C3H29_ARATH
ID C3H29_ARATH Reviewed; 597 AA.
AC Q9XEE6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Zinc finger CCCH domain-containing protein 29;
DE Short=AtC3H29;
DE AltName: Full=AtSZF2;
GN OrderedLocusNames=At2g40140; ORFNames=T07M07.3, T7M7.3;
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 [GENOMIC DNA].
RX PubMed=10207155;
RA Wang M.L., Belmonte S., Kim U., Dolan M., Morris J.W., Goodman H.M.;
RT "A cluster of ABA-regulated genes on Arabidopsis thaliana BAC T07M07.";
RL Genome Res. 9:325-333(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [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 FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17609218; DOI=10.1093/pcp/pcm088;
RA Sun J., Jiang H., Xu Y., Li H., Wu X., Xie Q., Li C.;
RT "The CCCH-type zinc finger proteins AtSZF1 and AtSZF2 regulate salt stress
RT responses in Arabidopsis.";
RL Plant Cell Physiol. 48:1148-1158(2007).
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).
CC -!- FUNCTION: Involved in salt stress response. May positively modulate
CC plant tolerance to salt stress. {ECO:0000269|PubMed:17609218}.
CC -!- INTERACTION:
CC Q9XEE6; F4JRB0-2: HHO5; NbExp=3; IntAct=EBI-15197095, EBI-15192423;
CC Q9XEE6; Q9LXU1: PIM1; NbExp=3; IntAct=EBI-15197095, EBI-15193025;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and anthers.
CC {ECO:0000269|PubMed:17609218}.
CC -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:17609218}.
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DR EMBL; AF085279; AAD25930.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09787.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09788.1; -; Genomic_DNA.
DR EMBL; AY093016; AAM13015.1; -; mRNA.
DR EMBL; AY128937; AAM91337.1; -; mRNA.
DR PIR; G84825; G84825.
DR RefSeq; NP_001031517.1; NM_001036440.2.
DR RefSeq; NP_181543.1; NM_129572.5.
DR AlphaFoldDB; Q9XEE6; -.
DR SMR; Q9XEE6; -.
DR BioGRID; 3943; 21.
DR IntAct; Q9XEE6; 19.
DR STRING; 3702.AT2G40140.1; -.
DR iPTMnet; Q9XEE6; -.
DR PaxDb; Q9XEE6; -.
DR PRIDE; Q9XEE6; -.
DR ProteomicsDB; 240299; -.
DR EnsemblPlants; AT2G40140.1; AT2G40140.1; AT2G40140.
DR EnsemblPlants; AT2G40140.2; AT2G40140.2; AT2G40140.
DR GeneID; 818605; -.
DR Gramene; AT2G40140.1; AT2G40140.1; AT2G40140.
DR Gramene; AT2G40140.2; AT2G40140.2; AT2G40140.
DR KEGG; ath:AT2G40140; -.
DR Araport; AT2G40140; -.
DR TAIR; locus:2065058; AT2G40140.
DR eggNOG; KOG1595; Eukaryota.
DR HOGENOM; CLU_015068_2_0_1; -.
DR InParanoid; Q9XEE6; -.
DR OMA; INEPGFW; -.
DR OrthoDB; 905042at2759; -.
DR PhylomeDB; Q9XEE6; -.
DR PRO; PR:Q9XEE6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9XEE6; baseline and differential.
DR Genevisible; Q9XEE6; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR045234; Unkempt-like.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14493; PTHR14493; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW ANK repeat; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Stress response; Zinc; Zinc-finger.
FT CHAIN 1..597
FT /note="Zinc finger CCCH domain-containing protein 29"
FT /id="PRO_0000371987"
FT REPEAT 76..106
FT /note="ANK 1"
FT REPEAT 111..143
FT /note="ANK 2"
FT ZN_FING 254..281
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 289..313
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 320..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 66153 MW; 42C4508E988A4F0A CRC64;
MCGAKSNLCS SKTLTEVEFM RQKSEDGASA TCLLEFAACD DLSSFKREIE ENPSVEIDES
GFWYCRRVGS KKMGFEERTP LMVAAMYGSM EVLNYIIATG RSDVNRVCSD EKVTALHCAV
SGCSVSIVEI IKILLDASAS PNCVDANGNK PVDLLAKDSR FVPNQSRKAV EVLLTGIHGS
VMEEEEEELK SVVTKYPADA SLPDINEGVY GTDDFRMFSF KVKPCSRAYS HDWTECPFVH
PGENARRRDP RKYPYTCVPC PEFRKGSCPK GDSCEYAHGV FESWLHPAQY RTRLCKDETG
CARRVCFFAH RRDELRPVNA STGSAMVSPR SSNQSPEMSV MSPLTLGSSP MNSPMANGVP
LSPRNGGLWQ NRVNSLTPPP LQLNGSRLKS TLSARDMDME MELRFRGLDN RRLGDLKPSN
LEETFGSYDS ASVMQLQSPS RHSQMNHYPS SPVRQPPPHG FESSAAMAAA VMNARSSAFA
KRSLSFKPAP VASNVSDWGS PNGKLEWGMQ RDELNKLRRS ASFGIHGNNN NSVSRPARDY
SDEPDVSWVN SLVKENAPER VNERVGNTVN GAASRDKFKL PSWAEQMYID HEQQIVA
