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REM19_ARATH
ID   REM19_ARATH             Reviewed;         226 AA.
AC   Q9XIB5; Q94B43;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=B3 domain-containing protein REM19;
DE   AltName: Full=Protein RELATED TO VERNALIZATION 1;
DE   AltName: Full=Protein REPRODUCTIVE MERISTEM 19;
GN   Name=REM19; Synonyms=RTV1; OrderedLocusNames=At1g49480; ORFNames=F13F21.8;
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   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY.
RX   PubMed=18986826; DOI=10.1016/j.tplants.2008.09.006;
RA   Swaminathan K., Peterson K., Jack T.;
RT   "The plant B3 superfamily.";
RL   Trends Plant Sci. 13:647-655(2008).
RN   [6]
RP   INTERACTION WITH ITN1.
RX   PubMed=22664102; DOI=10.1016/j.bbrc.2012.05.136;
RA   Sakamoto H., Sakata K., Kusumi K., Kojima M., Sakakibara H., Iba K.;
RT   "Interaction between a plasma membrane-localized ankyrin-repeat protein
RT   ITN1 and a nuclear protein RTV1.";
RL   Biochem. Biophys. Res. Commun. 423:392-397(2012).
RN   [7]
RP   INTERACTION WITH XLG2, INDUCTION BY COLD, DNA-BINDING, FUNCTION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=22232549; DOI=10.1074/jbc.m111.317412;
RA   Heo J.B., Sung S., Assmann S.M.;
RT   "Ca2+-dependent GTPase, extra-large G protein 2 (XLG2), promotes activation
RT   of DNA-binding protein related to vernalization 1 (RTV1), leading to
RT   activation of floral integrator genes and early flowering in Arabidopsis.";
RL   J. Biol. Chem. 287:8242-8253(2012).
CC   -!- FUNCTION: Involved in the regulation of vernalization (By similarity).
CC       Binds to DNA in vitro in a non-sequence-specific manner. XLG2 promotes
CC       the DNA binding activity of RTV1 specifically to promoter regions of FT
CC       and SOC1 in vivo and thus leads to the activation of floral integrator
CC       genes. {ECO:0000250, ECO:0000269|PubMed:22232549}.
CC   -!- SUBUNIT: Interacts with XLG2 (PubMed:22232549). Interacts with ITN1
CC       (PubMed:22664102). {ECO:0000269|PubMed:22232549,
CC       ECO:0000269|PubMed:22664102}.
CC   -!- INTERACTION:
CC       Q9XIB5; C6KIE6: XLG2; NbExp=4; IntAct=EBI-6869217, EBI-6868693;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00326,
CC       ECO:0000269|PubMed:22232549}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:22232549}.
CC   -!- INDUCTION: By cold. {ECO:0000269|PubMed:22232549}.
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DR   EMBL; AC007504; AAD43153.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32434.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM59711.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM59712.1; -; Genomic_DNA.
DR   EMBL; AY042868; AAK68808.1; -; mRNA.
DR   EMBL; BT015682; AAU15181.1; -; mRNA.
DR   PIR; E96531; E96531.
DR   RefSeq; NP_001322051.1; NM_001333385.1.
DR   RefSeq; NP_001322052.1; NM_001333384.1.
DR   RefSeq; NP_564547.1; NM_103836.4.
DR   AlphaFoldDB; Q9XIB5; -.
DR   SMR; Q9XIB5; -.
DR   BioGRID; 26597; 2.
DR   IntAct; Q9XIB5; 1.
DR   STRING; 3702.AT1G49480.1; -.
DR   iPTMnet; Q9XIB5; -.
DR   PaxDb; Q9XIB5; -.
DR   PRIDE; Q9XIB5; -.
DR   ProteomicsDB; 225955; -.
DR   EnsemblPlants; AT1G49480.1; AT1G49480.1; AT1G49480.
DR   EnsemblPlants; AT1G49480.2; AT1G49480.2; AT1G49480.
DR   EnsemblPlants; AT1G49480.3; AT1G49480.3; AT1G49480.
DR   GeneID; 841372; -.
DR   Gramene; AT1G49480.1; AT1G49480.1; AT1G49480.
DR   Gramene; AT1G49480.2; AT1G49480.2; AT1G49480.
DR   Gramene; AT1G49480.3; AT1G49480.3; AT1G49480.
DR   KEGG; ath:AT1G49480; -.
DR   Araport; AT1G49480; -.
DR   TAIR; locus:2010262; AT1G49480.
DR   eggNOG; ENOG502RXD2; Eukaryota.
DR   HOGENOM; CLU_015069_6_0_1; -.
DR   InParanoid; Q9XIB5; -.
DR   OMA; EPVNKGY; -.
DR   OrthoDB; 1255266at2759; -.
DR   PhylomeDB; Q9XIB5; -.
DR   PRO; PR:Q9XIB5; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9XIB5; baseline and differential.
DR   Genevisible; Q9XIB5; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR   CDD; cd10017; B3_DNA; 1.
DR   Gene3D; 2.40.330.10; -; 1.
DR   InterPro; IPR003340; B3_DNA-bd.
DR   InterPro; IPR015300; DNA-bd_pseudobarrel_sf.
DR   Pfam; PF02362; B3; 1.
DR   SMART; SM01019; B3; 1.
DR   SUPFAM; SSF101936; SSF101936; 1.
DR   PROSITE; PS50863; B3; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..226
FT                   /note="B3 domain-containing protein REM19"
FT                   /id="PRO_0000375112"
FT   DNA_BIND        129..223
FT                   /note="TF-B3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00326"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           70..73
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        33..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        32
FT                   /note="N -> I (in Ref. 3; AAK68808)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        48
FT                   /note="A -> D (in Ref. 3; AAK68808)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   226 AA;  25850 MW;  CB902C811E446A67 CRC64;
     MQMDSAQNQF NKRARLFEDP ELKDAKVIYP SNPESTEPVN KGYGGSTAIQ SFFKESKAEE
     TPKVLKKRGR KKKNPNPEEV NSSTPGGDDS ENRSKFYESA SARKRTVTAE ERERAVNAAK
     TFEPTNPYFR VVLRPSYLYR GCIMYLPSGF AEKYLSGISG FIKLQLGEKQ WPVRCLYKAG
     RAKFSQGWYE FTLENNIGEG DVCVFELLRT RDFVLEVTAF RVNEYV
 
 
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