FEI1_ARATH
ID FEI1_ARATH Reviewed; 591 AA.
AC C0LGF4; Q9C867;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase FEI 1;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=FEI1; OrderedLocusNames=At1g31420; ORFNames=T8E3.2;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 FUNCTION, MUTAGENESIS OF LYS-334, 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 C0LGF4; Q9SHI2: At1g17230; NbExp=2; IntAct=EBI-16896366, EBI-20651261;
CC C0LGF4; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-16896366, EBI-20651541;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19017745};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:19017745}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=C0LGF4-1; Sequence=Displayed;
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.
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=AAG51266.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC027135; AAG51266.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE31354.1; -; Genomic_DNA.
DR EMBL; FJ708643; ACN59239.1; -; mRNA.
DR PIR; B86440; B86440.
DR RefSeq; NP_001185122.1; NM_001198193.1. [C0LGF4-1]
DR AlphaFoldDB; C0LGF4; -.
DR SMR; C0LGF4; -.
DR BioGRID; 25267; 66.
DR IntAct; C0LGF4; 60.
DR STRING; 3702.AT1G31420.1; -.
DR PaxDb; C0LGF4; -.
DR PRIDE; C0LGF4; -.
DR ProteomicsDB; 231006; -. [C0LGF4-1]
DR EnsemblPlants; AT1G31420.2; AT1G31420.2; AT1G31420. [C0LGF4-1]
DR GeneID; 840032; -.
DR Gramene; AT1G31420.2; AT1G31420.2; AT1G31420. [C0LGF4-1]
DR KEGG; ath:AT1G31420; -.
DR Araport; AT1G31420; -.
DR eggNOG; ENOG502RBVT; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; C0LGF4; -.
DR PhylomeDB; C0LGF4; -.
DR PRO; PR:C0LGF4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0LGF4; baseline and differential.
DR Genevisible; C0LGF4; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR031071; FEI1/2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..591
FT /note="LRR receptor-like serine/threonine-protein kinase
FT FEI 1"
FT /id="PRO_0000387511"
FT TOPO_DOM 30..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..591
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 73..97
FT /note="LRR 1"
FT REPEAT 98..121
FT /note="LRR 2"
FT REPEAT 123..145
FT /note="LRR 3"
FT REPEAT 146..169
FT /note="LRR 4"
FT REPEAT 171..194
FT /note="LRR 5"
FT DOMAIN 306..578
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 429
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 312..320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 462
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 468
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 476
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 334
FT /note="K->R: Loss of kinase activity, normal interaction
FT with ACC synthases."
FT /evidence="ECO:0000269|PubMed:19017745"
SQ SEQUENCE 591 AA; 64916 MW; EA57944B55157D91 CRC64;
MMGICEMKSC CSWLLLISLL CSLSNESQAI SPDGEALLSF RNAVTRSDSF IHQWRPEDPD
PCNWNGVTCD AKTKRVITLN LTYHKIMGPL PPDIGKLDHL RLLMLHNNAL YGAIPTALGN
CTALEEIHLQ SNYFTGPIPA EMGDLPGLQK LDMSSNTLSG PIPASLGQLK KLSNFNVSNN
FLVGQIPSDG VLSGFSKNSF IGNLNLCGKH VDVVCQDDSG NPSSHSQSGQ NQKKNSGKLL
ISASATVGAL LLVALMCFWG CFLYKKLGKV EIKSLAKDVG GGASIVMFHG DLPYSSKDII
KKLEMLNEEH IIGCGGFGTV YKLAMDDGKV FALKRILKLN EGFDRFFERE LEILGSIKHR
YLVNLRGYCN SPTSKLLLYD YLPGGSLDEA LHERGEQLDW DSRVNIIIGA AKGLSYLHHD
CSPRIIHRDI KSSNILLDGN LEARVSDFGL AKLLEDEESH ITTIVAGTFG YLAPEYMQSG
RATEKTDVYS FGVLVLEVLS GKRPTDASFI EKGLNVVGWL KFLISEKRPR DIVDPNCEGM
QMESLDALLS IATQCVSPSP EERPTMHRVV QLLESEVMTP CPSEFYDSSS D
