HAT31_ARATH
ID HAT31_ARATH Reviewed; 723 AA.
AC Q04996; Q8GZA9; Q9LT66;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 3.
DT 25-MAY-2022, entry version 169.
DE RecName: Full=Homeobox protein HAT3.1;
GN Name=HAT3.1; OrderedLocusNames=At3g19510; ORFNames=MLD14.25, MLD14.37;
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 [MRNA].
RX PubMed=8106082; DOI=10.1046/j.1365-313x.1993.04010137.x;
RA Schindler U., Beckmann H., Cashmore A.R.;
RT "HAT3.1, a novel Arabidopsis homeodomain protein containing a conserved
RT cysteine-rich region.";
RL Plant J. 4:137-150(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Binds only to large DNA fragments. Recognizes a DNA fragment
CC carrying 8 copies of box7 motif of the light-induced cab-E promoter of
CC Nicotiana plumbaginifolia. Also recognizes the box7m1 motif.
CC -!- INTERACTION:
CC Q04996; Q8LA53: MBD2; NbExp=4; IntAct=EBI-4457944, EBI-4425826;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Primarily detected in root tissue.
CC -!- SIMILARITY: Belongs to the PHD-associated homeobox family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02476.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA49263.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X69512; CAA49263.1; ALT_FRAME; mRNA.
DR EMBL; AB025624; BAB02476.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE76250.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64472.1; -; Genomic_DNA.
DR EMBL; AK117105; BAC41784.1; -; mRNA.
DR EMBL; BT005965; AAO64900.1; -; mRNA.
DR PIR; S31437; S31437.
DR RefSeq; NP_001326497.1; NM_001338403.1.
DR RefSeq; NP_188582.1; NM_112838.4.
DR AlphaFoldDB; Q04996; -.
DR BioGRID; 6818; 6.
DR IntAct; Q04996; 5.
DR STRING; 3702.AT3G19510.1; -.
DR iPTMnet; Q04996; -.
DR PaxDb; Q04996; -.
DR PRIDE; Q04996; -.
DR ProteomicsDB; 230184; -.
DR EnsemblPlants; AT3G19510.1; AT3G19510.1; AT3G19510.
DR EnsemblPlants; AT3G19510.2; AT3G19510.2; AT3G19510.
DR GeneID; 821485; -.
DR Gramene; AT3G19510.1; AT3G19510.1; AT3G19510.
DR Gramene; AT3G19510.2; AT3G19510.2; AT3G19510.
DR KEGG; ath:AT3G19510; -.
DR Araport; AT3G19510; -.
DR TAIR; locus:2090694; AT3G19510.
DR eggNOG; KOG0490; Eukaryota.
DR eggNOG; KOG4299; Eukaryota.
DR HOGENOM; CLU_011923_0_0_1; -.
DR InParanoid; Q04996; -.
DR OMA; HFGPAIN; -.
DR OrthoDB; 536362at2759; -.
DR PhylomeDB; Q04996; -.
DR PRO; PR:Q04996; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q04996; baseline and differential.
DR Genevisible; Q04996; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR CDD; cd15504; PHD_PRHA_like; 1.
DR Gene3D; 3.30.40.10; -; 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 Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Homeobox; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..723
FT /note="Homeobox protein HAT3.1"
FT /id="PRO_0000049142"
FT ZN_FING 265..322
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT DNA_BIND 614..673
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..411
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..448
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 368
FT /note="D -> A (in Ref. 1; CAA49263)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 723 AA; 80461 MW; CBA7D4C8757FDECE CRC64;
MYKAVSKRVT RSSGSGLKQT NVDNGGEISP TVDRVSEQGK SSEAGSHMPT DANGNGHLHH
EIMDHGKGNE EQKPTPQTVK KDSNTNTKFS GSHRELVIGL PCRGQFEIHN RSRASTSSKR
LGGGGERNVL FASHKRAQRS KEDAGPSSVV ANSTPVGRPK KKNKTMNKGQ VREDDEYTRI
KKKLRYFLNR INYEQSLIDA YSLEGWKGSS LEKIRPEKEL ERATKEILRR KLKIRDLFQH
LDTLCAEGSL PESLFDTDGE ISSEDIFCAK CGSKDLSVDN DIILCDGFCD RGFHQYCLEP
PLRKEDIPPD DEGWLCPGCD CKDDSLDLLN DSLGTKFSVS DSWEKIFPEA AAALVGGGQN
LDCDLPSDDS DDEEYDPDCL NDNENDEDGS DDNEESENED GSSDETEFTS ASDEMIESFK
EGKDIMKDVM ALPSDDSEDD DYDPDAPTCD DDKESSNSDC TSDTEDLETS FKGDETNQQA
EDTPLEDPGR QTSQLQGDAI LESDVGLDDG PAGVSRRRNV ERLDYKKLYD EEYDNVPTSS
SDDDDWDKTA RMGKEDSESE DEGDTVPLKQ SSNAEDHTSK KLIRKSKRAD KKDTLEMPQE
GPGENGGSGE IEKSSSSACK QTDPKTQRLY ISFQENQYPD KATKESLAKE LQMTVKQVNN
WFKHRRWSIN SKPLVSEENV EKLKTGKEGE CETSVAGSSK QTMETESVAE KPTNTGSRKR
RRK
