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Y5900_ARATH
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   03-AUG-2022, entry version 132.
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}.
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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.AT5G39000.1; -.
DR   iPTMnet; Q9FID8; -.
DR   PaxDb; Q9FID8; -.
DR   PRIDE; Q9FID8; -.
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; locus:2177202; AT5G39000.
DR   eggNOG; KOG1187; Eukaryota.
DR   HOGENOM; CLU_000288_42_5_1; -.
DR   InParanoid; Q9FID8; -.
DR   OMA; INYMENT; -.
DR   OrthoDB; 684563at2759; -.
DR   PhylomeDB; Q9FID8; -.
DR   PRO; PR:Q9FID8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FID8; baseline and differential.
DR   Genevisible; Q9FID8; 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:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
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:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR   GO; GO:0010038; P:response to metal ion; IGI:TAIR.
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; PTHR27003; PTHR27003; 1.
DR   Pfam; PF12819; Malectin_like; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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
 
 
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