FLZ13_ARATH
ID FLZ13_ARATH Reviewed; 222 AA.
AC Q8GRN0; Q8LCV5; Q9CB02; Q9S7C1; Q9S817;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=FCS-Like Zinc finger 13 {ECO:0000303|PubMed:24901469};
GN Name=FLZ13 {ECO:0000303|PubMed:24901469};
GN Synonyms=DUF581-5 {ECO:0000303|PubMed:24600465};
GN OrderedLocusNames=At1g74940 {ECO:0000312|Araport:AT1G74940};
GN ORFNames=F25A4.9 {ECO:0000312|EMBL:AAD55282.1},
GN F9E10.21 {ECO:0000312|EMBL:AAG51932.1};
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=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=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, INTERACTION WITH KIN10 AND KIN11, SUBCELLULAR LOCATION, AND
RP 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 [6]
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 [7]
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 [8]
RP INDUCTION.
RX PubMed=26442059; DOI=10.3389/fpls.2015.00746;
RA Jamsheer K M., Laxmi A.;
RT "Expression of Arabidopsis FCS-Like Zinc finger genes is differentially
RT regulated by sugars, cellular energy level, and abiotic stress.";
RL Front. Plant Sci. 6:746-746(2015).
RN [9]
RP INTERACTION WITH KIN10; KIN11; KINB1; KINB2; KINB3 AND SNF4.
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:24600465, PubMed:29945970). Interacts with KINB1, KINB2,
CC KINB3 and SNF4 via its N-terminal part (PubMed:29945970).
CC {ECO:0000269|PubMed:24600465, ECO:0000269|PubMed:29945970}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24600465}. Cytoplasm
CC {ECO:0000269|PubMed:24600465}. Note=Shuttles from the cytoplasm to the
CC nucleus when associated with KIN10. {ECO:0000269|PubMed:24600465}.
CC -!- INDUCTION: Down-regulated by NaCl. {ECO:0000269|PubMed:26442059}.
CC -!- SIMILARITY: Belongs to the FLZ family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD55282.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG51932.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC008263; AAD55282.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC013258; AAG51932.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE35653.1; -; Genomic_DNA.
DR EMBL; BT000460; AAN17437.1; -; mRNA.
DR EMBL; BT002550; AAO00910.1; -; mRNA.
DR EMBL; AY086389; AAM64456.1; -; mRNA.
DR PIR; B96779; B96779.
DR PIR; E96778; E96778.
DR RefSeq; NP_565095.1; NM_106152.4.
DR AlphaFoldDB; Q8GRN0; -.
DR IntAct; Q8GRN0; 1.
DR STRING; 3702.AT1G74940.1; -.
DR iPTMnet; Q8GRN0; -.
DR PaxDb; Q8GRN0; -.
DR PRIDE; Q8GRN0; -.
DR ProteomicsDB; 230604; -.
DR EnsemblPlants; AT1G74940.1; AT1G74940.1; AT1G74940.
DR GeneID; 843833; -.
DR Gramene; AT1G74940.1; AT1G74940.1; AT1G74940.
DR KEGG; ath:AT1G74940; -.
DR Araport; AT1G74940; -.
DR TAIR; locus:2027278; AT1G74940.
DR eggNOG; ENOG502RZ1P; Eukaryota.
DR HOGENOM; CLU_103134_0_0_1; -.
DR InParanoid; Q8GRN0; -.
DR OMA; CRDATEF; -.
DR OrthoDB; 1530874at2759; -.
DR PhylomeDB; Q8GRN0; -.
DR PRO; PR:Q8GRN0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GRN0; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR InterPro; IPR044604; FLZ12/13/14.
DR InterPro; IPR007650; Zf-FLZ_dom.
DR PANTHER; PTHR47208; PTHR47208; 1.
DR Pfam; PF04570; zf-FLZ; 1.
DR PROSITE; PS51795; ZF_FLZ; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..222
FT /note="FCS-Like Zinc finger 13"
FT /id="PRO_0000445503"
FT ZN_FING 149..192
FT /note="FLZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01131"
FT CONFLICT 132
FT /note="T -> I (in Ref. 4; AAM64456)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 24969 MW; D76F01C17EA30D48 CRC64;
MILSKRPHLM IRKLSEMLVP RSRSAAIKPE EYTASPRSPL DLNFPSPVHS KRFGSGGVGL
GIVAALEETS NGINRHDPVR YSGRFRCPEI DLSDEEYTYV TSPNGPTKVY YNDDGFELSE
NDYRRVHKPM VTVDEPPVIE RQSVRGPTEF LSSCCLCKKK LQGKDIYMYK GEMGFCSAEC
RSVQIMNDER QEQCKTQVSR NADVLSSPYA AGQRLSAGVF VF
