IDD14_ARATH
ID IDD14_ARATH Reviewed; 419 AA.
AC Q9C9X7; A8MRJ3;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Protein indeterminate-domain 14 {ECO:0000303|PubMed:16784536};
DE Short=AtIDD14 {ECO:0000303|PubMed:16784536};
DE AltName: Full=Transcriptional regulator of starch metabolism IDD14 {ECO:0000303|PubMed:16784536};
GN Name=IDD14 {ECO:0000303|PubMed:16784536};
GN OrderedLocusNames=At1g68130 {ECO:0000312|Araport:AT1G68130};
GN ORFNames=T23K23.2 {ECO:0000312|EMBL:AAG51998.1};
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] (ISOFORM IDD14ALPHA).
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IDD14ALPHA).
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16784536; DOI=10.1186/1471-2164-7-158;
RA Colasanti J., Tremblay R., Wong A.Y., Coneva V., Kozaki A., Mable B.K.;
RT "The maize INDETERMINATE1 flowering time regulator defines a highly
RT conserved zinc finger protein family in higher plants.";
RL BMC Genomics 7:158-158(2006).
RN [6]
RP FUNCTION, ALTERNATIVE SPLICING, SUBUNIT, DISRUPTION PHENOTYPE, DOMAIN, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=21556057; DOI=10.1038/ncomms1303;
RA Seo P.J., Kim M.J., Ryu J.Y., Jeong E.Y., Park C.M.;
RT "Two splice variants of the IDD14 transcription factor competitively form
RT nonfunctional heterodimers which may regulate starch metabolism.";
RL Nat. Commun. 2:303-303(2011).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP AND INDUCTION BY AUXIN.
RX PubMed=24039602; DOI=10.1371/journal.pgen.1003759;
RA Cui D., Zhao J., Jing Y., Fan M., Liu J., Wang Z., Xin W., Hu Y.;
RT "The arabidopsis IDD14, IDD15, and IDD16 cooperatively regulate lateral
RT organ morphogenesis and gravitropism by promoting auxin biosynthesis and
RT transport.";
RL PLoS Genet. 9:E1003759-E1003759(2013).
CC -!- FUNCTION: Transcription factor regulating starch metabolism by binding
CC directly to the promoter of QQS (PubMed:21556057). The IDD14beta
CC isoform attenuates the transcription factor activity by competitively
CC forming heterodimers with reduced DNA-binding
CC capacity(PubMed:21556057). Regulates lateral organ morphogenesis and
CC gravitropic responses (PubMed:24039602). Has a redundant role with
CC IDD16 in directing leaf and floral organ morphogenesis
CC (PubMed:24039602). Involved in the establishment of auxin gradients
CC through the regulation of auxin biosynthesis and transport
CC (PubMed:24039602). {ECO:0000269|PubMed:21556057,
CC ECO:0000269|PubMed:24039602}.
CC -!- SUBUNIT: Homo- and heterodimer of IDD14alpha and IDD14beta.
CC {ECO:0000269|PubMed:21556057}.
CC -!- INTERACTION:
CC Q9C9X7; O80748: B-box domain protein 26; NbExp=3; IntAct=EBI-15191579, EBI-15191535;
CC Q9C9X7; Q17TI5: BRX; NbExp=3; IntAct=EBI-15191579, EBI-4426649;
CC Q9C9X7; Q84MC7: PYL9; NbExp=3; IntAct=EBI-15191579, EBI-2349513;
CC Q9C9X7; F4IPE3: SGR5; NbExp=5; IntAct=EBI-15191579, EBI-15192881;
CC Q9C9X7; O22152: YAB1; NbExp=4; IntAct=EBI-15191579, EBI-1113627;
CC Q9C9X7; Q9LDT3: YAB4; NbExp=3; IntAct=EBI-15191579, EBI-1115523;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21556057,
CC ECO:0000269|PubMed:24039602}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=IDD14alpha;
CC IsoId=Q9C9X7-1; Sequence=Displayed;
CC Name=IDD14beta;
CC IsoId=Q9C9X7-2; Sequence=VSP_057332;
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons and the vasculature of
CC reosette leaves. Weak expression in hypocotyls and floral organs, but
CC not detected in roots and inflorescence stems.
CC {ECO:0000269|PubMed:24039602}.
CC -!- INDUCTION: Not regulated by auxin. {ECO:0000269|PubMed:24039602}.
CC -!- DOMAIN: The coiled-coil domain (311-350) is involved in dimerization.
CC {ECO:0000269|PubMed:21556057}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:24039602).
CC Accelerated growth and slightly early flowering (PubMed:21556057).
CC {ECO:0000269|PubMed:21556057, ECO:0000269|PubMed:24039602}.
CC -!- MISCELLANEOUS: [Isoform IDD14beta]: Lacks a functional DNA-binding
CC domain. Induced under cold conditions. {ECO:0000269|PubMed:21556057}.
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DR EMBL; AC012563; AAG51998.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34752.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34753.1; -; Genomic_DNA.
DR EMBL; BT026478; ABH04585.1; -; mRNA.
DR EMBL; AB493524; BAH30362.1; -; mRNA.
DR PIR; F96704; F96704.
DR RefSeq; NP_001077791.1; NM_001084322.2. [Q9C9X7-2]
DR RefSeq; NP_176980.1; NM_105483.4. [Q9C9X7-1]
DR AlphaFoldDB; Q9C9X7; -.
DR IntAct; Q9C9X7; 9.
DR STRING; 3702.AT1G68130.1; -.
DR iPTMnet; Q9C9X7; -.
DR PaxDb; Q9C9X7; -.
DR PRIDE; Q9C9X7; -.
DR ProteomicsDB; 228779; -. [Q9C9X7-1]
DR EnsemblPlants; AT1G68130.1; AT1G68130.1; AT1G68130. [Q9C9X7-1]
DR EnsemblPlants; AT1G68130.2; AT1G68130.2; AT1G68130. [Q9C9X7-2]
DR GeneID; 843141; -.
DR Gramene; AT1G68130.1; AT1G68130.1; AT1G68130. [Q9C9X7-1]
DR Gramene; AT1G68130.2; AT1G68130.2; AT1G68130. [Q9C9X7-2]
DR KEGG; ath:AT1G68130; -.
DR Araport; AT1G68130; -.
DR TAIR; locus:2200196; AT1G68130.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_014578_0_1_1; -.
DR InParanoid; Q9C9X7; -.
DR OMA; CATNGSI; -.
DR PhylomeDB; Q9C9X7; -.
DR PRO; PR:Q9C9X7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9X7; baseline and differential.
DR Genevisible; Q9C9X7; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:TAIR.
DR GO; GO:0048444; P:floral organ morphogenesis; IGI:TAIR.
DR GO; GO:0009630; P:gravitropism; IGI:TAIR.
DR GO; GO:0009965; P:leaf morphogenesis; IGI:TAIR.
DR GO; GO:0010601; P:positive regulation of auxin biosynthetic process; IGI:TAIR.
DR GO; GO:2000012; P:regulation of auxin polar transport; IGI:TAIR.
DR GO; GO:2000904; P:regulation of starch metabolic process; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..419
FT /note="Protein indeterminate-domain 14"
FT /id="PRO_0000431548"
FT ZN_FING 70..92
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 112..142
FT /note="C2H2-type 2"
FT /evidence="ECO:0000305"
FT ZN_FING 148..175
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 175..198
FT /note="CCHC-type 2; atypical"
FT /evidence="ECO:0000305"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..197
FT /note="SHR-binding"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT REGION 200..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 313..349
FT /evidence="ECO:0000255"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT VAR_SEQ 1..86
FT /note="Missing (in isoform IDD14beta)"
FT /id="VSP_057332"
SQ SEQUENCE 419 AA; 47558 MW; A9EE78F7391EA840 CRC64;
MIDYERSNTT KNINTHHHNP PPSSSSSDLL PDGNGTAVTQ KRKRRPAGTP DPEAEVVSLS
PRTLLESDRY VCEICNQGFQ RDQNLQMHRR RHKVPWKLLK RETNEEVRKR VYVCPEPTCL
HHNPCHALGD LVGIKKHFRR KHSNHKQWIC ERCSKGYAVQ SDYKAHLKTC GTRGHSCDCG
RVFSRVESFI EHQDTCTVRR SQPSNHRLHE QQQHTTNATQ TASTAENNEN GDLSIGPILP
GHPLQRRQSP PSEQQPSTLL YPFVTNGSIE LQLLPSRNCA DETSLSLSIG TMDQKTMSEV
EKKSYEKGET SLEREEARRE TKRQIEIAEL EFAEAKRIRQ HARAELHKAH LFREEASRRI
SATMMQITCH NCKQHFQAPA ALVPPPPQTH CTDESTSLAV SYMSSATTEG EKASDRASS
