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FLZ15_ARATH
ID   FLZ15_ARATH             Reviewed;         150 AA.
AC   Q9FH22;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=FCS-Like Zinc finger 15 {ECO:0000303|PubMed:24901469};
GN   Name=FLZ15 {ECO:0000303|PubMed:24901469};
GN   Synonyms=DUF581-17 {ECO:0000303|PubMed:24600465};
GN   OrderedLocusNames=At5g49120 {ECO:0000312|Araport:AT5G49120};
GN   ORFNames=K20J1.9 {ECO:0000312|EMBL:BAB10094.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(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   GENE FAMILY, AND FUNCTION.
RX   PubMed=24600465; DOI=10.3389/fpls.2014.00054;
RA   Nietzsche M., Schiessl I., Boernke F.;
RT   "The complex becomes more complex: protein-protein interactions of SnRK1
RT   with DUF581 family proteins provide a framework for cell- and stimulus
RT   type-specific SnRK1 signaling in plants.";
RL   Front. Plant Sci. 5:54-54(2014).
RN   [4]
RP   ERRATUM OF PUBMED:24600465.
RX   PubMed=25544057; DOI=10.3389/fpls.2014.00693;
RA   Boernke F.;
RT   "Corrigendum: The complex becomes more complex: protein-protein
RT   interactions of SnRK1 with DUF581 family proteins provide a framework for
RT   cell- and stimulus type-specific SnRK1 signaling in plants.";
RL   Front. Plant Sci. 5:693-693(2014).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=24901469; DOI=10.1371/journal.pone.0099074;
RA   Jamsheer K M., Laxmi A.;
RT   "DUF581 is plant specific FCS-like zinc finger involved in protein-protein
RT   interaction.";
RL   PLoS ONE 9:E99074-E99074(2014).
RN   [6]
RP   INTERACTION WITH KIN10; KIN11; KINB1 AND KINB3, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=29945970; DOI=10.1074/jbc.ra118.002073;
RA   Jamsheer K M., Shukla B.N., Jindal S., Gopan N., Mannully C.T., Laxmi A.;
RT   "The FCS-like zinc finger scaffold of the kinase SnRK1 is formed by the
RT   coordinated actions of the FLZ domain and intrinsically disordered
RT   regions.";
RL   J. Biol. Chem. 293:13134-13150(2018).
CC   -!- FUNCTION: May act as an adapter to facilitate the interaction of SnRK1
CC       complex with effector proteins, conferring tissue- and stimulus-type
CC       specific differences in the SnRK1 regulation pathway.
CC       {ECO:0000269|PubMed:24600465}.
CC   -!- SUBUNIT: Interacts with KIN10 and KIN11 via its FLZ-type zinc finger
CC       domain (PubMed:29945970). Interacts with KINB1 and KINB3 via its N-
CC       terminal part (PubMed:29945970). Forms homodimer and heterodimer with
CC       FLZ1, FLZ2 and FLZ7 in vitro (PubMed:29945970).
CC       {ECO:0000269|PubMed:29945970}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:29945970}.
CC   -!- SIMILARITY: Belongs to the FLZ family. {ECO:0000305}.
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DR   EMBL; AB023028; BAB10094.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95773.1; -; Genomic_DNA.
DR   RefSeq; NP_199723.1; NM_124289.4.
DR   AlphaFoldDB; Q9FH22; -.
DR   PaxDb; Q9FH22; -.
DR   PRIDE; Q9FH22; -.
DR   ProteomicsDB; 230629; -.
DR   EnsemblPlants; AT5G49120.1; AT5G49120.1; AT5G49120.
DR   GeneID; 834971; -.
DR   Gramene; AT5G49120.1; AT5G49120.1; AT5G49120.
DR   KEGG; ath:AT5G49120; -.
DR   Araport; AT5G49120; -.
DR   TAIR; locus:2155174; AT5G49120.
DR   eggNOG; ENOG502S3GA; Eukaryota.
DR   HOGENOM; CLU_143767_0_0_1; -.
DR   InParanoid; Q9FH22; -.
DR   OMA; VECRYRQ; -.
DR   OrthoDB; 1576473at2759; -.
DR   PhylomeDB; Q9FH22; -.
DR   PRO; PR:Q9FH22; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FH22; baseline and differential.
DR   GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR007650; Zf-FLZ_dom.
DR   Pfam; PF04570; zf-FLZ; 1.
DR   PROSITE; PS51795; ZF_FLZ; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..150
FT                   /note="FCS-Like Zinc finger 15"
FT                   /id="PRO_0000445505"
FT   ZN_FING         67..111
FT                   /note="FLZ-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01131"
FT   REGION          12..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   150 AA;  17170 MW;  8177D321111B8E4A CRC64;
     MVGLSIVLEM TNNNNNNNNN NNNNNNKNPL SEGVLISPKV VNKANIIVTT AVTTDTTNLR
     RCYQDSGFLE HCFLCRRKLL PAKDIYMYKG DRAFCSVECR SKQMIMDEEE SLRREYCSLM
     DVKKKKFDSP ATAPSRYRRD PRNQAGGFAY
 
 
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