ID Y5900_ARATH Reviewed; 873 AA. AC Q9FID8; DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-NOV-2024, entry version 143. DE RecName: Full=Putative receptor-like protein kinase At5g39000; DE EC=2.7.11.-; DE Flags: Precursor; GN OrderedLocusNames=At5g39000; ORFNames=MXF12.2; 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=10048488; DOI=10.1093/dnares/5.6.379; RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence RT features of the regions of 1,081,958 bp covered by seventeen physically RT assigned P1 and TAC clones."; RL DNA Res. 5:379-391(1998). 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB016892; BAB10824.1; -; Genomic_DNA. DR EMBL; CP002688; AED94385.1; -; Genomic_DNA. DR RefSeq; NP_198716.1; NM_123262.2. DR AlphaFoldDB; Q9FID8; -. DR SMR; Q9FID8; -. DR STRING; 3702.Q9FID8; -. DR iPTMnet; Q9FID8; -. DR PaxDb; 3702-AT5G39000.1; -. DR ProteomicsDB; 242857; -. DR EnsemblPlants; AT5G39000.1; AT5G39000.1; AT5G39000. DR GeneID; 833892; -. DR Gramene; AT5G39000.1; AT5G39000.1; AT5G39000. DR KEGG; ath:AT5G39000; -. DR Araport; AT5G39000; -. DR TAIR; AT5G39000; MDS2. DR eggNOG; KOG1187; Eukaryota. DR HOGENOM; CLU_000288_42_5_1; -. DR InParanoid; Q9FID8; -. DR OMA; INYMENT; -. DR OrthoDB; 1122765at2759; -. DR PhylomeDB; Q9FID8; -. DR PRO; PR:Q9FID8; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q9FID8; baseline and differential. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009536; C:plastid; HDA:TAIR. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR GO; GO:0010038; P:response to metal ion; IGI:TAIR. DR CDD; cd14066; STKc_IRAK; 1. DR FunFam; 2.60.120.430:FF:000003; FERONIA receptor-like kinase; 1. DR FunFam; 2.60.120.430:FF:000007; FERONIA receptor-like kinase; 1. DR FunFam; 1.10.510.10:FF:000252; Receptor-like protein kinase FERONIA; 1. DR FunFam; 3.30.200.20:FF:000645; Receptor-like protein kinase FERONIA; 1. DR Gene3D; 2.60.120.430; Galactose-binding lectin; 2. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR045272; ANXUR1-like. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR024788; Malectin-like_Carb-bd_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR34590; OS03G0124300 PROTEIN-RELATED; 1. DR PANTHER; PTHR34590:SF5; OS04G0586500 PROTEIN; 1. DR Pfam; PF12819; Malectin_like; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Glycoprotein; Kinase; Membrane; Nucleotide-binding; KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..873 FT /note="Putative receptor-like protein kinase At5g39000" FT /id="PRO_0000388798" FT TOPO_DOM 22..445 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 446..466 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 467..873 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 518..803 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 472..494 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 813..843 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 475..494 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 646 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 524..532 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 547 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT CARBOHYD 49 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 64 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 138 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 168 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 216 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 266 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 300 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 437 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 873 AA; 97164 MW; B2879DE5BC7337A7 CRC64; MIRHALLIFS ILVSTPIVGE GATSTYEPTD VFLFNCGDTS NNVDVSGRNW TAENQKILSS NLVNASFTAQ ASYQESGVSQ IPYMTARIFR SEFTYSFPVT PGSNFLRLYF YPTRYGSQFN AVKSFFSVKV NGFTLLNNFS ADLTVKASKP QTEFIIKEFI IPVYQTLNLT FTPSLDSLAF VNGIEIVSIP NRFYSKGGFD DVITNVGSSV DFHIENSTAF ETVYRLNVGG KTVGDSGMFR RWVSDDEIIL SESSGISPIV PDIKINYTEK TPSYVAPDDV YATSRSMGNA DHPEQNLNFN LTWLFTVDAG FSYLVRLHFC ETLSEVNKEG QRVFSIFIEN QTATLEMDVF RMSGGSWIPM YLDYTVIAGS GSGRRHDLRL DLHPLVSINP KYYDAILNGV EILKMNDPDG NLAGPNPDPL VSPDLIPNRA TPRIRKNKSH ILPITLAVVG SLVVLAMFVV GVLVIMKKKK KSKPSTNSSW CPLPHGTDST NTKPAKSLPA DLCRRFSIFE IKSATNDFED KLIIGVGGFG SVYKGQIDGG ATLVAVKRLE ITSNQGAKEF ETELEMLSKL RHVHLVSLIG YCDEDNEMVL VYEYMPHGTL KDHLFRRDKT SDPPLSWKRR LEICIGAARG LQYLHTGAKY TIIHRDIKTT NILLDENFVT KVSDFGLSRV GPTSASQTHV STVVKGTFGY LDPEYYRRQV LTEKSDVYSF GVVLLEVLCC RPIRMQSVPP EQADLIRWVK SNYRRGTVDQ IIDSDLSADI TSTSLEKFCE IAVRCVQDRG MERPPMNDVV WALEFALQLH ETAKKKNDNV ESLDLMPSGE VGTTTDGEDD LFSRTTGHVG KSTTTDDSVL VVGDERSGSS WGVFSEINEP KAR //