GIP1_ARATH
ID GIP1_ARATH Reviewed; 567 AA.
AC Q8VZS6; Q84U77; Q9LK49;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=GBF-interacting protein 1 {ECO:0000303|PubMed:16117846};
GN Name=GIP1 {ECO:0000303|PubMed:16117846};
GN OrderedLocusNames=At3g13222 {ECO:0000312|Araport:AT3G13222};
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 [MRNA] OF 75-567, FUNCTION, INTERACTION WITH GBF1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16117846; DOI=10.1038/sj.cr.7290326;
RA Sehnke P.C., Laughner B.J., Lyerly Linebarger C.R., Gurley W.B., Ferl R.J.;
RT "Identification and characterization of GIP1, an Arabidopsis thaliana
RT protein that enhances the DNA binding affinity and reduces the oligomeric
RT state of G-box binding factors.";
RL Cell Res. 15:567-575(2005).
RN [5]
RP FUNCTION, INTERACTION WITH LBD18, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=24484953; DOI=10.1016/j.jplph.2013.11.003;
RA Lee H.W., Park J.H., Park M.Y., Kim J.;
RT "GIP1 may act as a coactivator that enhances transcriptional activity of
RT LBD18 in Arabidopsis.";
RL J. Plant Physiol. 171:14-18(2014).
RN [6]
RP FUNCTION, SUBUNIT, INTERACTION WITH BZIP16; BZIP68 AND GBF1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=25387999; DOI=10.1007/s00709-014-0726-9;
RA Shaikhali J.;
RT "GIP1 protein is a novel cofactor that regulates DNA-binding affinity of
RT redox-regulated members of bZIP transcription factors involved in the early
RT stages of Arabidopsis development.";
RL Protoplasma 252:867-883(2015).
CC -!- FUNCTION: Plant specific protein that enhances G-box-binding factor
CC (GBF) DNA binding activity. May function as a nuclear chaperone or
CC lever and regulate the multimeric state of GBFs. May contribute to
CC bZIP-mediated gene regulation. Is able to refold denatured rhodanese in
CC vitro (PubMed:16117846, PubMed:25387999). Reduces DNA-binding activity
CC of BZIP16, BZIP68 and GBF1 under non-reducing conditions through direct
CC physical interaction. Acts as negative co-regulator in red and blue
CC light-mediated hypocotyl elongation. Functions to promote hypocotyl
CC elongation during the early stages of seedling development by
CC regulating the repression effect by BZIP16 and the activation effect by
CC BZIP68 and GBF1 on LHCB2.4 expression (PubMed:25387999). Enhances
CC transcriptional activity of LBD18 in the EXP14 promoter. May act as a
CC transcriptional coactivator of LBD18 (PubMed:24484953).
CC {ECO:0000269|PubMed:16117846, ECO:0000269|PubMed:24484953,
CC ECO:0000269|PubMed:25387999}.
CC -!- SUBUNIT: Monomer, homodimer, homooligomer. Under non-reducing
CC conditions, predominantly present in high molecular weight forms, but
CC predominates in low molecular weight monomers under reducing conditions
CC (PubMed:25387999). Interacts with BZIP16, BZIP68 and GBF1
CC (PubMed:25387999). Interacts with LBD18 (PubMed:24484953).
CC {ECO:0000269|PubMed:24484953, ECO:0000269|PubMed:25387999}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16117846,
CC ECO:0000269|PubMed:24484953, ECO:0000269|PubMed:25387999}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC {ECO:0000269|PubMed:24484953}.
CC -!- SIMILARITY: Belongs to the GIP1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01415.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000375; BAB01415.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP002042; BAB01415.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE75313.1; -; Genomic_DNA.
DR EMBL; AY063883; AAL36239.1; -; mRNA.
DR EMBL; AY142588; AAN13157.1; -; mRNA.
DR EMBL; AF344829; AAO48724.1; -; mRNA.
DR RefSeq; NP_187929.4; NM_112163.6.
DR AlphaFoldDB; Q8VZS6; -.
DR IntAct; Q8VZS6; 17.
DR STRING; 3702.AT3G13222.1; -.
DR iPTMnet; Q8VZS6; -.
DR PaxDb; Q8VZS6; -.
DR PRIDE; Q8VZS6; -.
DR ProteomicsDB; 220766; -.
DR EnsemblPlants; AT3G13222.1; AT3G13222.1; AT3G13222.
DR GeneID; 820513; -.
DR Gramene; AT3G13222.1; AT3G13222.1; AT3G13222.
DR KEGG; ath:AT3G13222; -.
DR Araport; AT3G13222; -.
DR TAIR; locus:2090019; AT3G13222.
DR eggNOG; ENOG502RQC4; Eukaryota.
DR HOGENOM; CLU_482657_0_0_1; -.
DR InParanoid; Q8VZS6; -.
DR OMA; THQAANC; -.
DR OrthoDB; 345523at2759; -.
DR PhylomeDB; Q8VZS6; -.
DR PRO; PR:Q8VZS6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VZS6; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IDA:TAIR.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:TAIR.
DR InterPro; IPR044277; GIP1.
DR InterPro; IPR009719; GIP1_N.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR46775; PTHR46775; 1.
DR Pfam; PF06972; GIP1_N; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
PE 1: Evidence at protein level;
KW Chaperone; Nucleus; Reference proteome.
FT CHAIN 1..567
FT /note="GBF-interacting protein 1"
FT /id="PRO_0000435635"
FT REGION 70..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 521..522
FT /note="AG -> VDSRR (in Ref. 4; AAO48724)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 567 AA; 61812 MW; F9D3D36D1683F3FC CRC64;
MSRISGDGGS RVSIPADLLQ TIQNIREVTG KQHSDEDIFS VFKECFSDPH ETTQKLLYLD
TFHEVRSKRE RKKENLVPNT QGRGRTGRKN FASSYTDASN GRSAAFKKQS GANHIIGGSG
TASSAPNNAR NDTKPSSIMA PNPISLPSGI SNQKIQDAII SPVDKVDTEE QPLSKATSSS
KDVVEPDKSK ESSVSVAVSD SVVENDTQYA VVETFQIPQQ SERVIKSEVA ASKCKNESLL
KSDVGERPHV TFPVHIQVAK MLENGLTFGS FDSNFVREAS SDKFTIGCDD SNIESSHGTA
ASARKDISTF SQDKNHEISN SAAQNELTLQ PDQTVLPEEG SEGDKVKNEV LPITDTHQAA
KCDAPPISYP DQYSLAAAQQ AMHLYRQQYS LNYFPYGPYF PPYYMPQPYI HQYLSPNGFQ
QQSYLPPGDD APAPPGAELP LTHIKPGSDI GNSPPTTIPF SYTSYAFNHI PSAATINATH
KEEKKENMYT TGPLSLANLQ ASPMYNLSLQ GQPIAFPTMQ AGIRGLYQQT QPILAPLSIS
ARTEPIGPSH VTNQQPQAAR TNLGNNY
