C3H46_ARATH
ID C3H46_ARATH Reviewed; 540 AA.
AC Q9SV09; A0A1I9LPV9; Q8L9E0; Q8RXK0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Zinc finger CCCH domain-containing protein 46;
DE Short=AtC3H46;
DE EC=3.1.-.-;
GN OrderedLocusNames=At3g51950; ORFNames=F4F15.60;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
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 [6]
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 [7]
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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: Possesses RNA-binding and ribonuclease activities in vitro.
CC {ECO:0000269|PubMed:18582464}.
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DR EMBL; AL049711; CAB41315.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78866.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78867.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64616.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64617.1; -; Genomic_DNA.
DR EMBL; AY080846; AAL87320.1; -; mRNA.
DR EMBL; AY150500; AAN13016.1; -; mRNA.
DR EMBL; AK316715; BAH19442.1; -; mRNA.
DR EMBL; AY088484; AAM66020.1; -; mRNA.
DR PIR; T49074; T49074.
DR RefSeq; NP_001030840.1; NM_001035763.2.
DR RefSeq; NP_001326632.1; NM_001339542.1.
DR RefSeq; NP_001326633.1; NM_001339541.1.
DR RefSeq; NP_190763.1; NM_115054.4.
DR AlphaFoldDB; Q9SV09; -.
DR SMR; Q9SV09; -.
DR BioGRID; 9676; 3.
DR IntAct; Q9SV09; 2.
DR STRING; 3702.AT3G51950.2; -.
DR iPTMnet; Q9SV09; -.
DR PaxDb; Q9SV09; -.
DR PRIDE; Q9SV09; -.
DR ProteomicsDB; 240526; -.
DR EnsemblPlants; AT3G51950.1; AT3G51950.1; AT3G51950.
DR EnsemblPlants; AT3G51950.2; AT3G51950.2; AT3G51950.
DR EnsemblPlants; AT3G51950.3; AT3G51950.3; AT3G51950.
DR EnsemblPlants; AT3G51950.4; AT3G51950.4; AT3G51950.
DR GeneID; 824358; -.
DR Gramene; AT3G51950.1; AT3G51950.1; AT3G51950.
DR Gramene; AT3G51950.2; AT3G51950.2; AT3G51950.
DR Gramene; AT3G51950.3; AT3G51950.3; AT3G51950.
DR Gramene; AT3G51950.4; AT3G51950.4; AT3G51950.
DR KEGG; ath:AT3G51950; -.
DR Araport; AT3G51950; -.
DR TAIR; locus:2083740; AT3G51950.
DR eggNOG; ENOG502QWIK; Eukaryota.
DR HOGENOM; CLU_028778_0_0_1; -.
DR InParanoid; Q9SV09; -.
DR OMA; SCKFMHG; -.
DR OrthoDB; 394732at2759; -.
DR PhylomeDB; Q9SV09; -.
DR PRO; PR:Q9SV09; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SV09; baseline and differential.
DR Genevisible; Q9SV09; AT.
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; HDA:TAIR.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR CDD; cd12458; RRM_AtC3H46_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034365; AtC3H46-like_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Hydrolase; Metal-binding; Nuclease; Phosphoprotein;
KW Reference proteome; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..540
FT /note="Zinc finger CCCH domain-containing protein 46"
FT /id="PRO_0000372000"
FT DOMAIN 258..334
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 148..175
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 337..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT CONFLICT 187
FT /note="E -> D (in Ref. 5; AAM66020)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="T -> P (in Ref. 5; AAM66020)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="E -> V (in Ref. 3; AAL87320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 59789 MW; BE5C91248F985DF0 CRC64;
MDGYEATRIV LSRIQSLDPE NASKIMGLLL LQDHGEKEMI RLAFGPETLV HSVIVKAKKE
LGLMNCSRSP WSHQDELISP KNNRGSSLNP ASLPFYANGG RSSRDLTNDF ELMDDMNSRS
TDFLGSVHAR SGSCVLDGLG YGGDSDLGFG GVPCSYFARG FCKNGASCRF VHSDGGADLV
GSPSRIELLR SNSVPPRLAH HFMTRSSLPS FSTKGVNLQQ NDVQRAAAAL MIGDELQKLG
RWRPERIDLS AMACPASRQI YLTFPADSRF REEDVSNYFS TFGPVQDVRI PYQQKRMFGF
VTFVYPETVK SILAKGNPHF VCDSRVLVKP YKEKGKVPDK YRTNQTTERE LSPTGLDSSP
RDVLGGRGFY NNTQDVLWRS KFEEEILELQ SRRLMNLQLL DVKKHFQLNS PTNIHSPNPF
SQSLISPRPL SVIKREYDGG EKGKGSSKEG SDDDTMNLPE RLEDSLPDSP FASPAHHLLL
FADSADNNGS DLWSPSSDND DNSTPSTLSD SFNSFNYQMP RLPAIGMLPG RGGPTCRVGI
