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GIR2_ARATH
ID   GIR2_ARATH              Reviewed;         117 AA.
AC   Q9SRN4; A0A178VFZ0;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Protein GL2-INTERACTING REPRESSOR 2 {ECO:0000303|PubMed:28526410};
GN   Name=GIR2 {ECO:0000303|PubMed:28526410};
GN   OrderedLocusNames=At3g11600 {ECO:0000312|Araport:AT3G11600};
GN   ORFNames=T19F11.1 {ECO:0000312|EMBL:AAF02129.1};
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=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   [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=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
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   FUNCTION, INTERACTION WITH GL2, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=28526410; DOI=10.1016/j.bbrc.2017.05.084;
RA   Wu R., Citovsky V.;
RT   "Adaptor proteins GIR1 and GIR2. I. Interaction with the repressor GLABRA2
RT   and regulation of root hair development.";
RL   Biochem. Biophys. Res. Commun. 488:547-553(2017).
RN   [7]
RP   FUNCTION, INTERACTION WITH TPL, SUBCELLULAR LOCATION, AND EAR MOTIF.
RX   PubMed=28526412; DOI=10.1016/j.bbrc.2017.05.085;
RA   Wu R., Citovsky V.;
RT   "Adaptor proteins GIR1 and GIR2. II. Interaction with the co-repressor
RT   TOPLESS and promotion of histone deacetylation of target chromatin.";
RL   Biochem. Biophys. Res. Commun. 488:609-613(2017).
CC   -!- FUNCTION: Acts as negative regulator of root hair development
CC       redundantly with GIR1 (PubMed:28526410). GIR1 and GIR2 may function as
CC       adapter proteins that associate with GL2 and participate in the control
CC       of root hair formation (PubMed:28526410). GIR1 and GIR2 may function as
CC       adapter proteins that associate with TPL and participate in the
CC       repression of root gene expression (PubMed:28526412).
CC       {ECO:0000269|PubMed:28526410, ECO:0000269|PubMed:28526412}.
CC   -!- SUBUNIT: Interacts with GL2 (PubMed:28526410). Interacts with TPL
CC       (PubMed:28526412). {ECO:0000269|PubMed:28526410,
CC       ECO:0000269|PubMed:28526412}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28526410,
CC       ECO:0000269|PubMed:28526412}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but the double mutant seedlings gir1 and gir2 exhibit
CC       excessive root hair formation. {ECO:0000269|PubMed:28526410}.
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DR   EMBL; AC009918; AAF02129.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75072.1; -; Genomic_DNA.
DR   EMBL; AK117497; BAC42160.1; -; mRNA.
DR   EMBL; BT005174; AAO50707.1; -; mRNA.
DR   EMBL; AY085790; AAM63007.1; -; mRNA.
DR   RefSeq; NP_566393.1; NM_111993.3.
DR   AlphaFoldDB; Q9SRN4; -.
DR   STRING; 3702.AT3G11600.1; -.
DR   PaxDb; Q9SRN4; -.
DR   PRIDE; Q9SRN4; -.
DR   EnsemblPlants; AT3G11600.1; AT3G11600.1; AT3G11600.
DR   GeneID; 820333; -.
DR   Gramene; AT3G11600.1; AT3G11600.1; AT3G11600.
DR   KEGG; ath:AT3G11600; -.
DR   Araport; AT3G11600; -.
DR   TAIR; locus:2098328; AT3G11600.
DR   eggNOG; ENOG502S48P; Eukaryota.
DR   HOGENOM; CLU_109567_2_1_1; -.
DR   InParanoid; Q9SRN4; -.
DR   OMA; FLQENAF; -.
DR   OrthoDB; 1564121at2759; -.
DR   PhylomeDB; Q9SRN4; -.
DR   PRO; PR:Q9SRN4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SRN4; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0080147; P:root hair cell development; IGI:TAIR.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..117
FT                   /note="Protein GL2-INTERACTING REPRESSOR 2"
FT                   /id="PRO_0000450105"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           10..15
FT                   /note="EAR"
FT                   /evidence="ECO:0000305|PubMed:28526412"
FT   COMPBIAS        18..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   117 AA;  13040 MW;  FE63B45D73D9FD8C CRC64;
     MSRRNKNGPK LELRLNLSPP PSQASQMSLV RSPNRSNTTS PSSCVSSETN QEENETITSM
     VLVGCPRCLM YVMLSDDDPK CPKCKSTVLL DFLQENAFAA TTATAANTRR KKKTWWN
 
 
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