C3H2_ARATH
ID C3H2_ARATH Reviewed; 393 AA.
AC Q9ZWA1; Q8GZ44;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Zinc finger CCCH domain-containing protein 2 {ECO:0000303|PubMed:18221561};
DE Short=AtC3H2 {ECO:0000303|PubMed:18221561};
DE AltName: Full=Protein SOMNUS {ECO:0000303|PubMed:18487351};
DE Short=SOM {ECO:0000303|PubMed:18487351};
DE AltName: Full=Tandem CCCH Zinc Finger protein 4 {ECO:0000303|PubMed:26978070};
DE Short=AtTZF4 {ECO:0000303|PubMed:26978070};
GN Name=TZF4 {ECO:0000303|PubMed:26978070};
GN Synonyms=SOM {ECO:0000303|PubMed:18487351};
GN OrderedLocusNames=At1g03790 {ECO:0000312|Araport:AT1G03790};
GN ORFNames=F11M21.28 {ECO:0000312|EMBL:AAD10689.1};
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18487351; DOI=10.1105/tpc.108.058859;
RA Kim D.H., Yamaguchi S., Lim S., Oh E., Park J., Hanada A., Kamiya Y.,
RA Choi G.;
RT "SOMNUS, a CCCH-type zinc finger protein in Arabidopsis, negatively
RT regulates light-dependent seed germination downstream of PIL5.";
RL Plant Cell 20:1260-1277(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=22483719; DOI=10.1016/j.devcel.2012.01.024;
RA Cho J.-N., Ryu J.-Y., Jeong Y.-M., Park J., Song J.-J., Amasino R.M.,
RA Noh B., Noh Y.-S.;
RT "Control of seed germination by light-induced histone arginine
RT demethylation activity.";
RL Dev. Cell 22:736-748(2012).
RN [8]
RP INTERACTION WITH MARD1 AND RD21A.
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 -!- FUNCTION: Probable transcription repressor that functions as negative
CC regulator of phytochrome-mediated promotion of seed germination.
CC Inhibits seed germination by regulating the expression of gibberellic
CC acid (GA) and abscisic acid (ABA) metabolic genes. Does not regulate
CC the expression of the DELLA genes RGA and RGA1. Activated by PIL5, a
CC phytochrome-interacting basic helix-loop-helix transcription factor
CC (PubMed:18487351). Represses directly JMJ20 and JMJ22 expression in the
CC absence of red light (R) and in far-red (FR) conditions
CC (PubMed:22483719). {ECO:0000269|PubMed:18487351,
CC ECO:0000269|PubMed:22483719}.
CC -!- SUBUNIT: Interacts with MARD1/FLZ9 and RD21A.
CC {ECO:0000269|PubMed:26978070}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18487351}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in seeds.
CC {ECO:0000269|PubMed:18487351}.
CC -!- DISRUPTION PHENOTYPE: Increased levels of JMJ20 and JMJ22 in far-red
CC (FR) conditions. {ECO:0000269|PubMed:22483719}.
CC -!- MISCELLANEOUS: Plants lacking SOM germinate in darkness, independently
CC of various light regimens.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC003027; AAD10689.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27614.1; -; Genomic_DNA.
DR EMBL; AK117219; BAC41895.1; -; mRNA.
DR EMBL; BT005342; AAO63406.1; -; mRNA.
DR PIR; D86168; D86168.
DR RefSeq; NP_171875.1; NM_100258.3.
DR AlphaFoldDB; Q9ZWA1; -.
DR BioGRID; 24643; 7.
DR IntAct; Q9ZWA1; 7.
DR STRING; 3702.AT1G03790.1; -.
DR PaxDb; Q9ZWA1; -.
DR PRIDE; Q9ZWA1; -.
DR ProteomicsDB; 240447; -.
DR EnsemblPlants; AT1G03790.1; AT1G03790.1; AT1G03790.
DR GeneID; 839408; -.
DR Gramene; AT1G03790.1; AT1G03790.1; AT1G03790.
DR KEGG; ath:AT1G03790; -.
DR Araport; AT1G03790; -.
DR TAIR; locus:2024112; AT1G03790.
DR eggNOG; KOG1595; Eukaryota.
DR HOGENOM; CLU_044407_3_0_1; -.
DR InParanoid; Q9ZWA1; -.
DR OMA; SDPDLGW; -.
DR OrthoDB; 937629at2759; -.
DR PhylomeDB; Q9ZWA1; -.
DR PRO; PR:Q9ZWA1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZWA1; baseline and differential.
DR Genevisible; Q9ZWA1; AT.
DR GO; GO:0005634; C:nucleus; 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 GO; GO:0010187; P:negative regulation of seed germination; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
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 DNA-binding; Germination; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..393
FT /note="Zinc finger CCCH domain-containing protein 2"
FT /id="PRO_0000371964"
FT ZN_FING 122..150
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 159..181
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 360
FT /note="M -> I (in Ref. 3; BAC41895 and 4; AAO63406)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 43614 MW; 4DF703696ED090B4 CRC64;
MDVVCTEHQM RKPTVEIPPR KLLLSSKSFP SDSSSPRSPR KHNWNKSNKI TSEHEEDNED
NNRENKEYCY DSDSDDPYAS DHFRMFEFKI RRCTRSRSHD WTDCPFAHPG EKARRRDPRR
FQYSGEVCPE FRRGGDCSRG DDCEFAHGVF ECWLHPIRYR TEACKDGKHC KRKVCFFAHS
PRQLRVLPPE NVSGVSASPS PAAKNPCCLF CSSSPTSTLL GNLSHLSRSP SLSPPMSPAN
KAAAFSRLRN RAASAVSAAA AAGSMNYKDV LSELVNSLDS MSLAEALQAS SSSPVTTPVS
AAAAAFASSC GLSNQRLHLQ QQQPSSPLQF ALSPSTPSYL TNSPQANFFS DDFTPRRRQM
NDFTAMTAVR ENTNIEDGSC GDPDLGWVND LLT
