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   27-MAR-2024, entry version 98.
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.C0LGF4; -.
DR   GlyCosmos; C0LGF4; 3 sites, No reported glycans.
DR   PaxDb; 3702-AT1G31420-1; -.
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   TAIR; AT1G31420; FEI1.
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   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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0099402; P:plant organ development; IEA:UniProt.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
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; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR   PANTHER; PTHR48056:SF77; LRR RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE FEI 1 ISOFORM X1; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; C0LGF4; AT.
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
//