Y5537_ARATH
ID Y5537_ARATH Reviewed; 872 AA.
AC O65238; Q0WL86; Q0WVA9; Q9FZP3;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At5g35370;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At5g35370; ORFNames=T26D22.12;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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=AAC13608.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB11487.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE98939.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AB025636; BAB11487.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF058826; AAC13608.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93959.1; -; Genomic_DNA.
DR EMBL; AK226846; BAE98939.1; ALT_SEQ; mRNA.
DR EMBL; AK230321; BAF02121.1; -; mRNA.
DR PIR; T01181; T01181.
DR RefSeq; NP_198387.2; NM_122928.3.
DR AlphaFoldDB; O65238; -.
DR SMR; O65238; -.
DR STRING; 3702.AT5G35370.1; -.
DR PaxDb; O65238; -.
DR PRIDE; O65238; -.
DR ProteomicsDB; 242835; -.
DR EnsemblPlants; AT5G35370.1; AT5G35370.1; AT5G35370.
DR GeneID; 833498; -.
DR Gramene; AT5G35370.1; AT5G35370.1; AT5G35370.
DR KEGG; ath:AT5G35370; -.
DR Araport; AT5G35370; -.
DR TAIR; locus:2182603; AT5G35370.
DR eggNOG; ENOG502QU6U; Eukaryota.
DR HOGENOM; CLU_000288_116_2_1; -.
DR InParanoid; O65238; -.
DR OMA; VQGKKDF; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O65238; -.
DR PRO; PR:O65238; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O65238; baseline and differential.
DR Genevisible; O65238; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00028; B_lectin; 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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 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; 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..872
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase At5g35370"
FT /id="PRO_0000401331"
FT TOPO_DOM 27..443
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..872
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..156
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 283..322
FT /note="EGF-like; atypical"
FT DOMAIN 338..423
FT /note="PAN"
FT DOMAIN 515..814
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 603..620
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT REGION 836..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 639
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 521..529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 543
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 673
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 287..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DISULFID 293..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DISULFID 372..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DISULFID 376..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
SQ SEQUENCE 872 AA; 96046 MW; FADB4EBB3A0F4374 CRC64;
MKSTFLLLLL LLSLNLLFVF VSCASSIEFV YPNFTASNLR FVDSSKGAFL LSRNSIFKAG
LFSPGGDDSS TGFYFSVVHV DSGSTIWSSN RDSPVSSSGT MNLTPQGISV IEDGKSQIPV
WSTPVLASPV KSLRLTDAGN LLLLDHLNVS LWESFDFPTD SIVLGQRLKL GMFLSGSVSR
SDFSTGDYKF LVGESDGLMQ WRGQNYWKLR MHIRANVDSN FPVEYLTVTT SGLALMARNG
TVVVVRVALP PSSDFRVAKM DSSGKFIVSR FSGKNLVTEF SGPMDSCQIP FVCGKLGLCN
LDNASENQSC SCPDEMRMDA GKGVCVPVSQ SLSLPVSCEA RNISYLELGL GVSYFSTHFT
DPVEHGLPLL ACHDICSKNC SCLGVFYENT SRSCYLVKDS FGSLSLVKNS PENHDLIGYV
KLSIRKTNAQ PPGNNNRGGS SFPVIALVLL PCSGFFLLIA LGLLWWRRCA VMRYSSIREK
QVTRPGSFES GDLGSFHIPG LPQKFEFEEL EQATENFKMQ IGSGGFGSVY KGTLPDETLI
AVKKITNHGL HGRQEFCTEI AIIGNIRHTN LVKLRGFCAR GRQLLLVYEY MNHGSLEKTL
FSGNGPVLEW QERFDIALGT ARGLAYLHSG CDQKIIHCDV KPENILLHDH FQPKISDFGL
SKLLNQEESS LFTTMRGTRG YLAPEWITNA AISEKADVYS YGMVLLELVS GRKNCSFRSR
SNSVTEDNNQ NHSSTTTTST GLVYFPLYAL DMHEQGRYME LADPRLEGRV TSQEAEKLVR
IALCCVHEEP ALRPTMAAVV GMFEGSIPLG NPRMESLNFL RFYGLRFAES SMVEGQNGES
ETMVFHRRES SNSGGSRQSA SYIASQEVSG PR
