HIRA_ARATH
ID HIRA_ARATH Reviewed; 1024 AA.
AC Q9LXN4; F4J343;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Protein HIRA;
DE AltName: Full=Histone regulator protein;
GN Name=HIRA; OrderedLocusNames=At3g44530; ORFNames=F14L2.80;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH AS1, AND DISRUPTION
RP PHENOTYPE.
RC TISSUE=Apices;
RX PubMed=16243907; DOI=10.1105/tpc.105.035477;
RA Phelps-Durr T.L., Thomas J., Vahab P., Timmermans M.C.P.;
RT "Maize rough sheath2 and its Arabidopsis orthologue ASYMMETRIC LEAVES1
RT interact with HIRA, a predicted histone chaperone, to maintain knox gene
RT silencing and determinacy during organogenesis.";
RL Plant Cell 17:2886-2898(2005).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP HISTONE H3.3; UBN1; UBN2 AND ASF1A.
RC STRAIN=cv. Columbia;
RX PubMed=25086063; DOI=10.1242/bio.20148680;
RA Nie X., Wang H., Li J., Holec S., Berger F.;
RT "The HIRA complex that deposits the histone H3.3 is conserved in
RT Arabidopsis and facilitates transcriptional dynamics.";
RL Biol. Open 3:794-802(2014).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, AND GENE FAMILY.
RX PubMed=25600486; DOI=10.1111/tpj.12758;
RA Duc C., Benoit M., Le Goff S., Simon L., Poulet A., Cotterell S.,
RA Tatout C., Probst A.V.;
RT "The histone chaperone complex HIR maintains nucleosome occupancy and
RT counterbalances impaired histone deposition in CAF-1 complex mutants.";
RL Plant J. 81:707-722(2015).
CC -!- FUNCTION: Histone chaperone involved in maintining knox genes silencing
CC throughout leaf development (PubMed:16243907). Involved in
CC heterochromatic and euchromatic gene silencing, especially upon salt
CC stress (PubMed:25600486). Involved in gene expression reprogramming
CC during dedifferentiation probably by modifying histone H3.3 recruitment
CC at the nucleolus (PubMed:25086063, PubMed:25600486). Contributes to
CC maintenance of silencing of pericentromeric repeats and certain
CC transposons (PubMed:25600486). {ECO:0000269|PubMed:16243907,
CC ECO:0000269|PubMed:25086063, ECO:0000269|PubMed:25600486}.
CC -!- SUBUNIT: Component of the HIRA complex made of UBN1, UBN2, ASF1A,
CC CABIN1 and HIRA (PubMed:25086063, PubMed:25600486). Binds to histone
CC H3.3, UBN1, UBN2 and ASF1A (PubMed:25086063). Interacts with AS1
CC (PubMed:16243907). {ECO:0000269|PubMed:16243907,
CC ECO:0000269|PubMed:25086063, ECO:0000269|PubMed:25600486}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25086063}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:25086063}. Note=Localized at rDNA loci in
CC the nucleolus. {ECO:0000269|PubMed:25086063}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LXN4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in the meristem and developing leaf
CC primordia. {ECO:0000269|PubMed:16243907}.
CC -!- DISRUPTION PHENOTYPE: Plants are embryo lethal when homozygous
CC (PubMed:16243907). Retarded root growth. Abnormal gene expression
CC reprogramming during dedifferentiation in root-derived protoplasts
CC (PubMed:25086063). Reduced fertility leading to less seeds production.
CC Reduced histone H3 levels and decreases nucleosome occupancy at both
CC actively transcribed genes and heterochromatic regions
CC (PubMed:25600486). {ECO:0000269|PubMed:16243907,
CC ECO:0000269|PubMed:25086063, ECO:0000269|PubMed:25600486}.
CC -!- SIMILARITY: Belongs to the WD repeat HIR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE77910.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB88535.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL353818; CAB88535.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77910.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77911.2; -; Genomic_DNA.
DR PIR; T48933; T48933.
DR RefSeq; NP_001319681.1; NM_001339149.1. [Q9LXN4-1]
DR RefSeq; NP_190039.2; NM_114321.3.
DR AlphaFoldDB; Q9LXN4; -.
DR SMR; Q9LXN4; -.
DR BioGRID; 8898; 10.
DR STRING; 3702.AT3G44530.1; -.
DR PaxDb; Q9LXN4; -.
DR PRIDE; Q9LXN4; -.
DR ProteomicsDB; 230204; -. [Q9LXN4-1]
DR EnsemblPlants; AT3G44530.2; AT3G44530.2; AT3G44530. [Q9LXN4-1]
DR GeneID; 823578; -.
DR Gramene; AT3G44530.2; AT3G44530.2; AT3G44530. [Q9LXN4-1]
DR KEGG; ath:AT3G44530; -.
DR Araport; AT3G44530; -.
DR eggNOG; KOG0973; Eukaryota.
DR InParanoid; Q9LXN4; -.
DR OrthoDB; 685536at2759; -.
DR PRO; PR:Q9LXN4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LXN4; baseline and differential.
DR GO; GO:0000417; C:HIR complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030875; C:rDNA protrusion; IDA:UniProtKB.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR031120; HIR1.
DR InterPro; IPR011494; Hira.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13831; PTHR13831; 1.
DR Pfam; PF07569; Hira; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Coiled coil; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; WD repeat.
FT CHAIN 1..1024
FT /note="Protein HIRA"
FT /id="PRO_0000299132"
FT REPEAT 10..50
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 64..103
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 123..162
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 165..204
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 214..256
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 279..329
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 333..374
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REPEAT 570..609
FT /note="WD 8"
FT /evidence="ECO:0000255"
FT REPEAT 649..687
FT /note="WD 9"
FT /evidence="ECO:0000255"
FT REPEAT 689..727
FT /note="WD 10"
FT /evidence="ECO:0000255"
FT REPEAT 745..790
FT /note="WD 11"
FT /evidence="ECO:0000255"
FT REPEAT 869..910
FT /note="WD 12"
FT /evidence="ECO:0000255"
FT REGION 409..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 923..946
FT /evidence="ECO:0000255"
FT COMPBIAS 409..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 112390 MW; CC5722C814F3BD6F CRC64;
MIAEKPFWVK HEGLQIFSID VQPNGERFAT GGGDHKVRIW NMKSVDKDLQ NIDTKERLLA
TLRDHFGSVN CVRWAKNSRY VASGSDDQVI QIHERKPGSG TTEFGSGEAP DVENWKAVMT
LRGHTADVVD LNWSPDDSML ASGSLDNTVH IWNMRTGMCT TVLRGHLSLV KGVTWDPIGS
FIASQSDDKT VIIWRTSDWG MAHRTDGHWA KSLGSTFFRR LGWSPCGHFL TTTHGFQKPK
HSAPVLERGE WSVAYDFLGH SAPIIVVRFN HSMFKRIPSS THETKQVGWS NGTSKSGEKD
LQSYNVIAMG SQDRTITVWT TGSARPLFVA KHFFGQSVVD LSWSPDGYSL FACSLDGTVA
MIHFDPKELG VRLTDTELDE LKKSRYGDVR GRQANLVESP AQLLLETAST KQAGSKRAAS
DVQQNQVTTK PSVSVESTAK RRKSQVDDRN KAAESTGQTL NKASTLNRVS SPVNQKVYRR
PDGRKRIIPE AVGVPQQENN IMINGESHNF LPASAAAPAK GDSGDFPVEI SNRDLSGKEI
VCRNPDLKER SRITARATIT ESLVIEKVPG TSGRDGVLNV EQSVGIKESS STDLLIRVFD
WKDGEAAPPV CLEACPREHA LDTVGAVSTS MVKETEISCK KSGETLWSDR IMGRVTVLAG
NPNFWAAGCE DGSLQVYTKC GRRAMPTMMM GSAATFIDCD DSWKLLLVTR KGSLYVWDLF
NRKCVLHDSL SSLVSSDVNL SSTVKGTIKV ISVKLSKSGS PLVVLATRHA FLFDTSLMCW
LRVADDCFPA SNFSSSWNLG SAPCGELAGL QVDVRKYMAR KPGWNRITDD GTQTRAHLES
QLASSLALES PNEYRQCLLA YVRFLAREAD ESRLREVCES FLGPPTGMAE AASSDTNLSW
DPYVLGVKKH KLLRNDILPA MASNRKVQRL LNEFIDLLSE YEDVETADPA PKGSTPTMNC
GGVPSSLDQI GSDPPAMTAT TPMTIDNDKP VSLENPAALD IGVCEKTGSE DRDKQDQNSR
DSGS
