AHL4_ARATH
ID AHL4_ARATH Reviewed; 419 AA.
AC Q9FHM5;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=AT-hook motif nuclear-localized protein 4 {ECO:0000312|EMBL:FAA00275.1};
GN Name=AHL4 {ECO:0000303|PubMed:15604740};
GN OrderedLocusNames=At5g51590 {ECO:0000312|Araport:AT5G51590};
GN ORFNames=K17N15.14 {ECO:0000312|EMBL:BAB08675.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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., 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 [4]
RP IDENTIFICATION, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=15604740; DOI=10.1007/s11103-004-3249-5;
RA Fujimoto S., Matsunaga S., Yonemura M., Uchiyama S., Azuma T., Fukui K.;
RT "Identification of a novel plant MAR DNA binding protein localized on
RT chromosomal surfaces.";
RL Plant Mol. Biol. 56:225-239(2004).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH AHL3, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23335615; DOI=10.1105/tpc.112.102210;
RA Zhou J., Wang X., Lee J.Y., Lee J.Y.;
RT "Cell-to-cell movement of two interacting AT-hook factors in Arabidopsis
RT root vascular tissue patterning.";
RL Plant Cell 25:187-201(2013).
RN [6]
RP GENE FAMILY, AND DOMAIN PPC.
RX PubMed=24218605; DOI=10.1073/pnas.1219277110;
RA Zhao J., Favero D.S., Peng H., Neff M.M.;
RT "Arabidopsis thaliana AHL family modulates hypocotyl growth redundantly by
RT interacting with each other via the PPC/DUF296 domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E4688-E4697(2013).
CC -!- FUNCTION: Transcription factor that specifically binds AT-rich DNA
CC sequences related to the nuclear matrix attachment regions (MARs) (By
CC similarity). Acts redundantly with AHL3 to regulate the formation of
CC tissue boundary between the xylem and procambium in the root meristem.
CC Cell-to-cell movement of AHL4 from the procambium to the xylem is
CC critical for its function in root vascular patterning
CC (PubMed:23335615). {ECO:0000250|UniProtKB:Q8VYJ2,
CC ECO:0000269|PubMed:23335615}.
CC -!- SUBUNIT: Homodimer. Interacts with AHL3. {ECO:0000269|PubMed:23335615}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23335615}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the stele of the root
CC meristem with a specificity to the procambium.
CC {ECO:0000269|PubMed:23335615}.
CC -!- DOMAIN: The PPC domain mediates interactions between AHL proteins.
CC {ECO:0000269|PubMed:24218605}.
CC -!- DISRUPTION PHENOTYPE: Misspecification of tissue boundaries between the
CC xylem and procambium. {ECO:0000269|PubMed:23335615}.
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DR EMBL; AB018109; BAB08675.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96101.1; -; Genomic_DNA.
DR EMBL; AB493788; BAH30626.1; -; mRNA.
DR EMBL; BR000340; FAA00275.1; -; mRNA.
DR RefSeq; NP_199972.1; NM_124538.4.
DR AlphaFoldDB; Q9FHM5; -.
DR SMR; Q9FHM5; -.
DR STRING; 3702.AT5G51590.1; -.
DR PaxDb; Q9FHM5; -.
DR PRIDE; Q9FHM5; -.
DR ProteomicsDB; 244848; -.
DR EnsemblPlants; AT5G51590.1; AT5G51590.1; AT5G51590.
DR GeneID; 835233; -.
DR Gramene; AT5G51590.1; AT5G51590.1; AT5G51590.
DR KEGG; ath:AT5G51590; -.
DR Araport; AT5G51590; -.
DR TAIR; locus:2153142; AT5G51590.
DR eggNOG; ENOG502QTAR; Eukaryota.
DR HOGENOM; CLU_039808_0_0_1; -.
DR InParanoid; Q9FHM5; -.
DR OMA; FGGHSES; -.
DR OrthoDB; 1053982at2759; -.
DR PhylomeDB; Q9FHM5; -.
DR PRO; PR:Q9FHM5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHM5; baseline and differential.
DR Genevisible; Q9FHM5; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IEA:InterPro.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0010051; P:xylem and phloem pattern formation; IMP:UniProtKB.
DR GO; GO:0010089; P:xylem development; IMP:TAIR.
DR CDD; cd11378; DUF296; 1.
DR InterPro; IPR039605; AHL.
DR InterPro; IPR005175; PPC_dom.
DR PANTHER; PTHR31500; PTHR31500; 1.
DR Pfam; PF03479; PCC; 1.
DR PROSITE; PS51742; PPC; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..419
FT /note="AT-hook motif nuclear-localized protein 4"
FT /id="PRO_0000432022"
FT DOMAIN 174..314
FT /note="PPC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01078"
FT DNA_BIND 78..90
FT /note="A.T hook"
FT /evidence="ECO:0000255"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 78..86
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000305"
FT COMPBIAS 38..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..410
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 419 AA; 44594 MW; BDB62A87D187EBF0 CRC64;
MEEREGTNIN NIPTSFGLKQ HETPLPPPGY PPRSENPNLF PVGQSSTSSA AAAVKPSENV
APPFSLTMPV ENSSSELKKK RGRPRKYNPD GSLAVTLSPM PISSSVPLTS EFGSRKRGRG
RGRGRGRGRG RGQGQGSREP NNNNNDNNWL KNPQMFEFNN NTPTSGGGGP AEIVSPSFTP
HVLTVNAGED VTMKIMTFSQ QGSRAICILS ANGPISNVTL RQSMTSGGTL TYEGHFEILS
LTGSFIPSES GGTRSRAGGM SVSLAGQDGR VFGGGLAGLF IAAGPVQVMV GSFIAGQEES
QQQQQQIKKQ RRERLGIPTT TQASNISFGG SAEDPKARYG LNKPVVIQPP PVSAPPVSFS
HEPSTNTVHG YYANNTANHI KDLFSSLPGE DREEDEDDLE GEDDEEFGGH SESDTEVPS
