ZFP3_ARATH
ID ZFP3_ARATH Reviewed; 235 AA.
AC Q39262;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Zinc finger protein 3 {ECO:0000305};
GN Name=ZFP3 {ECO:0000303|PubMed:7599312}; OrderedLocusNames=At5g25160;
GN ORFNames=F21J6.6;
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 [MRNA].
RC STRAIN=cv. Landsberg erecta; TISSUE=Root;
RX PubMed=7599312; DOI=10.1007/bf00020246;
RA Tague B.W., Goodman H.M.;
RT "Characterization of a family of Arabidopsis zinc finger protein cDNAs.";
RL Plant Mol. Biol. 28:267-279(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=24808098; DOI=10.1104/pp.113.234294;
RA Joseph M.P., Papdi C., Kozma-Bognar L., Nagy I., Lopez-Carbonell M.,
RA Rigo G., Koncz C., Szabados L.;
RT "The Arabidopsis ZINC FINGER PROTEIN3 interferes with abscisic acid and
RT light signaling in seed germination and plant development.";
RL Plant Physiol. 165:1203-1220(2014).
CC -!- FUNCTION: Acts as negative regulator of abscisic acid (ABA) signaling
CC during germination and early seedling development. Involved in the
CC regulation of vegetative development and fertility. Modulates red light
CC signaling in seedling photomorphogenesis.
CC {ECO:0000269|PubMed:24808098}.
CC -!- INTERACTION:
CC Q39262; O82239: RFI2; NbExp=3; IntAct=EBI-15200178, EBI-4425094;
CC Q39262; O22152: YAB1; NbExp=3; IntAct=EBI-15200178, EBI-1113627;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q39261}.
CC -!- TISSUE SPECIFICITY: Expressed in the chalaze of seeds, hypocotyls,
CC cotyledons, roots, emerging lateral roots, leaves, sepals and stamens.
CC These data suggest that ZFP3 is expressed in most organs, showing high
CC expression in vascular tissues.
CC -!- INDUCTION: Down-regulated by abscisic acid (ABA).
CC {ECO:0000269|PubMed:24808098}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seeds are hypersensitivite to inhibition of
CC germination by abscisic acid (ABA). {ECO:0000269|PubMed:24808098}.
CC -!- MISCELLANEOUS: Seeds over-expressing ZFP3 are insensitive to inhibition
CC of germination by abscisic acid (ABA). Plants over-expressing ZFP3 are
CC dwarf, have reduced number and size of siliques, which contains few
CC seeds or are empty. {ECO:0000269|PubMed:24808098}.
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DR EMBL; L39646; AAA87299.1; -; mRNA.
DR EMBL; AC006259; AAC98442.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93407.1; -; Genomic_DNA.
DR EMBL; BT008308; AAP37667.1; -; mRNA.
DR PIR; S55883; S55883.
DR RefSeq; NP_197898.1; NM_122425.3.
DR AlphaFoldDB; Q39262; -.
DR BioGRID; 17862; 40.
DR IntAct; Q39262; 38.
DR STRING; 3702.AT5G25160.1; -.
DR PaxDb; Q39262; -.
DR PRIDE; Q39262; -.
DR ProteomicsDB; 242923; -.
DR EnsemblPlants; AT5G25160.1; AT5G25160.1; AT5G25160.
DR GeneID; 832587; -.
DR Gramene; AT5G25160.1; AT5G25160.1; AT5G25160.
DR KEGG; ath:AT5G25160; -.
DR Araport; AT5G25160; -.
DR TAIR; locus:2146960; AT5G25160.
DR eggNOG; ENOG502RXWM; Eukaryota.
DR HOGENOM; CLU_078088_0_0_1; -.
DR InParanoid; Q39262; -.
DR OMA; IHKPNSH; -.
DR OrthoDB; 1344003at2759; -.
DR PhylomeDB; Q39262; -.
DR PRO; PR:Q39262; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39262; baseline and differential.
DR Genevisible; Q39262; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR InterPro; IPR044246; ZFP3-like.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR47287; PTHR47287; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..235
FT /note="Zinc finger protein 3"
FT /id="PRO_0000047844"
FT ZN_FING 61..83
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 186..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 235 AA; 26351 MW; BE4E98D3F72C0049 CRC64;
MDASIVSSST AFPYQDSLNQ SIEDEERDVH NSSHELNLID CIDDTTSIVN ESTTSTEQKL
FSCNYCQRTF YSSQALGGHQ NAHKRERTLA KRGQRMAASA SAFGHPYGFS PLPFHGQYNN
HRSLGIQAHS ISHKLSSYNG FGGHYGQINW SRLPFDQQPA IGKFPSMDNF HHHHHQMMMM
APSVNSRSNN IDSPSNTGRV LEGSPTLEQW HGDKGLLLST SHHEEQQKLD LSLKL
