGK DANVFHTVPN
IKPPDFYEYA DSVDAEECQQ NCLNNCSCLA FAYIPGIGCL MWSKDLMDTV QFAAGGELLS
IRLARSELDV NKRKKTIIAI TVSLTLFVIL GFTAFGFWRR RVEQNALISE DAWRNDLQTQ
DVPGLEYFEM NTIQTATNNF SLSNKLGHGG FGSVYKGKLQ DGREIAVKRL SSSSEQGKQE
FMNEIVLISK LQHRNLVRVL GCCVEGTEKL LIYEFMKNKS LDTFVFDSKK RLEIDWPKRF
DIIQGIARGL LYLHRDSRLR IIHRDLKVSN ILLDEKMNPK ISDFGLARMF HGTEYQDKTR
RVVGTLGYMS PEYAWAGVFS EKSDIYSFGV LLLEIISGEK ISRFSYGEEG KTLLAYAWEC
WCGARGVNLL DQALGDSCHP YEVGRCVQIG LLCVQYQPAD RPNTLELLSM LTTTSDLPLP
KQPTFVVHTR DGKSPSNDSM ITVNEMTESV IHGR
