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RZ1B_ARATH
ID   RZ1B_ARATH              Reviewed;         292 AA.
AC   O22703;
DT   26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 157.
DE   RecName: Full=Glycine-rich RNA-binding protein RZ1B {ECO:0000305};
DE            Short=AtRZ-1a {ECO:0000303|PubMed:20850334};
GN   Name=RZ1B {ECO:0000305};
GN   OrderedLocusNames=At1g60650 {ECO:0000312|Araport:AT1G60650};
GN   ORFNames=F8A5.17 {ECO:0000312|EMBL:AAB71977.1};
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY COLD, AND
RP   DISRUPTION PHENOTYPE.
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).
CC   -!- FUNCTION: Binds RNA and DNA sequences non-specifically. May be involved
CC       in tolerance to cold stress. {ECO:0000269|PubMed:20850334}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20850334}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, rosette and cauline leaves,
CC       stems, floral buds and flowers. {ECO:0000269|PubMed:20850334}.
CC   -!- INDUCTION: By cold stress. Down-regulated by dehydration.
CC       {ECO:0000269|PubMed:20850334}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions. {ECO:0000269|PubMed:20850334}.
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DR   EMBL; AC002292; AAB71977.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33714.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33715.1; -; Genomic_DNA.
DR   EMBL; BT002328; AAN86161.1; -; mRNA.
DR   EMBL; AK221863; BAD94150.1; -; mRNA.
DR   EMBL; AY088195; AAM65738.1; -; mRNA.
DR   PIR; G96631; G96631.
DR   RefSeq; NP_564759.1; NM_104748.3.
DR   RefSeq; NP_849832.1; NM_179501.1.
DR   AlphaFoldDB; O22703; -.
DR   SMR; O22703; -.
DR   BioGRID; 27583; 10.
DR   IntAct; O22703; 7.
DR   STRING; 3702.AT1G60650.2; -.
DR   PaxDb; O22703; -.
DR   PRIDE; O22703; -.
DR   ProteomicsDB; 226694; -.
DR   EnsemblPlants; AT1G60650.1; AT1G60650.1; AT1G60650.
DR   EnsemblPlants; AT1G60650.2; AT1G60650.2; AT1G60650.
DR   GeneID; 842359; -.
DR   Gramene; AT1G60650.1; AT1G60650.1; AT1G60650.
DR   Gramene; AT1G60650.2; AT1G60650.2; AT1G60650.
DR   KEGG; ath:AT1G60650; -.
DR   Araport; AT1G60650; -.
DR   TAIR; locus:2036520; AT1G60650.
DR   eggNOG; KOG0118; Eukaryota.
DR   HOGENOM; CLU_012062_28_0_1; -.
DR   InParanoid; O22703; -.
DR   OMA; ARTYDDR; -.
DR   OrthoDB; 1579773at2759; -.
DR   PhylomeDB; O22703; -.
DR   PRO; PR:O22703; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O22703; baseline and differential.
DR   Genevisible; O22703; AT.
DR   GO; GO:0016607; C:nuclear speck; IDA: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:0003676; F:nucleic acid binding; IDA:TAIR.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IGI:TAIR.
DR   GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IGI:TAIR.
DR   GO; GO:0009409; P:response to cold; IEP:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; IEP: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   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding; Stress response; Zinc; Zinc-finger.
FT   CHAIN           1..292
FT                   /note="Glycine-rich RNA-binding protein RZ1B"
FT                   /id="PRO_0000431281"
FT   DOMAIN          12..90
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   ZN_FING         117..132
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          93..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..213
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..274
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8RWN5"
SQ   SEQUENCE   292 AA;  34398 MW;  DCB6CF13E32A9AF0 CRC64;
     MKDRENDGNL ESRIFVGGLS WDVTERQLES TFDRYGKITE CQIMVGRDTG RPRGFGFITF
     TDRRGADDAI KHMHGRELGN KVISVNKAEP KVGGEDVDQL KKGGGYSSRG KGTEDECFKC
     RRPGHWARDC PSTGDDRERF RVPLAMRSRI GDIDGHRDRY GDRDLERERE REREFDRYMD
     GRRDRDGGRY SYRDRFDSGD KYEPRDHYPF ERYAPPGDRF VSDRYGMPEH HLENEYRGRE
     RSYDRDRYAR DTSDRYGDMG PIRDEGRPYR SRPGPYDRPS RPGGRPSSYE RW
 
 
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