ID Y1148_ARATH Reviewed; 809 AA.
AC O64771;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 27-MAR-2024, entry version 170.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At1g61480;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g61480; ORFNames=T1F9.2;
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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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=AAC13892.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BX816606; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC004255; AAC13892.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33843.1; -; Genomic_DNA.
DR EMBL; BX816606; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A96640; A96640.
DR RefSeq; NP_176343.2; NM_104829.3.
DR AlphaFoldDB; O64771; -.
DR SMR; O64771; -.
DR STRING; 3702.O64771; -.
DR PaxDb; 3702-AT1G61480-1; -.
DR EnsemblPlants; AT1G61480.1; AT1G61480.1; AT1G61480.
DR GeneID; 842442; -.
DR Gramene; AT1G61480.1; AT1G61480.1; AT1G61480.
DR KEGG; ath:AT1G61480; -.
DR Araport; AT1G61480; -.
DR TAIR; AT1G61480; -.
DR eggNOG; ENOG502QSUU; Eukaryota.
DR HOGENOM; CLU_000288_116_1_1; -.
DR InParanoid; O64771; -.
DR OMA; RIMFFAS; -.
DR OrthoDB; 625308at2759; -.
DR PhylomeDB; O64771; -.
DR PRO; PR:O64771; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O64771; baseline and differential.
DR Genevisible; O64771; AT.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR CDD; cd00028; B_lectin; 1.
DR CDD; cd01098; PAN_AP_plant; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR32444:SF219; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
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; alpha-D-mannose-specific plant lectins; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 2: Evidence at transcript level;
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..809
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase At1g61480"
FT /id="PRO_0000401322"
FT TOPO_DOM 25..425
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..809
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..144
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 278..314
FT /note="EGF-like"
FT DOMAIN 333..415
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 496..781
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 585..602
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 621
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 502..510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 545
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 638
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 655
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
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 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 282..294
FT /evidence="ECO:0000250"
FT DISULFID 288..302
FT /evidence="ECO:0000250"
FT DISULFID 368..389
FT /evidence="ECO:0000250"
FT DISULFID 372..378
FT /evidence="ECO:0000250"
SQ SEQUENCE 809 AA; 90741 MW; 4BD5AF08635185D0 CRC64;
MGKKRIMFFA SLLLITIFLS FSYAGITRES PLSIGKTLSS SNGVYELGFF SFNNSQNQYV
GIWFKGIIPR VVVWVANREK PVTDSAANLT ISSNGSLLLF NENHSVVWSI GETFASNGSR
AELTDNGNLV VIDNNSGRTL WESFEHFGDT MLPFSNLMYN LATGEKRVLT SWKSHTDPSP
GDFTVQITPQ VPSQACTMRG SKTYWRSGPW AKTRFTGIPV MDDTYTSPFS LQQDTNGSGS
FTYFERNFKL SYIMITSEGS LKIFQHNGMD WELNFEAPEN SCDIYGFCGP FGICVMSVPP
KCKCFKGFVP KSIEEWKRGN WTDGCVRHTE LHCQGNTNGK TVNGFYHVAN IKPPDFYEFA
SFVDAEGCYQ ICLHNCSCLA FAYINGIGCL MWNQDLMDAV QFSAGGEILS IRLASSELGG
NKRNKIIVAS IVSLSLFVIL AFAAFCFLRY KVKHTVSAKI SKIASKEAWN NDLEPQDVSG
LKFFEMNTIQ TATDNFSLSN KLGQGGFGSV YKGKLQDGKE IAVKRLSSSS GQGKEEFMNE
IVLISKLQHK NLVRILGCCI EGEERLLVYE FLLNKSLDTF LFDSRKRLEI DWPKRFNIIE
GIARGLHYLH RDSCLRVIHR DLKVSNILLD EKMNPKISDF GLARMYQGTE YQDNTRRVAG
TLGYMAPEYA WTGMFSEKSD IYSFGVILLE IITGEKISRF SYGRQGKTLL AYAWESWCES
GGIDLLDKDV ADSCHPLEVE RCVQIGLLCV QHQPADRPNT MELLSMLTTT SDLTSPKQPT
FVVHTRDEES LSQGLITVNE MTQSVILGR
//
