RZ1A_ARATH
ID RZ1A_ARATH Reviewed; 245 AA.
AC Q9LIN3;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 156.
DE RecName: Full=Glycine-rich RNA-binding protein RZ1A {ECO:0000305};
DE Short=AtRZ-1a {ECO:0000303|PubMed:15941401};
GN Name=RZ1A {ECO:0000305};
GN OrderedLocusNames=At3g26420 {ECO:0000312|Araport:AT3G26420};
GN ORFNames=F20C19.15 {ECO:0000312|EMBL:AAK96804.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY COLD, AND DISRUPTION PHENOTYPE.
RX PubMed=15941401; DOI=10.1111/j.1365-313x.2005.02420.x;
RA Kim Y.O., Kim J.S., Kang H.;
RT "Cold-inducible zinc finger-containing glycine-rich RNA-binding protein
RT contributes to the enhancement of freezing tolerance in Arabidopsis
RT thaliana.";
RL Plant J. 42:890-900(2005).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=20850334; DOI=10.1016/j.plaphy.2010.08.013;
RA Kim W.Y., Kim J.Y., Jung H.J., Oh S.H., Han Y.S., Kang H.;
RT "Comparative analysis of Arabidopsis zinc finger-containing glycine-rich
RT RNA-binding proteins during cold adaptation.";
RL Plant Physiol. Biochem. 48:866-872(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Binds RNA and DNA sequences with a preference to single-
CC stranded nucleic acids. Displays strong affinity to poly(G) and poly(U)
CC sequences. May be involved in tolerance to cold stress.
CC {ECO:0000269|PubMed:15941401}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20850334}. Cytoplasm
CC {ECO:0000269|PubMed:20850334}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC {ECO:0000269|PubMed:15941401}.
CC -!- INDUCTION: By cold stress. {ECO:0000269|PubMed:15941401}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but germination of mutant seeds is strongly delayed under
CC low temperature conditions. {ECO:0000269|PubMed:15941401}.
CC -!- MISCELLANEOUS: Plants over-expressing RZ1A have enhanced freezing
CC tolerance. {ECO:0000269|PubMed:15941401}.
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DR EMBL; AP001298; BAB02203.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77156.1; -; Genomic_DNA.
DR EMBL; AF424613; AAL11606.1; -; mRNA.
DR EMBL; AY054613; AAK96804.1; -; mRNA.
DR EMBL; AY072457; AAL66872.1; -; mRNA.
DR EMBL; AK221725; BAD93728.1; -; mRNA.
DR EMBL; AK227088; BAE99140.1; -; mRNA.
DR RefSeq; NP_189273.1; NM_113549.3.
DR AlphaFoldDB; Q9LIN3; -.
DR SMR; Q9LIN3; -.
DR BioGRID; 7577; 1.
DR IntAct; Q9LIN3; 1.
DR STRING; 3702.AT3G26420.1; -.
DR iPTMnet; Q9LIN3; -.
DR PaxDb; Q9LIN3; -.
DR PRIDE; Q9LIN3; -.
DR ProteomicsDB; 232832; -.
DR EnsemblPlants; AT3G26420.1; AT3G26420.1; AT3G26420.
DR GeneID; 822246; -.
DR Gramene; AT3G26420.1; AT3G26420.1; AT3G26420.
DR KEGG; ath:AT3G26420; -.
DR Araport; AT3G26420; -.
DR TAIR; locus:2079276; AT3G26420.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_012062_28_1_1; -.
DR InParanoid; Q9LIN3; -.
DR OMA; KYGHLVE; -.
DR PhylomeDB; Q9LIN3; -.
DR PRO; PR:Q9LIN3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR Genevisible; Q9LIN3; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0000166; F:nucleotide binding; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; RNA-binding; Stress response; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..245
FT /note="Glycine-rich RNA-binding protein RZ1A"
FT /id="PRO_0000431280"
FT DOMAIN 7..85
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 120..135
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 80..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 245 AA; 26923 MW; 898EEE3F4AED32B2 CRC64;
MSEDPEYRCF IGGLAWTTSD RGLRDAFEKY GHLVEAKVVL DKFSGRSRGF GFITFDEKKA
MDEAIAAMNG MDLDGRTITV DKAQPHQGGA GRDNDGDRGR DRGYDRDRSR PSGGRGGGDC
FKCGKPGHFA RECPSESSRD GGGRFSSKDD RYSSKDDRYG AKDDRYGAKE DRYGAKDDRY
SSKDDRYSSK DDRYGSRDGG GSRYGPDRSG ERAGGRSRDG GSRGAPGGER HSRAPYDRPR
AGGFH
