C3H3_ARATH
ID C3H3_ARATH Reviewed; 404 AA.
AC Q94AD9; Q9MAU8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Zinc finger CCCH domain-containing protein 3;
DE Short=AtC3H3;
DE EC=3.1.-.-;
DE AltName: Full=Zinc finger CCCH domain-containing protein ZFN-like 4;
GN OrderedLocusNames=At1g04990; ORFNames=F13M7.1;
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 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 FUNCTION.
RX PubMed=18582464; DOI=10.1016/j.febslet.2008.06.029;
RA Addepalli B., Hunt A.G.;
RT "Ribonuclease activity is a common property of Arabidopsis CCCH-containing
RT zinc-finger proteins.";
RL FEBS Lett. 582:2577-2582(2008).
CC -!- FUNCTION: Possesses RNA-binding and ribonuclease activities in vitro.
CC {ECO:0000269|PubMed:18582464}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF40461.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004809; AAF40461.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27775.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27776.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60931.1; -; Genomic_DNA.
DR EMBL; AY048253; AAK82515.1; -; mRNA.
DR EMBL; AY113065; AAM47373.1; -; mRNA.
DR PIR; F86183; F86183.
DR RefSeq; NP_001318923.1; NM_001331509.1.
DR RefSeq; NP_563725.1; NM_100378.5.
DR RefSeq; NP_973759.1; NM_202030.2.
DR AlphaFoldDB; Q94AD9; -.
DR BioGRID; 24586; 8.
DR IntAct; Q94AD9; 5.
DR STRING; 3702.AT1G04990.1; -.
DR iPTMnet; Q94AD9; -.
DR PaxDb; Q94AD9; -.
DR PRIDE; Q94AD9; -.
DR ProteomicsDB; 240493; -.
DR EnsemblPlants; AT1G04990.1; AT1G04990.1; AT1G04990.
DR EnsemblPlants; AT1G04990.2; AT1G04990.2; AT1G04990.
DR EnsemblPlants; AT1G04990.6; AT1G04990.6; AT1G04990.
DR GeneID; 839351; -.
DR Gramene; AT1G04990.1; AT1G04990.1; AT1G04990.
DR Gramene; AT1G04990.2; AT1G04990.2; AT1G04990.
DR Gramene; AT1G04990.6; AT1G04990.6; AT1G04990.
DR KEGG; ath:AT1G04990; -.
DR Araport; AT1G04990; -.
DR TAIR; locus:2010562; AT1G04990.
DR eggNOG; KOG1677; Eukaryota.
DR HOGENOM; CLU_033292_2_0_1; -.
DR InParanoid; Q94AD9; -.
DR OMA; WATYMGA; -.
DR OrthoDB; 544409at2759; -.
DR PhylomeDB; Q94AD9; -.
DR PRO; PR:Q94AD9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94AD9; baseline and differential.
DR Genevisible; Q94AD9; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF00642; zf-CCCH; 5.
DR SMART; SM00356; ZnF_C3H1; 5.
DR SUPFAM; SSF90229; SSF90229; 5.
DR PROSITE; PS50103; ZF_C3H1; 5.
PE 2: Evidence at transcript level;
KW DNA-binding; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..404
FT /note="Zinc finger CCCH domain-containing protein 3"
FT /id="PRO_0000213918"
FT ZN_FING 47..75
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 90..118
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 135..163
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 261..289
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 307..335
FT /note="C3H1-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 350..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 404 AA; 44704 MW; 7589B71A89B995F3 CRC64;
MRTPMSDTQH VQSSLVSIRS SDKIEDAFRK MKVNETGVEE LNPYPDRPGE RDCQFYLRTG
LCGYGSSCRY NHPTHLPQDV AYYKEELPER IGQPDCEYFL KTGACKYGPT CKYHHPKDRN
GAQPVMFNVI GLPMRLGEKP CPYYLRTGTC RFGVACKFHH PQPDNGHSTA YGMSSFPAAD
LRYASGLTMM STYGTLPRPQ VPQSYVPILV SPSQGFLPPQ GWAPYMAASN SMYNVKNQPY
YSGSSASMAM AVALNRGLSE SSDQPECRFF MNTGTCKYGD DCKYSHPGVR ISQPPPSLIN
PFVLPARPGQ PACGNFRSYG FCKFGPNCKF DHPMLPYPGL TMATSLPTPF ASPVTTHQRI
SPTPNRSDSK SLSNGKPDVK KESSETEKPD NGEVQDLSED ASSP
