RZF1_ARATH
ID RZF1_ARATH Reviewed; 320 AA.
AC Q94AK4; Q9LXY2;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=E3 ubiquitin-protein ligase RZF1 {ECO:0000303|PubMed:23415322};
DE EC=2.3.2.27 {ECO:0000269|PubMed:23415322};
DE AltName: Full=RING-H2 zinc finger protein 1 {ECO:0000303|PubMed:23415322};
DE Short=AtRZF1 {ECO:0000303|PubMed:23415322};
GN Name=RZF1 {ECO:0000303|PubMed:23415322};
GN OrderedLocusNames=At3g56580 {ECO:0000312|Araport:AT3G56580};
GN ORFNames=T5P19.230 {ECO:0000312|EMBL:CAB88061.1};
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=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 [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, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND REPRESSION BY DROUGHT AND OSMOTIC STRESS.
RC STRAIN=cv. Columbia;
RX PubMed=23415322; DOI=10.1016/j.plantsci.2012.12.007;
RA Ju H.-W., Min J.-H., Chung M.-S., Kim C.S.;
RT "The atrzf1 mutation of the novel RING-type E3 ubiquitin ligase increases
RT proline contents and enhances drought tolerance in Arabidopsis.";
RL Plant Sci. 203:1-7(2013).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that promotes osmotic stress
CC responses. Regulates negatively drought-mediated control of early
CC seedling development, probably by influencing proline content, water
CC loss, membrane ion leakage and the expression of dehydration stress-
CC related genes (e.g. RAB18, RD29A, RD29B, AOX1A, ERD15, ERD1, COR15A,
CC P5CS1 and P5CR). {ECO:0000269|PubMed:23415322}.
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:23415322};
CC -!- TISSUE SPECIFICITY: Expressed in seedlings and in flowers.
CC {ECO:0000269|PubMed:23415322}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, especially present in the vascular
CC system. In flowers, observed in sepals, anthers of stamen, and pollen.
CC {ECO:0000269|PubMed:23415322}.
CC -!- INDUCTION: Repressed by drought and osmotic (e.g. 400 mM mannitol)
CC stresses. {ECO:0000269|PubMed:23415322}.
CC -!- DISRUPTION PHENOTYPE: Reduced sensitivity to osmotic stress during
CC early seedling development. Increased proline accumulation and higher
CC expression of stress-related genes (e.g. RAB18, RD29A, RD29B, AOX1A,
CC ERD15, ERD1, COR15A, P5CS1 and P5CR) under drought stress.
CC {ECO:0000269|PubMed:23415322}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB88061.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ059114; AAY57600.1; -; mRNA.
DR EMBL; AL163972; CAB88061.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79537.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79538.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79539.1; -; Genomic_DNA.
DR EMBL; AY045983; AAK76657.1; -; mRNA.
DR EMBL; AY096613; AAM20263.1; -; mRNA.
DR PIR; T49059; T49059.
DR RefSeq; NP_001030874.1; NM_001035797.1.
DR RefSeq; NP_567039.1; NM_115516.3.
DR RefSeq; NP_974448.1; NM_202719.1.
DR AlphaFoldDB; Q94AK4; -.
DR SMR; Q94AK4; -.
DR STRING; 3702.AT3G56580.1; -.
DR PaxDb; Q94AK4; -.
DR PRIDE; Q94AK4; -.
DR EnsemblPlants; AT3G56580.1; AT3G56580.1; AT3G56580.
DR EnsemblPlants; AT3G56580.2; AT3G56580.2; AT3G56580.
DR EnsemblPlants; AT3G56580.3; AT3G56580.3; AT3G56580.
DR GeneID; 824825; -.
DR Gramene; AT3G56580.1; AT3G56580.1; AT3G56580.
DR Gramene; AT3G56580.2; AT3G56580.2; AT3G56580.
DR Gramene; AT3G56580.3; AT3G56580.3; AT3G56580.
DR KEGG; ath:AT3G56580; -.
DR Araport; AT3G56580; -.
DR TAIR; locus:2102569; AT3G56580.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_034892_1_2_1; -.
DR InParanoid; Q94AK4; -.
DR OMA; SIRNTHW; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; Q94AK4; -.
DR PRO; PR:Q94AK4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94AK4; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:1902006; P:negative regulation of proline biosynthetic process; IMP:TAIR.
DR GO; GO:0047484; P:regulation of response to osmotic stress; IMP:UniProtKB.
DR GO; GO:2000070; P:regulation of response to water deprivation; IMP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR GO; GO:0030104; P:water homeostasis; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14369; zinc_ribbon_9; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Metal-binding; Reference proteome; Stress response;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8LPN7"
FT CHAIN 2..320
FT /note="E3 ubiquitin-protein ligase RZF1"
FT /id="PRO_0000439876"
FT ZN_FING 186..227
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 229..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q8LPN7"
SQ SEQUENCE 320 AA; 35791 MW; C8E6677D53D22F89 CRC64;
MSSIRNTHWC HRCQRAVWLR ARDAVCSYCG GGFVEEIDIG PSRAHRDVER DPTFDLMEAF
SAFMRSRLAE RSYDREISGR LGSAGSESFS NLAPLLIFGG QAPFRLAGGD NSSVEAFVNG
AAPGIGIARG TNAGDYFFGP GLEELIEQLS SGTHHRGPPP APKSSIDALP TIKITQKHLK
SSDSHCPVCK DEFELKSEAK QMPCHHIYHS DCIVPWLVQH NSCPVCRKEL PSRGSSSSTQ
SSQNRSTNGR ENSRRRNIFS NLWPFRSSSS SSTQNRRDTN NTATAEEGHY HHHQQQQQQH
QHQHQQQQSH MGYSGWPFDY
