Y5389_ARATH
ID Y5389_ARATH Reviewed; 880 AA.
AC Q9FID9; Q8RWQ0;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable receptor-like protein kinase At5g38990;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN OrderedLocusNames=At5g38990; ORFNames=K15E6.170;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY.
RX PubMed=19529822; DOI=10.1093/mp/ssn083;
RA Chae L., Sudat S., Dudoit S., Zhu T., Luan S.;
RT "Diverse transcriptional programs associated with environmental stress and
RT hormones in the Arabidopsis receptor-like kinase gene family.";
RL Mol. Plant 2:84-107(2009).
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; BAB10823.1; -; Genomic_DNA.
DR EMBL; AB009048; BAB10823.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED94384.1; -; Genomic_DNA.
DR EMBL; AY091785; AAM10331.1; -; mRNA.
DR EMBL; BT000634; AAN18200.1; -; mRNA.
DR RefSeq; NP_198715.1; NM_123261.4.
DR AlphaFoldDB; Q9FID9; -.
DR SMR; Q9FID9; -.
DR BioGRID; 19142; 15.
DR IntAct; Q9FID9; 15.
DR STRING; 3702.AT5G38990.1; -.
DR iPTMnet; Q9FID9; -.
DR PaxDb; Q9FID9; -.
DR PRIDE; Q9FID9; -.
DR ProteomicsDB; 243109; -.
DR EnsemblPlants; AT5G38990.1; AT5G38990.1; AT5G38990.
DR GeneID; 833891; -.
DR Gramene; AT5G38990.1; AT5G38990.1; AT5G38990.
DR KEGG; ath:AT5G38990; -.
DR Araport; AT5G38990; -.
DR TAIR; locus:2152312; AT5G38990.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_42_5_1; -.
DR InParanoid; Q9FID9; -.
DR OMA; FINSQMA; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9FID9; -.
DR PRO; PR:Q9FID9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FID9; baseline and differential.
DR Genevisible; Q9FID9; 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 2: Evidence at transcript level;
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..880
FT /note="Probable receptor-like protein kinase At5g38990"
FT /id="PRO_0000386560"
FT TOPO_DOM 22..440
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..880
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 525..810
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 471..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 653
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 531..539
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 602
FT /note="M -> L (in Ref. 4; AAM10331/AAN18200)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 880 AA; 97953 MW; 1D44A69588B436B0 CRC64;
MICHVLVIFT ILVSAVVDAT ASYEPTDVFL INCGDTSNNM DYSGRNWTTE NPKFMSSNAV
DDASFTSSAS YQESGIPQVP YLKARIFRYD FTYSFPVSPG WKFLRLYFYP TRYGSDFDAV
KSFFSVNVNR FTLLHNFSVK ASIPESSSLI KEFIVPVNQT LDLTFTPSPN SLAFVNGIEI
ISMPDRFYSK GGFDDVVRNV GRDVDFEIDN STAFETVYRV NVGGKVVGDV GDSGMFRRWL
SDEGFLLGIN SGAIPNITGV KINYTDKTPA YVAPEDVYTT CRLMGNKDSP ELNLNFNLTW
LFEVDAGFAY IVRLHFCETQ PEVNKTGDRV FSIFFGYQLA MREMDVFRLS GGFRLPMYLD
FKVLVDADGT SQRPSLRVDL TPYKEDYPTY YDAILSGVEI LKLSNSDGNL AGLNPIPQLS
PPPQSITPLK GKGKSSHVLP IIIAVVGSAV ALAFFVLVVV LVVMKRKKKS NESSVDTTNK
PSTNSSWGPL LHGTGSTNTK SASSLPSDLC RRFSIYEIKS ATNDFEEKLI IGVGGFGSVY
KGRIDGGATL VAVKRLEITS NQGAKEFDTE LEMLSKLRHV HLVSLIGYCD DDNEMVLVYE
YMPHGTLKDH LFRRDKASDP PLSWKRRLEI CIGAARGLQY LHTGAKYTII HRDIKTTNIL
LDENFVAKVS DFGLSRVGPT SASQTHVSTV VKGTFGYLDP EYYRRQILTE KSDVYSFGVV
LLEVLCCRPI RMQSVPPEQA DLIRWVKSNF NKRTVDQIID SDLTADITST SMEKFCEIAI
RCVQDRGMER PPMNDVVWAL EFALQLHETA KKKNDNVESL DLMPSGEVGT TTDGEDDLFS
RTTGHVGKST TTDDSVLVVG DERSGSSWGV FSEINEPKAR
