Y2685_ARATH
ID Y2685_ARATH Reviewed; 633 AA.
AC Q8S8N4;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probably inactive receptor-like protein kinase At2g46850;
DE Flags: Precursor;
GN OrderedLocusNames=At2g46850; ORFNames=F19D11.13;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. Lacks the conserved Asp active site at position 476, which is
CC replaced by an Asn residue.
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; AC005310; AAM15020.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10763.1; -; Genomic_DNA.
DR PIR; T02686; T02686.
DR RefSeq; NP_182208.1; NM_130252.3.
DR AlphaFoldDB; Q8S8N4; -.
DR SMR; Q8S8N4; -.
DR STRING; 3702.AT2G46850.1; -.
DR PaxDb; Q8S8N4; -.
DR PRIDE; Q8S8N4; -.
DR ProteomicsDB; 232471; -.
DR EnsemblPlants; AT2G46850.1; AT2G46850.1; AT2G46850.
DR GeneID; 819298; -.
DR Gramene; AT2G46850.1; AT2G46850.1; AT2G46850.
DR KEGG; ath:AT2G46850; -.
DR Araport; AT2G46850; -.
DR TAIR; locus:2044365; AT2G46850.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_43_5_1; -.
DR InParanoid; Q8S8N4; -.
DR OMA; WVKNRSA; -.
DR OrthoDB; 287298at2759; -.
DR PhylomeDB; Q8S8N4; -.
DR PRO; PR:Q8S8N4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S8N4; baseline and differential.
DR Genevisible; Q8S8N4; 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:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR045274; WAK-like.
DR InterPro; IPR025287; WAK_GUB.
DR PANTHER; PTHR27005; PTHR27005; 1.
DR Pfam; PF13947; GUB_WAK_bind; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..633
FT /note="Probably inactive receptor-like protein kinase
FT At2g46850"
FT /id="PRO_0000389475"
FT TOPO_DOM 29..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..633
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 355..633
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 361..369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 384
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 633 AA; 70166 MW; DB7C35AE9FC6BFD7 CRC64;
MPPLFLPSSS SALFLLLLLL LTLQTLTSIS LSQPQALRSP EKCGNFSVSF PFQLSSSSSA
AAFRLSCENS STLFLHINHQ SYRIIEFFTD GLLVDFPSSP SCRQFNDLRS FPFSANQFFS
ISFENVIGLY DCEDSSLCKF GCETNDLFGC DGREEDETSG GDIGCCYPLS DHSAWRVGDD
FSVFSRYGCR GFSSWLVPRG TNRGKRGVKL EWAIPRNSPE AICDREARTV NATAIEGSVR
CVCRDGFVGD GFLHGTGCLK SCFKDGKELY GDKCKIKKHN GKKLTVLAGV LAPLFILGSL
LALFCLLKRP VTSHKDQQFD ISTTTTTTNS VSFRKGYNKT RLFTYRELEE ATKGFQDSQK
LTQGKTGTIY SGNLTNGTRV IVHKVLCENQ IEFMEISSQI DHLSAVLHRN LARIIGFCMD
IGYNPLVVYE YPVNGSLGDR LRLGLDWCKR VNIVAEVAGL LALLQYENYP PILHTNISSG
NIFLDEDFQA KVTGFGLQRK QRIDTSMYDF AVLLLEIVTG LKQREETVTQ ALQKIRSGKL
EEIVDPSMYF HEQPVAFREQ IGLVADIATR CVLFGGDGKF GMVDAARELL QIAGNNGGGG
CDKKRDGIEE TFSNSSLLQM ISMSPDSIYL PKT
