MIP1A_ARATH
ID MIP1A_ARATH Reviewed; 117 AA.
AC Q1G3I2;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=B-box domain protein 30 {ECO:0000303|PubMed:19920209};
DE Short=AtBBX30 {ECO:0000303|PubMed:19920209};
DE AltName: Full=Microprotein 1A {ECO:0000303|PubMed:27015278};
GN Name=MIP1A {ECO:0000303|PubMed:27015278};
GN Synonyms=BBX30 {ECO:0000303|PubMed:19920209};
GN OrderedLocusNames=At4g15248 {ECO:0000312|Araport:AT4G15248};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19920209; DOI=10.1105/tpc.109.069088;
RA Khanna R., Kronmiller B., Maszle D.R., Coupland G., Holm M., Mizuno T.,
RA Wu S.H.;
RT "The Arabidopsis B-box zinc finger family.";
RL Plant Cell 21:3416-3420(2009).
RN [5]
RP FUNCTION, 3D-STRUCTURE MODELING, INTERACTION WITH CO AND TPL, MUTAGENESIS
RP OF CYS-32; CYS-35; CYS-43; CYS-51; CYS-54; HIS-59; HIS-68 AND
RP 113-PRO--LEU-117, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY, AND
RP DOMAIN.
RX PubMed=27015278; DOI=10.1371/journal.pgen.1005959;
RA Graeff M., Straub D., Eguen T., Dolde U., Rodrigues V., Brandt R.,
RA Wenkel S.;
RT "Microprotein-mediated recruitment of CONSTANS into a TOPLESS trimeric
RT complex represses flowering in Arabidopsis.";
RL PLoS Genet. 12:E1005959-E1005959(2016).
CC -!- FUNCTION: Developmental regulator acting by forming heterodimeric
CC complexes, that sequester CO and CO-like (COL) proteins into non-
CC functional complexes. Engages CO and the transcriptional repressor TPL
CC in a tripartite complex. Involved in the CO-mediated long-day
CC flowering-promotion pathway. {ECO:0000269|PubMed:27015278}.
CC -!- SUBUNIT: Interacts with CO (via B-box) and with TPL (via PFVFL motif).
CC {ECO:0000269|PubMed:27015278}.
CC -!- INTERACTION:
CC Q1G3I2; O23379: COL11; NbExp=3; IntAct=EBI-15191905, EBI-15191913;
CC Q1G3I2; Q9SSE5: COL9; NbExp=3; IntAct=EBI-15191905, EBI-15197469;
CC Q1G3I2; P93007: ERF112; NbExp=4; IntAct=EBI-15191905, EBI-15191903;
CC Q1G3I2; Q1G3Q4: RITF1; NbExp=3; IntAct=EBI-15191905, EBI-15193003;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27015278}.
CC -!- TISSUE SPECIFICITY: Highly expressed in shoot apical meristems and in
CC vascular tissues of leaves. Also detected in petioles.
CC {ECO:0000269|PubMed:27015278}.
CC -!- INDUCTION: Circadian-regulation. Peak of expression toward the end of
CC the dark period in both long day and short day photoperiods.
CC {ECO:0000269|PubMed:27015278}.
CC -!- DOMAIN: The PFVFL motif is required for interaction with TPL.
CC {ECO:0000269|PubMed:27015278}.
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DR EMBL; AL117321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002687; AEE83576.1; -; Genomic_DNA.
DR EMBL; DQ487602; ABF59389.1; -; Genomic_DNA.
DR RefSeq; NP_001031645.1; NM_001036568.3.
DR AlphaFoldDB; Q1G3I2; -.
DR IntAct; Q1G3I2; 20.
DR STRING; 3702.AT4G15248.1; -.
DR PaxDb; Q1G3I2; -.
DR PRIDE; Q1G3I2; -.
DR EnsemblPlants; AT4G15248.1; AT4G15248.1; AT4G15248.
DR GeneID; 3769879; -.
DR Gramene; AT4G15248.1; AT4G15248.1; AT4G15248.
DR KEGG; ath:AT4G15248; -.
DR Araport; AT4G15248; -.
DR TAIR; locus:1009023318; AT4G15248.
DR eggNOG; ENOG502S3MI; Eukaryota.
DR HOGENOM; CLU_159621_0_0_1; -.
DR InParanoid; Q1G3I2; -.
DR OMA; ATVYCEA; -.
DR OrthoDB; 1492277at2759; -.
DR PhylomeDB; Q1G3I2; -.
DR PRO; PR:Q1G3I2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q1G3I2; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0009909; P:regulation of flower development; IMP:UniProtKB.
DR InterPro; IPR000315; Znf_B-box.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00336; BBOX; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..117
FT /note="B-box domain protein 30"
FT /id="PRO_0000436350"
FT ZN_FING 27..73
FT /note="B box-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOTIF 113..117
FT /note="PFVFL"
FT /evidence="ECO:0000305"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MUTAGEN 32
FT /note="C->A: In miP1a*; loss of interaction with CO, but no
FT effect on interaction with TPL; when associated with A-35,
FT A-43, A-51, A-54, A-59 and A-68."
FT /evidence="ECO:0000269|PubMed:27015278"
FT MUTAGEN 35
FT /note="C->A: In miP1a*; loss of interaction with CO, but no
FT effect on interaction with TPL; when associated with A-32,
FT A-43, A-51, A-54, A-59 and A-68."
FT /evidence="ECO:0000269|PubMed:27015278"
FT MUTAGEN 43
FT /note="C->A: In miP1a*; loss of interaction with CO, but no
FT effect on interaction with TPL; when associated with A-32,
FT A-35, A-51, A-54, A-59 and A-68."
FT /evidence="ECO:0000269|PubMed:27015278"
FT MUTAGEN 51
FT /note="C->A: In miP1a*; loss of interaction with CO, but no
FT effect on interaction with TPL; when associated with A-32,
FT A-35, A-43, A-54, A-59 and A-68."
FT /evidence="ECO:0000269|PubMed:27015278"
FT MUTAGEN 54
FT /note="C->A: In miP1a*; loss of interaction with CO, but no
FT effect on interaction with TPL; when associated with A-32,
FT A-35, A-43, A-51, A-59 and A-68."
FT /evidence="ECO:0000269|PubMed:27015278"
FT MUTAGEN 59
FT /note="H->A: In miP1a*; loss of interaction with CO, but no
FT effect on interaction with TPL; when associated with A-32,
FT A-35, A-43, A-51, A-54 and A-68."
FT /evidence="ECO:0000269|PubMed:27015278"
FT MUTAGEN 68
FT /note="H->A: In miP1a*; loss of interaction with CO, but no
FT effect on interaction with TPL; when associated with A-32,
FT A-35, A-43, A-51, A-54 and A-59."
FT /evidence="ECO:0000269|PubMed:27015278"
FT MUTAGEN 113..117
FT /note="Missing: Loss of interaction with TPL."
FT /evidence="ECO:0000269|PubMed:27015278"
SQ SEQUENCE 117 AA; 13562 MW; 18C42029A49AFCE7 CRC64;
MCRGFEKEEE RRSDNGGCQR LCTESHKAPV SCELCGENAT VYCEADAAFL CRKCDRWVHS
ANFLARRHLR RVICTTCRKL TRRCLVGDNF NVVLPEIRMI ARIEEHSSDH KIPFVFL
