Y1639_ARATH
ID Y1639_ARATH Reviewed; 831 AA.
AC O64781;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At1g61390;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g61390; ORFNames=T1F9.12;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O64781-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O64781-2; Sequence=VSP_040156;
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; AC004255; AAC13902.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33830.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33831.1; -; Genomic_DNA.
DR PIR; D96639; D96639.
DR RefSeq; NP_001154439.1; NM_001160967.2. [O64781-2]
DR RefSeq; NP_176334.1; NM_104820.2. [O64781-1]
DR AlphaFoldDB; O64781; -.
DR SMR; O64781; -.
DR PaxDb; O64781; -.
DR PRIDE; O64781; -.
DR EnsemblPlants; AT1G61390.1; AT1G61390.1; AT1G61390. [O64781-1]
DR EnsemblPlants; AT1G61390.2; AT1G61390.2; AT1G61390. [O64781-2]
DR GeneID; 842433; -.
DR Gramene; AT1G61390.1; AT1G61390.1; AT1G61390. [O64781-1]
DR Gramene; AT1G61390.2; AT1G61390.2; AT1G61390. [O64781-2]
DR KEGG; ath:AT1G61390; -.
DR Araport; AT1G61390; -.
DR TAIR; locus:2197704; AT1G61390.
DR HOGENOM; CLU_000288_116_4_1; -.
DR InParanoid; O64781; -.
DR OMA; WQKENDP; -.
DR OrthoDB; 407794at2759; -.
DR PhylomeDB; O64781; -.
DR PRO; PR:O64781; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O64781; baseline and differential.
DR Genevisible; O64781; 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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
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..42
FT /evidence="ECO:0000255"
FT CHAIN 43..831
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase At1g61390"
FT /id="PRO_0000401320"
FT TOPO_DOM 43..448
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..831
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..162
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 298..334
FT /note="EGF-like; atypical"
FT DOMAIN 353..439
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 520..803
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 609..626
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 645
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 526..534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 548
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 679
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 302..314
FT /evidence="ECO:0000250"
FT DISULFID 308..322
FT /evidence="ECO:0000250"
FT DISULFID 392..413
FT /evidence="ECO:0000250"
FT DISULFID 396..402
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..168
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040156"
SQ SEQUENCE 831 AA; 93048 MW; FAD97A615046F014 CRC64;
MYKLPQRNCA DKQEYTVHMR KMGMVIFACL LLLIIFPTFG YADINTSSPL SIGQTLSSPD
GVYELGFFSP NNSRKQYVGI WFKNIAPQVV VWVANRDKPV TKTAANLTIS SNGSLILLDG
TQDVIWSTGE AFTSNKCHAE LLDTGNLVVI DDVSGKTLWK SFENLGNTML PQSSVMYDIP
RGKNRVLTSW RSNSDPSPGE FTLEFTPQVP PQGLIRRGSS PYWRSGPWAK TRFSGIPGID
ASYVSPFTVL QDVAKGTASF SYSMLRNYKL SYVTLTSEGK MKILWNDGKS WKLHFEAPTS
SCDLYRACGP FGLCVRSRNP KCICLKGFVP KSDDEWKKGN WTSGCVRRTQ LSCHTNSSTK
TQGKETDSFY HMTRVKTPDL YQLAGFLNAE QCYQDCLGNC SCTAFAYISG IGCLVWNREL
VDTVQFLSDG ESLSLRLASS ELAGSNRTKI ILGTTVSLSI FVILVFAAYK SWRYRTKQNE
PNPMFIHSSQ DAWAKDMEPQ DVSGVNLFDM HTIRTATNNF SSSNKLGQGG FGPVYKGKLV
DGKEIAVKRL SSSSGQGTDE FMNEIRLISK LQHKNLVRLL GCCIKGEEKL LIYEYLVNKS
LDVFLFDSTL KFEIDWQKRF NIIQGVARGL LYLHRDSRLR VIHRDLKVSN ILLDEKMIPK
ISDFGLARMS QGTQYQDNTR RVVGTLGYMA PEYAWTGVFS EKSDIYSFGV LLLEIIIGEK
ISRFSEEGKT LLAYAWESWC ETKGVDLLDQ ALADSSHPAE VGRCVQIGLL CVQHQPADRP
NTLELMSMLT TISELPSPKQ PTFTVHSRDD DSTSNDLITV NEITQSVIQG R
