FEI2_ARATH
ID FEI2_ARATH Reviewed; 589 AA.
AC C0LGL9; Q0WLU4; Q9ZQN5;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase FEI 2;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=FEI2; OrderedLocusNames=At2g35620; ORFNames=T20F21.18;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 294-589.
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.
RN [5]
RP FUNCTION, MUTAGENESIS OF LYS-336, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND INTERACTION WITH ACS5 AND ACS9.
RX PubMed=19017745; DOI=10.1105/tpc.108.063354;
RA Xu S.-L., Rahman A., Baskin T.I., Kieber J.J.;
RT "Two leucine-rich repeat receptor kinases mediate signaling, linking cell
RT wall biosynthesis and ACC synthase in Arabidopsis.";
RL Plant Cell 20:3065-3079(2008).
CC -!- FUNCTION: Involved in the signaling pathway that regulates cell wall
CC function, including cellulose biosynthesis, likely via an 1-
CC aminocyclopropane-1-carboxylic acid (ACC)-mediated signal (a precursor
CC of ethylene). {ECO:0000269|PubMed:19017745}.
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 -!- SUBUNIT: Interacts with the ACC synthases ACS5 and ACS9 but not ACS2,
CC via the kinase domain. {ECO:0000269|PubMed:19017745}.
CC -!- INTERACTION:
CC C0LGL9; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-16921113, EBI-20651541;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19017745};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:19017745}.
CC -!- TISSUE SPECIFICITY: Expressed in the root meristem and elongation zone,
CC and in hypocotyls of etiolated seedlings.
CC {ECO:0000269|PubMed:19017745}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Fei1 and fei2 double
CC mutants exhibit disrupted anisotropic expansion (e.g. during hypocotyl
CC elongation), impaired synthesis of cell wall polymers, and abnormal
CC cellulose biosynthesis. {ECO:0000269|PubMed:19017745}.
CC -!- MISCELLANEOUS: 'Fei' means fat in Chinese.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD15451.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006068; AAD15451.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09131.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09132.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61923.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61924.1; -; Genomic_DNA.
DR EMBL; FJ708709; ACN59304.1; -; mRNA.
DR EMBL; AK230094; BAF01913.1; -; mRNA.
DR PIR; H84770; H84770.
DR RefSeq; NP_001189684.1; NM_001202755.2.
DR RefSeq; NP_001324112.1; NM_001336566.1.
DR RefSeq; NP_001324113.1; NM_001336565.1.
DR RefSeq; NP_181105.2; NM_129116.5.
DR AlphaFoldDB; C0LGL9; -.
DR SMR; C0LGL9; -.
DR BioGRID; 3475; 49.
DR IntAct; C0LGL9; 47.
DR STRING; 3702.AT2G35620.1; -.
DR PaxDb; C0LGL9; -.
DR PRIDE; C0LGL9; -.
DR ProteomicsDB; 230774; -.
DR EnsemblPlants; AT2G35620.1; AT2G35620.1; AT2G35620.
DR EnsemblPlants; AT2G35620.2; AT2G35620.2; AT2G35620.
DR EnsemblPlants; AT2G35620.3; AT2G35620.3; AT2G35620.
DR EnsemblPlants; AT2G35620.4; AT2G35620.4; AT2G35620.
DR GeneID; 818130; -.
DR Gramene; AT2G35620.1; AT2G35620.1; AT2G35620.
DR Gramene; AT2G35620.2; AT2G35620.2; AT2G35620.
DR Gramene; AT2G35620.3; AT2G35620.3; AT2G35620.
DR Gramene; AT2G35620.4; AT2G35620.4; AT2G35620.
DR KEGG; ath:AT2G35620; -.
DR Araport; AT2G35620; -.
DR TAIR; locus:2058759; AT2G35620.
DR eggNOG; ENOG502RBVT; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; C0LGL9; -.
DR OMA; ASENRRM; -.
DR OrthoDB; 297889at2759; -.
DR PhylomeDB; C0LGL9; -.
DR PRO; PR:C0LGL9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; C0LGL9; baseline and differential.
DR Genevisible; C0LGL9; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:InterPro.
DR GO; GO:0010192; P:mucilage biosynthetic process; IMP:TAIR.
DR GO; GO:0048354; P:mucilage biosynthetic process involved in seed coat development; IMP:TAIR.
DR GO; GO:0009664; P:plant-type cell wall organization; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR031071; FEI1/2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45974:SF4; PTHR45974:SF4; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 2.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..589
FT /note="LRR receptor-like serine/threonine-protein kinase
FT FEI 2"
FT /id="PRO_0000387512"
FT TOPO_DOM 29..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..589
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 72..96
FT /note="LRR 1"
FT REPEAT 97..120
FT /note="LRR 2"
FT REPEAT 122..144
FT /note="LRR 3"
FT REPEAT 145..168
FT /note="LRR 4"
FT REPEAT 170..193
FT /note="LRR 5"
FT DOMAIN 304..576
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 427
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 310..318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 460
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 461
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 466
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 474
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 336
FT /note="K->R: Normal interaction with ACC synthases."
FT /evidence="ECO:0000269|PubMed:19017745"
SQ SEQUENCE 589 AA; 64355 MW; A3A78CA54E1E1400 CRC64;
MGICLMKRCC SWFLLISFLS ALTNENEAIS PDGEALLSFR NGVLASDGVI GLWRPEDPDP
CNWKGVTCDA KTKRVIALSL TYHKLRGPLP PELGKLDQLR LLMLHNNALY QSIPASLGNC
TALEGIYLQN NYITGTIPSE IGNLSGLKNL DLSNNNLNGA IPASLGQLKR LTKFNVSNNF
LVGKIPSDGL LARLSRDSFN GNRNLCGKQI DIVCNDSGNS TASGSPTGQG GNNPKRLLIS
ASATVGGLLL VALMCFWGCF LYKKLGRVES KSLVIDVGGG ASIVMFHGDL PYASKDIIKK
LESLNEEHII GCGGFGTVYK LSMDDGNVFA LKRIVKLNEG FDRFFERELE ILGSIKHRYL
VNLRGYCNSP TSKLLLYDYL PGGSLDEALH KRGEQLDWDS RVNIIIGAAK GLAYLHHDCS
PRIIHRDIKS SNILLDGNLE ARVSDFGLAK LLEDEESHIT TIVAGTFGYL APEYMQSGRA
TEKTDVYSFG VLVLEVLSGK LPTDASFIEK GFNIVGWLNF LISENRAKEI VDLSCEGVER
ESLDALLSIA TKCVSSSPDE RPTMHRVVQL LESEVMTPCP SDFYDSSSD
