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Database: UniProt
Entry: B9RNT4_RICCO
LinkDB: B9RNT4_RICCO
Original site: B9RNT4_RICCO 
ID   B9RNT4_RICCO            Unreviewed;       984 AA.
AC   B9RNT4;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Serine/threonine-protein kinase bri1, putative {ECO:0000313|EMBL:EEF46852.1};
DE            EC=1.3.1.74 {ECO:0000313|EMBL:EEF46852.1};
GN   ORFNames=RCOM_0920670 {ECO:0000313|EMBL:EEF46852.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC   -!- SIMILARITY: Belongs to the RLP family. {ECO:0000256|ARBA:ARBA00009592}.
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DR   EMBL; EQ973791; EEF46852.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9RNT4; -.
DR   STRING; 3988.B9RNT4; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   InParanoid; B9RNT4; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
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; IPR046956; RLP23-like.
DR   PANTHER; PTHR48061; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE EMS1-LIKE-RELATED; 1.
DR   PANTHER; PTHR48061:SF12; VOC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 6.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SUPFAM; SSF52058; L domain-like; 3.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:EEF46852.1};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000313|EMBL:EEF46852.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:EEF46852.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..984
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002890904"
FT   TRANSMEM        932..955
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..76
FT                   /note="Leucine-rich repeat-containing N-terminal plant-
FT                   type"
FT                   /evidence="ECO:0000259|Pfam:PF08263"
SQ   SEQUENCE   984 AA;  109486 MW;  99F6C78918E43F51 CRC64;
     MAPSLHLLSF LLLLIHSIGC CYSSSICHDD ERSALWQFKE SLVVDNFACD PSAKLSSWSL
     QGDMNNCCSW GGIECNNNTG HVIALDLSSS CLYGSINSSS TIFRLIYLTS LNLADNNFNA
     STIPSEIRTL SSLTYLNLSL SNFSNQIPIQ VLELSKLVSL DLSDNPLKLQ NPSLKDLVEK
     LAHLSQLHLN GVTISSEVPQ SLANLSFLSS LLLRDCKLQG EFPVKIFQLP NLRILIVRLN
     PDLTGYLPEF QVGSSLEALW LEGTNFSGQL PHSIGNLKLL SSFVAGSCRF GGPIPPSIGD
     LGNLNFLDLS YNNFSGKIPS SFGNLLQLTY LSLSFNNFSP GTLYWLGNLT NLYFLNLAQT
     NSHGNIPSSV GNMTKLIYLR LYSNKLTGQV PSWLGNLTAL LELQLAANEL QGPIPESIFE
     LPSLQVLELH SNNLSGTLKF DLFLKSKNLV SLQLSDNHLS LISSPPINIT VHRFKTLGLN
     SCNLSEFPFF LRGENDDLEH LDLSQNEIQG LIPDWITDLG TESLIILNLA SNFLTGFERP
     FNVLPWKNLH VLNLSANNLE GPLPIPPPSI SIYIISQNSL TGEISPMFCN LTSVLTLDLS
     RNNLSGSLPR CLGNFSNFVL VMDLRSNNFS GTIPDRFESE CKVRMMDFSH NKLEGKLPRS
     LANCTKLEML NLGNNQIYDV FPSWAGLLPQ LRVLILRSNR LVGVVGKPET NFDFPQLQII
     DLSDNTFTGE LPFEYFQKWT AMKSIDQDQL KYIEVDISFQ VLDYSWSNHF SYSITITNKG
     RETTYERILK FFAVINFSSN RFEGRIPEVI GNLREVQLLN LSNNILTGQI PPSLGSMKEL
     EALDLSRNQL SGEIPMKLAQ LSFLAFFNVS DNNLTGPVPR GNQFDTFENN SFDANPGLCG
     NPLSKKCGFS EASTLAPSNF EQDQGSEFPL EFGWKVVLFG YASGLVIGVV IGCILDTEKN
     EWLVNTFANW QLKVRRTLCE IWRT
//
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