C3H61_ARATH
ID C3H61_ARATH Reviewed; 381 AA.
AC Q9FKW2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Zinc finger CCCH domain-containing protein 61;
DE Short=AtC3H61;
DE AltName: Full=Tandem CCCH Zinc Finger protein 5 {ECO:0000303|PubMed:26978070};
DE Short=AtTZF5 {ECO:0000303|PubMed:26978070};
GN Name=TZF5 {ECO:0000303|PubMed:26978070};
GN OrderedLocusNames=At5g44260 {ECO:0000312|Araport:AT5G44260};
GN ORFNames=K9L2.1 {ECO:0000312|EMBL:BAB10111.1};
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 NOMENCLATURE.
RX PubMed=18221561; DOI=10.1186/1471-2164-9-44;
RA Wang D., Guo Y., Wu C., Yang G., Li Y., Zheng C.;
RT "Genome-wide analysis of CCCH zinc finger family in Arabidopsis and rice.";
RL BMC Genomics 9:44-44(2008).
RN [5]
RP INTERACTION WITH MARD1 AND RD21A, AND SUBCELLULAR LOCATION.
RX PubMed=26978070; DOI=10.1371/journal.pone.0151574;
RA Bogamuwa S., Jang J.C.;
RT "Plant tandem CCCH zinc finger proteins interact with ABA, drought, and
RT stress response regulators in processing-bodies and stress granules.";
RL PLoS ONE 11:E0151574-E0151574(2016).
CC -!- SUBUNIT: Interacts with MARD1/FLZ9 and RD21A via its CCCH zing finger
CC domains. {ECO:0000269|PubMed:26978070}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:26978070}. Cytoplasm, P-body
CC {ECO:0000269|PubMed:26978070}.
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DR EMBL; AB011475; BAB10111.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95082.1; -; Genomic_DNA.
DR EMBL; AY034916; AAK59423.1; -; mRNA.
DR EMBL; AY142542; AAN13124.1; -; mRNA.
DR RefSeq; NP_199239.1; NM_123793.3.
DR AlphaFoldDB; Q9FKW2; -.
DR BioGRID; 19699; 10.
DR IntAct; Q9FKW2; 10.
DR STRING; 3702.AT5G44260.1; -.
DR iPTMnet; Q9FKW2; -.
DR PaxDb; Q9FKW2; -.
DR PRIDE; Q9FKW2; -.
DR ProteomicsDB; 240489; -.
DR EnsemblPlants; AT5G44260.1; AT5G44260.1; AT5G44260.
DR GeneID; 834449; -.
DR Gramene; AT5G44260.1; AT5G44260.1; AT5G44260.
DR KEGG; ath:AT5G44260; -.
DR Araport; AT5G44260; -.
DR TAIR; locus:2158685; AT5G44260.
DR eggNOG; KOG1595; Eukaryota.
DR HOGENOM; CLU_044407_3_0_1; -.
DR InParanoid; Q9FKW2; -.
DR OMA; EVCPEFS; -.
DR OrthoDB; 937629at2759; -.
DR PhylomeDB; Q9FKW2; -.
DR PRO; PR:Q9FKW2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKW2; baseline and differential.
DR Genevisible; Q9FKW2; AT.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:TAIR.
DR GO; GO:0000932; C:P-body; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR045234; Unkempt-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR14493; PTHR14493; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..381
FT /note="Zinc finger CCCH domain-containing protein 61"
FT /id="PRO_0000372011"
FT ZN_FING 101..128
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 137..159
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 381 AA; 42058 MW; 3B30AEC755CD3FAF CRC64;
MDVEHHKSGH ISRPTVDIPP RKLLSSAKSP SSVSSPLRDY KEQKDYCYDS DSEDPYAGDH
FRMYEFKIRR CTRSRSHDWT DCPFSHPGEK ARRRDPRRFH YTGEVCPEFS RHGDCSRGDE
CGFAHGVFEC WLHPSRYRTE ACKDGKHCKR KVCFFAHSPR QLRVLPPSPE NHISGGCGGS
PSSSPASVLS NKNNRCCLFC SHSPTSTLLN LSRSPSSSPP LSPADKADAF SRLSRRRTAV
LNELISSLDS LSLTEALAAS SSSPVTMPIS TATMIASSNL SSNHHHHRLP PWLDVGDRDL
QLQQSSPLRF ALSPSSTPSY LHGQLQPPPS SFFGDEFTPR GGRLSDFSVA AAAAAQARDK
NSFEVGSSGD LDLGWVNDLL T