IDD16_ARATH
ID IDD16_ARATH Reviewed; 362 AA.
AC Q9FRH4; C0SUX3;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Protein indeterminate-domain 16 {ECO:0000303|PubMed:16784536};
DE Short=AtIDD16 {ECO:0000303|PubMed:16784536};
GN Name=IDD16 {ECO:0000303|PubMed:16784536};
GN OrderedLocusNames=At1g25250 {ECO:0000312|Araport:AT1G25250};
GN ORFNames=F4F7.36 {ECO:0000312|EMBL:AAG28820.1};
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].
RA Fujita M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, 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 lateral organ morphogenesis
CC and gravitropic responses (PubMed:24039602). Has a redundant role with
CC IDD14 in directing leaf and floral organ morphogenesis
CC (PubMed:24039602). Acts cooperatively with IDD15 to control silique and
CC branche orientation (PubMed:24039602). Involved in the establishment of
CC auxin gradients through the regulation of auxin biosynthesis and
CC transport (PubMed:24039602). {ECO:0000269|PubMed:24039602}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FRH4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FRH4-2; Sequence=VSP_057333;
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves, hypocotyls, roots,
CC vasculature of cotyledons, floral organs and in the endodermis and
CC vasculaturenof inflorescence stems. {ECO:0000269|PubMed:24039602}.
CC -!- INDUCTION: Not regulated by auxin. {ECO:0000269|PubMed:24039602}.
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DR EMBL; AC079374; AAG28820.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30593.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59434.1; -; Genomic_DNA.
DR EMBL; AB493476; BAH30314.1; -; mRNA.
DR PIR; B86382; B86382.
DR RefSeq; NP_001321791.1; NM_001332672.1. [Q9FRH4-2]
DR RefSeq; NP_173896.1; NM_102334.1. [Q9FRH4-1]
DR AlphaFoldDB; Q9FRH4; -.
DR STRING; 3702.AT1G25250.1; -.
DR PaxDb; Q9FRH4; -.
DR PRIDE; Q9FRH4; -.
DR ProteomicsDB; 228781; -. [Q9FRH4-1]
DR EnsemblPlants; AT1G25250.1; AT1G25250.1; AT1G25250. [Q9FRH4-1]
DR EnsemblPlants; AT1G25250.3; AT1G25250.3; AT1G25250. [Q9FRH4-2]
DR GeneID; 839108; -.
DR Gramene; AT1G25250.1; AT1G25250.1; AT1G25250. [Q9FRH4-1]
DR Gramene; AT1G25250.3; AT1G25250.3; AT1G25250. [Q9FRH4-2]
DR KEGG; ath:AT1G25250; -.
DR Araport; AT1G25250; -.
DR TAIR; locus:2032985; AT1G25250.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_014578_0_1_1; -.
DR InParanoid; Q9FRH4; -.
DR OMA; MIHYEQN; -.
DR PhylomeDB; Q9FRH4; -.
DR PRO; PR:Q9FRH4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FRH4; baseline and differential.
DR Genevisible; Q9FRH4; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0043565; F:sequence-specific DNA binding; IPI: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:2000122; P:negative regulation of stomatal complex development; IMP: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:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR InterPro; IPR039288; SGR5-like.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR34946; PTHR34946; 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 2: Evidence at transcript 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..362
FT /note="Protein indeterminate-domain 16"
FT /id="PRO_0000431549"
FT ZN_FING 39..61
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 82..112
FT /note="C2H2-type 2"
FT /evidence="ECO:0000305"
FT ZN_FING 118..142
FT /note="CCHC-type 1; atypical"
FT /evidence="ECO:0000305"
FT ZN_FING 145..168
FT /note="CCHC-type 2; atypical"
FT /evidence="ECO:0000305"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..167
FT /note="SHR-binding"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT REGION 247..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 252..319
FT /evidence="ECO:0000255"
FT COMPBIAS 249..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT VAR_SEQ 1..19
FT /note="MELTQPIRENGDPQGHQLT -> MIHYEQNNNLQNLPSSSSNDLLLGINGAD
FT ATHKRKRRPAGTP (in isoform 2)"
FT /id="VSP_057333"
SQ SEQUENCE 362 AA; 41481 MW; 20D31B518682397A CRC64;
MELTQPIREN GDPQGHQLTD PDAEVVSLSP RTLLESDRYV CEICNQGFQR DQNLQMHRRR
HKVPWKLLKR DKKDEEVRKR VYVCPEPTCL HHDPCHALGD LVGIKKHFRR KHSVHKQWVC
ERCSKGYAVQ SDYKAHLKTC GSRGHSCDCG RVFSRVESFI EHQDTCTIRQ PQPTNHRHLQ
QHTMGLDAPS RTTSTASFGP LLHGLPLLRP PRPSNQHSPA FAYPFNASSA PFESLELQLS
IGMARTSAQA RHNEKRETSL TKERANEEAR KAEETRQEAK RQIEMAEKDF EKAKRIREEA
KTELEKAHVV REEAIKRINA TMMEITCHSC KQLFQLPVTA DESTSSLVMS YVSSATTEGE
CE
