CENH3_ARATH
ID CENH3_ARATH Reviewed; 178 AA.
AC Q8RVQ9; Q8LCW8; Q9LNI6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Histone H3-like centromeric protein CENH3 {ECO:0000303|PubMed:17028205};
DE AltName: Full=Centromeric histone CENH3 {ECO:0000303|PubMed:17028205};
DE AltName: Full=Centromeric histone H3 {ECO:0000303|PubMed:17028205};
DE AltName: Full=Histone H3-like centromeric protein HTR12 {ECO:0000303|PubMed:12034896};
GN Name=CENH3 {ECO:0000303|PubMed:17028205};
GN Synonyms=HTR12 {ECO:0000303|PubMed:12034896};
GN OrderedLocusNames=At1g01370 {ECO:0000312|Araport:AT1G01370};
GN ORFNames=F6F3.17 {ECO:0000312|EMBL:AAF97340.1};
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 [MRNA], VARIANT ALA-21, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Be-0, cv. Bu-20, cv. Columbia, cv. Fi-0, cv. Kl-0,
RC cv. Landsberg erecta, cv. Nd-1, cv. No-0, and cv. Tac-0; TISSUE=Flower;
RX PubMed=12034896; DOI=10.1105/tpc.010425;
RA Talbert P.B., Masuelli R., Tyagi A.P., Comai L., Henikoff S.;
RT "Centromeric localization and adaptive evolution of an Arabidopsis histone
RT H3 variant.";
RL Plant Cell 14:1053-1066(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Kawabe A., Nasuda S.;
RT "Histone H3-like gene of Arabidopsis species.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP IDENTIFICATION, NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=16262706; DOI=10.1111/j.1365-313x.2005.02554.x;
RA Okada T., Endo M., Singh M.B., Bhalla P.L.;
RT "Analysis of the histone H3 gene family in Arabidopsis and identification
RT of the male-gamete-specific variant AtMGH3.";
RL Plant J. 44:557-568(2005).
RN [9]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=17028205; DOI=10.1105/tpc.106.043174;
RA Lermontova I., Schubert V., Fuchs J., Klatte S., Macas J., Schubert I.;
RT "Loading of Arabidopsis centromeric histone CENH3 occurs mainly during G2
RT and requires the presence of the histone fold domain.";
RL Plant Cell 18:2443-2451(2006).
RN [10]
RP INTERACTION WITH ORTH2.
RX PubMed=17242155; DOI=10.1101/gad.1512007;
RA Woo H.R., Pontes O., Pikaard C.S., Richards E.J.;
RT "VIM1, a methylcytosine-binding protein required for centromeric
RT heterochromatinization.";
RL Genes Dev. 21:267-277(2007).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=21695238; DOI=10.1371/journal.pgen.1002121;
RA Ravi M., Shibata F., Ramahi J.S., Nagaki K., Chen C., Murata M., Chan S.W.;
RT "Meiosis-specific loading of the centromere-specific histone CENH3 in
RT Arabidopsis thaliana.";
RL PLoS Genet. 7:E1002121-E1002121(2011).
CC -!- FUNCTION: Histone H3-like variant which exclusively replaces
CC conventional H3 in the nucleosome core of centromeric chromatin at the
CC inner plate of the kinetochore. Required for recruitment and assembly
CC of kinetochore proteins, mitotic progression and chromosome
CC segregation. May serve as an epigenetic mark that propagates centromere
CC identity through replication and cell division (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms a nucleosome-like histone octamer containing two
CC molecules each of H2A, H2B, CENH3 and H4 assembled in one CENH3-H4
CC heterotetramer and two H2A-H2B heterodimers (By similarity). Interacts
CC with ORTH2. {ECO:0000250, ECO:0000269|PubMed:17242155}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:12034896, ECO:0000269|PubMed:17028205,
CC ECO:0000269|PubMed:21695238}. Note=Localizes exclusively in the
CC kinetochore domain of centromeres (PubMed:12034896, PubMed:17028205).
CC Localized at centromeres in both mitotic and meiotic cells
CC (PubMed:21695238). {ECO:0000269|PubMed:12034896,
CC ECO:0000269|PubMed:17028205, ECO:0000269|PubMed:21695238}.
CC -!- DEVELOPMENTAL STAGE: Expressed and/or deposited to centromeres during
CC G2 phase. {ECO:0000269|PubMed:17028205}.
CC -!- DOMAIN: The C-terminal histone fold domain is sufficient to direct
CC CENH3 to centromeres.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF97340.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF465800; AAL86775.1; -; mRNA.
DR EMBL; AB081500; BAC79427.1; -; mRNA.
DR EMBL; AC023628; AAF97340.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27278.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27279.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60590.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60591.1; -; Genomic_DNA.
DR EMBL; BT024771; ABD59109.1; -; mRNA.
DR EMBL; AK175840; BAD43603.1; -; mRNA.
DR EMBL; AY086361; AAM64429.1; -; mRNA.
DR PIR; B86144; B86144.
DR RefSeq; NP_001030927.1; NM_001035850.3.
DR RefSeq; NP_001322867.1; NM_001331269.1.
DR RefSeq; NP_001322868.1; NM_001331270.1.
DR RefSeq; NP_563627.1; NM_100019.2.
DR AlphaFoldDB; Q8RVQ9; -.
DR SMR; Q8RVQ9; -.
DR BioGRID; 24341; 2.
DR STRING; 3702.AT1G01370.1; -.
DR iPTMnet; Q8RVQ9; -.
DR PaxDb; Q8RVQ9; -.
DR PRIDE; Q8RVQ9; -.
DR ProteomicsDB; 232176; -.
DR EnsemblPlants; AT1G01370.1; AT1G01370.1; AT1G01370.
DR EnsemblPlants; AT1G01370.2; AT1G01370.2; AT1G01370.
DR EnsemblPlants; AT1G01370.3; AT1G01370.3; AT1G01370.
DR EnsemblPlants; AT1G01370.4; AT1G01370.4; AT1G01370.
DR GeneID; 839104; -.
DR Gramene; AT1G01370.1; AT1G01370.1; AT1G01370.
DR Gramene; AT1G01370.2; AT1G01370.2; AT1G01370.
DR Gramene; AT1G01370.3; AT1G01370.3; AT1G01370.
DR Gramene; AT1G01370.4; AT1G01370.4; AT1G01370.
DR KEGG; ath:AT1G01370; -.
DR Araport; AT1G01370; -.
DR TAIR; locus:2035252; AT1G01370.
DR eggNOG; KOG1745; Eukaryota.
DR HOGENOM; CLU_078295_3_0_1; -.
DR InParanoid; Q8RVQ9; -.
DR OMA; ISHFYAP; -.
DR OrthoDB; 1564596at2759; -.
DR PhylomeDB; Q8RVQ9; -.
DR PRO; PR:Q8RVQ9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RVQ9; baseline and differential.
DR Genevisible; Q8RVQ9; AT.
DR GO; GO:0000785; C:chromatin; IDA:TAIR.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:TAIR.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0034508; P:centromere complex assembly; IMP:TAIR.
DR GO; GO:0009567; P:double fertilization forming a zygote and endosperm; IEP:TAIR.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:TAIR.
DR GO; GO:0051307; P:meiotic chromosome separation; IMP:TAIR.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Acetylation; Centromere; Chromosome; DNA-binding; Kinetochore; Methylation;
KW Nucleosome core; Phosphoprotein; Reference proteome.
FT CHAIN 1..178
FT /note="Histone H3-like centromeric protein CENH3"
FT /id="PRO_0000264610"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 63
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 63
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 75
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 75
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 75
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT VARIANT 21
FT /note="G -> A (in strain: cv. Be-0, cv. Kl-0, cv. Tac-0 and
FT cv. Wassilewskija)"
FT /evidence="ECO:0000269|PubMed:12034896"
FT CONFLICT 132
FT /note="A -> S (in Ref. 7; AAM64429)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 178 AA; 19709 MW; D19826721CF6202E CRC64;
MARTKHRVTR SQPRNQTDAA GASSSQAAGP TTTPTRRGGE GGDNTQQTNP TTSPATGTRR
GAKRSRQAMP RGSQKKSYRY RPGTVALKEI RHFQKQTNLL IPAASFIREV RSITHMLAPP
QINRWTAEAL VALQEAAEDY LVGLFSDSML CAIHARRVTL MRKDFELARR LGGKGRPW
