MCC1_ARATH
ID MCC1_ARATH Reviewed; 247 AA.
AC Q9M8T9;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Histone acetyltransferase MCC1;
DE EC=2.3.1.48;
DE AltName: Full=Protein MEIOTIC CONTROL OF CROSSOVERS 1;
GN Name=MCC1; OrderedLocusNames=At3g02980; ORFNames=F13E7.7;
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], AND FUNCTION.
RX PubMed=20230492; DOI=10.1111/j.1365-313x.2010.04191.x;
RA Perrella G., Consiglio M.F., Aiese-Cigliano R., Cremona G.,
RA Sanchez-Moran E., Barra L., Errico A., Bressan R.A., Franklin F.C.,
RA Conicella C.;
RT "Histone hyperacetylation affects meiotic recombination and chromosome
RT segregation in Arabidopsis.";
RL Plant J. 62:796-806(2010).
RN [2]
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 [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).
CC -!- FUNCTION: Histone acetyltransferase that probably regulates acetylation
CC status of histone H3 during meiosis. Histone acetylation may influence
CC recombination and chromosome segregation.
CC {ECO:0000269|PubMed:20230492}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC -!- MISCELLANEOUS: The gain-of-function mutant mcc1 (T-DNA tagging) has
CC elongated rosette leaves, increased stem length elongation, early
CC flowering and reduced fertility and seed number due to defects in
CC meiosis. {ECO:0000305|PubMed:20230492}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; EU598461; ACF05703.1; -; mRNA.
DR EMBL; AC018363; AAF26961.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73887.1; -; Genomic_DNA.
DR RefSeq; NP_186948.1; NM_111168.2.
DR AlphaFoldDB; Q9M8T9; -.
DR SMR; Q9M8T9; -.
DR STRING; 3702.AT3G02980.1; -.
DR PaxDb; Q9M8T9; -.
DR PRIDE; Q9M8T9; -.
DR ProteomicsDB; 238818; -.
DR EnsemblPlants; AT3G02980.1; AT3G02980.1; AT3G02980.
DR GeneID; 821166; -.
DR Gramene; AT3G02980.1; AT3G02980.1; AT3G02980.
DR KEGG; ath:AT3G02980; -.
DR Araport; AT3G02980; -.
DR TAIR; locus:2075467; AT3G02980.
DR eggNOG; KOG3138; Eukaryota.
DR HOGENOM; CLU_013985_5_0_1; -.
DR InParanoid; Q9M8T9; -.
DR OMA; SEFFQCV; -.
DR OrthoDB; 1619974at2759; -.
DR PhylomeDB; Q9M8T9; -.
DR PRO; PR:Q9M8T9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M8T9; baseline and differential.
DR Genevisible; Q9M8T9; AT.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0043966; P:histone H3 acetylation; IMP:TAIR.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:TAIR.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR045141; NAA60-like.
DR PANTHER; PTHR14744; PTHR14744; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Chromatin regulator; Chromosome partition; Meiosis;
KW Reference proteome; Transferase.
FT CHAIN 1..247
FT /note="Histone acetyltransferase MCC1"
FT /id="PRO_0000423405"
FT DOMAIN 25..198
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 247 AA; 28306 MW; 05374712546E00DA CRC64;
MSRFPRRFID DSSMEDAGIS LCPSIHYRPI NPNDLDRLEQ IHRDIFPIKY ESEFFQSVVN
GVDIVSWAAV DRSRPDDHSD ELIGFVTAKF VLAKDSEIDD LIHYDSSKGE ETLIYILTLG
VVETYRNRGI AMSLISEVIK YASGLSVCRG VYLHVIAHNN AAICLYKRLM FRCVRRLHGF
YLINRHHFDA FLFVYFINGS RTPCSPLEVA MFVVNYMKSG IKSVASKLAN KDEKGLKWLF
CKDTDCV
