ID HAZ1_ORYSJ Reviewed; 792 AA.
AC Q8H991; Q8H990;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 166.
DE RecName: Full=Homeobox protein HAZ1 {ECO:0000305};
DE AltName: Full=Homeobox protein HOX1A homolog {ECO:0000305};
GN Name=HAZ1 {ECO:0000303|PubMed:15094187};
GN Synonyms=HOX1A {ECO:0000303|PubMed:21951842};
GN OrderedLocusNames=Os06g0229300 {ECO:0000312|EMBL:BAF19128.1},
GN LOC_Os06g12400 {ECO:0000305};
GN ORFNames=P0525F01.18 {ECO:0000312|EMBL:BAD37267.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Nipponbare;
RX PubMed=15094187; DOI=10.1016/j.gene.2004.02.040;
RA Ito Y., Chujo A., Eiguchi M., Kurata N.;
RT "Radial axis differentiation in a globular embryo is marked by HAZ1, a PHD-
RT finger homeobox gene of rice.";
RL Gene 331:9-15(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ilpoombyeo;
RA Yoon U.H., Lee G.S., Lee J.S., Hahn J.H., Kim C.K., Lee J.H., Kim Y.H.;
RT "Oryza sativa japonica group clone KCS150D11 PHD-finger family homeodomain
RT protein mRNA.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY
RP GIBBERELLIN.
RX PubMed=21951842; DOI=10.1111/j.1744-7909.2011.01075.x;
RA Wen B.Q., Xing M.Q., Zhang H., Dai C., Xue H.W.;
RT "Rice homeobox transcription factor HOX1a positively regulates gibberellin
RT responses by directly suppressing EL1.";
RL J. Integr. Plant Biol. 53:869-878(2011).
CC -!- FUNCTION: Transcriptional repressor involved in the regulation of
CC gibberrelin (GA) signaling. Binds to the 5'-GATC-3' motif of HD16/EL1
CC promoter. Functions as a positive regulator of GA signaling by
CC suppressing the expression of HD16/EL1, a negative regulator of GA
CC signaling. {ECO:0000269|PubMed:21951842}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21951842}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, panicle and
CC seeds. {ECO:0000269|PubMed:21951842}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the outer layers of globular embryos.
CC {ECO:0000269|PubMed:15094187}.
CC -!- INDUCTION: Induced by gibberellin. {ECO:0000269|PubMed:21951842}.
CC -!- MISCELLANEOUS: Plants over-expressing HAZ1 show increased length of the
CC uppermost internode and panicle, due to enhanced gibberellin signaling.
CC {ECO:0000269|PubMed:21951842}.
CC -!- SIMILARITY: Belongs to the PHD-associated homeobox family.
CC {ECO:0000305}.
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DR EMBL; AB081340; BAC15621.1; -; mRNA.
DR EMBL; AB081341; BAC15622.1; -; Genomic_DNA.
DR EMBL; FJ940197; ADB84619.1; -; mRNA.
DR EMBL; AP003509; BAD37267.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19128.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS96897.1; -; Genomic_DNA.
DR EMBL; AK121314; BAH00425.1; -; mRNA.
DR RefSeq; XP_015644127.1; XM_015788641.1.
DR AlphaFoldDB; Q8H991; -.
DR SMR; Q8H991; -.
DR STRING; 39947.Q8H991; -.
DR PaxDb; 39947-Q8H991; -.
DR EnsemblPlants; Os06t0229300-01; Os06t0229300-01; Os06g0229300.
DR GeneID; 4340565; -.
DR Gramene; Os06t0229300-01; Os06t0229300-01; Os06g0229300.
DR KEGG; osa:4340565; -.
DR eggNOG; KOG4299; Eukaryota.
DR HOGENOM; CLU_011923_0_0_1; -.
DR InParanoid; Q8H991; -.
DR OMA; HFGPAIN; -.
DR OrthoDB; 473783at2759; -.
DR PlantReactome; R-OSA-9631623; Regulation of embryo development.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IDA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR GO; GO:0009939; P:positive regulation of gibberellic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR CDD; cd15504; PHD_PRHA_like; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR045876; PRHA-like_PHD-finger.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12628:SF22; HOMEOBOX PROTEIN HAZ1; 1.
DR PANTHER; PTHR12628; POLYCOMB-LIKE TRANSCRIPTION FACTOR; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Gibberellin signaling pathway; Homeobox; Metal-binding;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..792
FT /note="Homeobox protein HAZ1"
FT /id="PRO_0000437437"
FT ZN_FING 244..301
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT DNA_BIND 610..669
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 87306 MW; D16F30BFFB24683B CRC64;
MDKTTTSDLV LDNDNIGSNA GSAQEPLTTN GKTSGVRNRY KQTVKRGRKG SQISPSKTYP
LRSSHSNVRV LRSASKKKNE TPIVPTNDNT AVQRVAKKRK RSKPLRPAPS RVLRSTSEKK
NKAHNELLND GAGVQPAEKK RKVGRPPKGG TPKDDYLMIR KRVRYVLNRM NYEQSLIQAY
ASEGWKGQSL EKIRPEKELE RAKVEILRCK SRIREAFRNL DSLLSEGKLD ESMFDSAGEI
SSEDIFCAAC GSKDVTLKND IILCDGICDR GFHQYCLNPP LLAEDIPQGD EGWLCPACDC
KIDCIDVLNE LQGVKLSIHD SWEKVFPEAA SFLNGSKQID ASDLPSDDSA DNDYDPTLAQ
GHKVDEEKSS GEDGGEGLDS DDSSSEDSES SEKEKSKTSQ NGRTVDDLGL PSEDSEDGDF
DPAGPDSDKE QNDESNSDQS DESDFTSDSD DFCAEIAKSC GQDEISGPSS SQIRTVDRTD
GSGFDGEPNA ENSNLAFMET ELEQDMVLPI SSKRQVERLD YKKLYNEAYG KASSDSSDDE
EWYGNSTPEK GNLEDSETDS LAESPQGGKG FSRRAPVRYH NNEHTPQNVR PGGSVSDQQT
EVLCSNSNGS TAKNRHFGPA INQKLKAHFK EDPYPSRATK ENLAQELGLT FNQVTKWFSS
TRHYARVAAT KKENNIENHT AENNNNTNTV DSIQLRGSND IVSVDRNDMV SEERTGQSNL
NEGTPLRSDT SCGQSVAVTP MVHPENQGND SSSNVRTPNA KSAEKLIPGL ENSDEARRKA
VQRELRKMKT GR
//
