C3H7_ARATH
ID C3H7_ARATH Reviewed; 470 AA.
AC Q3ED78; F4HY24; Q0WQL3; Q9LPK3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Zinc finger CCCH domain-containing protein 7;
DE Short=AtC3H7;
DE EC=3.1.-.-;
DE AltName: Full=AtSmicl;
GN OrderedLocusNames=At1g21570; ORFNames=F24J8.21;
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;
RA Kim C.J., Bautista V.R., Chen H., De Los Reyes C., Wu S.Y., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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, AND MUTAGENESIS OF CYS-262; PRO-263; HIS-266; CYS-287; LYS-288;
RP HIS-291; CYS-314; PRO-315; HIS-318; CYS-342; ARG-343; HIS-346; CYS-365;
RP LYS-366 AND HIS-369.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAF87903.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At1g21570 and At1g21580.; Evidence={ECO:0000305};
CC Sequence=AEE30120.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At1g21570 and At1g21580.; Evidence={ECO:0000305};
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DR EMBL; AC015447; AAF87903.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30120.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BT030384; ABO45687.1; -; mRNA.
DR AlphaFoldDB; Q3ED78; -.
DR iPTMnet; Q3ED78; -.
DR PeptideAtlas; Q3ED78; -.
DR PRIDE; Q3ED78; -.
DR ProteomicsDB; 240525; -.
DR EnsemblPlants; AT1G21580.1; AT1G21580.1; AT1G21580.
DR Gramene; AT1G21580.1; AT1G21580.1; AT1G21580.
DR Araport; AT1G21570; -.
DR HOGENOM; CLU_001506_0_0_1; -.
DR InParanoid; Q3ED78; -.
DR PhylomeDB; Q3ED78; -.
DR PRO; PR:Q3ED78; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q3ED78; baseline and differential.
DR Genevisible; Q3ED78; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR000571; Znf_CCCH.
DR SMART; SM00356; ZnF_C3H1; 5.
DR PROSITE; PS50103; ZF_C3H1; 5.
PE 1: Evidence at protein level;
KW DNA-binding; Hydrolase; Metal-binding; Nuclease; Reference proteome;
KW Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..470
FT /note="Zinc finger CCCH domain-containing protein 7"
FT /id="PRO_0000343168"
FT ZN_FING 240..269
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 273..294
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 295..321
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 322..349
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 350..372
FT /note="C3H1-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 122..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..386
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 262
FT /note="C->S: Loss of RNA binding and reduction of
FT ribonuclease activity; when associated with P-263 and H-
FT 266."
FT /evidence="ECO:0000269|PubMed:18582464"
FT MUTAGEN 263
FT /note="P->T: Loss of RNA binding and reduction of
FT ribonuclease activity; when associated with C-262 and H-
FT 266."
FT /evidence="ECO:0000269|PubMed:18582464"
FT MUTAGEN 266
FT /note="H->Y: Loss of RNA binding and reduction of
FT ribonuclease activity; when associated with C-262 and P-
FT 263."
FT /evidence="ECO:0000269|PubMed:18582464"
FT MUTAGEN 287
FT /note="C->S: Loss of RNA binding and reduction of
FT ribonuclease activity; when associated with K-288 and H-
FT 291."
FT /evidence="ECO:0000269|PubMed:18582464"
FT MUTAGEN 288
FT /note="K->T: Loss of RNA binding and reduction of
FT ribonuclease activity; when associated with C-287 and H-
FT 291."
FT /evidence="ECO:0000269|PubMed:18582464"
FT MUTAGEN 291
FT /note="H->Y: Loss of RNA binding and reduction of
FT ribonuclease activity; when associated with C-287 and K-
FT 288."
FT /evidence="ECO:0000269|PubMed:18582464"
FT MUTAGEN 314
FT /note="C->S: No effect on RNA-binding and ribonuclease
FT activities; when associated with P-315 and H-318."
FT /evidence="ECO:0000269|PubMed:18582464"
FT MUTAGEN 315
FT /note="P->T: No effect on RNA-binding and ribonuclease
FT activities; when associated with C-314 and H-318."
FT /evidence="ECO:0000269|PubMed:18582464"
FT MUTAGEN 318
FT /note="H->Y: No effect on RNA-binding and ribonuclease
FT activities; when associated with C-314 and P-318."
FT /evidence="ECO:0000269|PubMed:18582464"
FT MUTAGEN 342
FT /note="C->S: No effect on RNA-binding and ribonuclease
FT activities; when associated with R-343 and H-346."
FT /evidence="ECO:0000269|PubMed:18582464"
FT MUTAGEN 343
FT /note="R->T: No effect on RNA-binding and ribonuclease
FT activities; when associated with C-342 and H-346."
FT /evidence="ECO:0000269|PubMed:18582464"
FT MUTAGEN 346
FT /note="H->Y: No effect on RNA-binding and ribonuclease
FT activities; when associated with C-342 and R-343."
FT /evidence="ECO:0000269|PubMed:18582464"
FT MUTAGEN 365
FT /note="C->S: Loss of RNA binding and reduction of
FT ribonuclease activity; when associated with K-366 and H-
FT 369."
FT /evidence="ECO:0000269|PubMed:18582464"
FT MUTAGEN 366
FT /note="K->T: Loss of RNA binding and reduction of
FT ribonuclease activity; when associated with C-365 and H-
FT 369."
FT /evidence="ECO:0000269|PubMed:18582464"
FT MUTAGEN 369
FT /note="H->Y: Loss of RNA binding and reduction of
FT ribonuclease activity; when associated with C-365 and K-
FT 366."
FT /evidence="ECO:0000269|PubMed:18582464"
SQ SEQUENCE 470 AA; 53768 MW; C4709E973CD912A6 CRC64;
MRPFKQSKFS LVWTQNDPQP RMPIAHMRNQ NIVPQLVPWK RVTYWRRLMN SVSAFRNGSS
LNISRKLSMM RKRHTIYTRS TNGYSLRKSK VLSVGGSHLK WSKSIERDSR KANEEATLAV
AAYSKKESEK QSGQNNTSTA SRNHLARERV FRFGSLRYKM DSSRRTLQRI SDVDSPCSGP
SENGKGVKRP FIPKRLVIGN EEYVRFGNGN QLVRDPKKRT RVLANEKVRW SLHNARLRLA
KKKKYCQFFT RFGKCNKDDG KCPYVHDPSK IAVCTKFLNG LCANANCKLT HKVIPERMPD
CSYYLQGLCN NEACPYRHVH VNPIAPICDG FLKGYCSEGD ECRKKHSYNC PVFEATGSCS
QGLKCKLHHP KNQSKGRKRK RTNEPSQKNA RRRYFSSLHN ILSESEPMVF NRRSTDSEVF
GMESLDFITL GTAEYEAGDD NDPATVQSIS SDSESLISIY NLITPVALMQ
