ZFP34_ARATH
ID ZFP34_ARATH Reviewed; 291 AA.
AC Q9FFB6; Q8L9Y9;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=E3 ubiquitin-protein ligase RZFP34 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:26508764};
DE AltName: Full=CHY zinc-finger and RING protein 1 {ECO:0000303|PubMed:26508764};
DE AltName: Full=RING zinc-finger protein 34 {ECO:0000305};
DE AltName: Full=RZFP34 protein homolog {ECO:0000303|PubMed:25002225};
DE Short=AtRZPF34 {ECO:0000303|PubMed:25002225};
GN Name=RZPF34 {ECO:0000303|PubMed:25002225};
GN Synonyms=CHYR1 {ECO:0000303|PubMed:26508764};
GN OrderedLocusNames=At5g22920 {ECO:0000312|Araport:AT5G22920};
GN ORFNames=MRN17.15 {ECO:0000312|EMBL:BAB10613.1};
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 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 INDUCTION.
RX PubMed=17217462; DOI=10.1111/j.1365-313x.2006.02979.x;
RA Osuna D., Usadel B., Morcuende R., Gibon Y., Blaesing O.E., Hoehne M.,
RA Guenter M., Kamlage B., Trethewey R., Scheible W.R., Stitt M.;
RT "Temporal responses of transcripts, enzyme activities and metabolites after
RT adding sucrose to carbon-deprived Arabidopsis seedlings.";
RL Plant J. 49:463-491(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25002225; DOI=10.1007/s11103-014-0217-6;
RA Hsu K.H., Liu C.C., Wu S.J., Kuo Y.Y., Lu C.A., Wu C.R., Lian P.J.,
RA Hong C.Y., Ke Y.T., Huang J.H., Yeh C.H.;
RT "Expression of a gene encoding a rice RING zinc-finger protein, OsRZFP34,
RT enhances stomata opening.";
RL Plant Mol. Biol. 86:125-137(2014).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH SRK2D/2SNRK2.2;
RP SRK2I/SNRK2.3 AND SRK2E/SNRK2.6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION, PHOSPHORYLATION AT SER-173; THR-178 AND SER-208, AND MUTAGENESIS
RP OF CYS-182; HIS-184 AND HIS-187.
RX PubMed=26508764; DOI=10.1105/tpc.15.00321;
RA Ding S., Zhang B., Qin F.;
RT "Arabidopsis RZFP34/CHYR1, a ubiquitin E3 ligase, regulates stomatal
RT movement and drought tolerance via SnRK2.6-mediated phosphorylation.";
RL Plant Cell 27:3228-3244(2015).
CC -!- FUNCTION: Possesses E3 ubiquitin-protein ligase activity in vitro.
CC Mediates mainly 'Lys-48'-linked polyubiquitination. Promotes abscisic
CC acid (ABA)-induced stomatal closure, reactive oxygen species (ROS)
CC production and drought tolerance (PubMed:26508764). Involved in the
CC regulation of stomatal aperture (PubMed:25002225).
CC {ECO:0000269|PubMed:25002225, ECO:0000269|PubMed:26508764}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:26508764};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with SRK2D/2SNRK2.2, SRK2I/SNRK2.3 and
CC SRK2E/SNRK2.6. {ECO:0000269|PubMed:26508764}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26508764}. Cytoplasm
CC {ECO:0000269|PubMed:26508764}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:26508764}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, and anthers and stigma
CC of open flowers. {ECO:0000269|PubMed:26508764}.
CC -!- INDUCTION: Induced during sucrose starvation. Repressed by sucrose
CC (PubMed:17217462). Induced by cold, drought and salt stresses, and
CC abscisic acid (ABA) (PubMed:26508764). {ECO:0000269|PubMed:17217462,
CC ECO:0000269|PubMed:26508764}.
CC -!- PTM: Phosphorylated at Ser-173, Thr-178 and Ser-208 by SRK2E/SNRK2.6 in
CC response to abscisic acid (ABA). Phosphorylation activates its E3
CC ubiquitin-protein ligase activity. {ECO:0000269|PubMed:26508764}.
CC -!- DISRUPTION PHENOTYPE: Decreased relative stomata aperture under normal
CC growth conditions (PubMed:25002225). No visible phenotype under normal
CC growth conditions, but mutant plants display decreased sensitivity to
CC abscisic acid (ABA) during seed germination (PubMed:26508764).
CC {ECO:0000269|PubMed:25002225, ECO:0000269|PubMed:26508764}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM65683.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ059131; AAY57617.1; -; mRNA.
DR EMBL; AB005243; BAB10613.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93097.1; -; Genomic_DNA.
DR EMBL; AY052362; AAK96553.1; -; mRNA.
DR EMBL; BT002635; AAO11551.1; -; mRNA.
DR EMBL; AY088138; AAM65683.1; ALT_INIT; mRNA.
DR RefSeq; NP_197683.1; NM_122198.3.
DR AlphaFoldDB; Q9FFB6; -.
DR SMR; Q9FFB6; -.
DR STRING; 3702.AT5G22920.1; -.
DR iPTMnet; Q9FFB6; -.
DR PaxDb; Q9FFB6; -.
DR PRIDE; Q9FFB6; -.
DR ProteomicsDB; 242948; -.
DR EnsemblPlants; AT5G22920.1; AT5G22920.1; AT5G22920.
DR GeneID; 832356; -.
DR Gramene; AT5G22920.1; AT5G22920.1; AT5G22920.
DR KEGG; ath:AT5G22920; -.
DR Araport; AT5G22920; -.
DR TAIR; locus:2172656; AT5G22920.
DR eggNOG; KOG1940; Eukaryota.
DR HOGENOM; CLU_013368_1_1_1; -.
DR InParanoid; Q9FFB6; -.
DR OMA; SHVQFHI; -.
DR OrthoDB; 1303946at2759; -.
DR PhylomeDB; Q9FFB6; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FFB6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFB6; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:1902456; P:regulation of stomatal opening; IMP:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039512; RCHY1_zinc-ribbon.
DR InterPro; IPR008913; Znf_CHY.
DR InterPro; IPR037274; Znf_CHY_sf.
DR InterPro; IPR017921; Znf_CTCHY.
DR InterPro; IPR037275; Znf_CTCHY_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF05495; zf-CHY; 1.
DR Pfam; PF14634; zf-RING_5; 1.
DR Pfam; PF14599; zinc_ribbon_6; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF161219; SSF161219; 1.
DR SUPFAM; SSF161245; SSF161245; 1.
DR PROSITE; PS51266; ZF_CHY; 1.
DR PROSITE; PS51270; ZF_CTCHY; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..291
FT /note="E3 ubiquitin-protein ligase RZFP34"
FT /id="PRO_0000440630"
FT ZN_FING 20..96
FT /note="CHY-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT ZN_FING 98..162
FT /note="CTCHY-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT ZN_FING 163..206
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 271..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26508764"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26508764"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26508764"
FT MUTAGEN 182
FT /note="C->S: Abolishes E3 ubiquitin-protein ligase
FT activity; when associated with Y-184 and Y-187."
FT /evidence="ECO:0000269|PubMed:26508764"
FT MUTAGEN 184
FT /note="H->Y: Abolishes E3 ubiquitin-protein ligase
FT activity; when associated with Y-184 and Y-187."
FT /evidence="ECO:0000269|PubMed:26508764"
FT MUTAGEN 187
FT /note="H->Y: Abolishes E3 ubiquitin-protein ligase
FT activity; when associated with Y-184 and Y-187."
FT /evidence="ECO:0000269|PubMed:26508764"
FT CONFLICT 231
FT /note="M -> L (in Ref. 5; AAM65683)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 33549 MW; A54E62844ED93A66 CRC64;
MDMGFHENEQ NQEFANLMEI GSGHYGCSHY RRRCKIRAPC CDEIFDCRHC HNEAKDSLHI
EQHHRHELPR HEVSKVICSL CETEQDVQQN CSNCGVCMGK YFCSKCKFFD DDLSKKQYHC
DECGICRTGG EENFFHCKRC RCCYSKIMED KHQCVEGAMH HNCPVCFEYL FDSTRDITVL
RCGHTMHLEC TKDMGLHNRY TCPVCSKSIC DMSNLWKKLD EEVAAYPMPK MYENKMVWIL
CNDCGSNTNV RFHLIAHKCS SCGSYNTRQT QRGSDSHSCS SGMPQVVGST G
