CTF7_ARATH
ID CTF7_ARATH Reviewed; 345 AA.
AC A7UL74; O49589;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Protein CHROMOSOME TRANSMISSION FIDELITY 7 {ECO:0000303|PubMed:10617198, ECO:0000303|PubMed:20671110};
DE EC=2.3.1.-;
DE AltName: Full=Cohesion establishment factor CTF7 {ECO:0000303|PubMed:10617198, ECO:0000303|PubMed:20671110};
DE AltName: Full=Protein ESTABLISHMENT OF COHESION 1 {ECO:0000303|PubMed:10617198};
GN Name=CTF7 {ECO:0000303|PubMed:10617198, ECO:0000303|PubMed:20671110};
GN Synonyms=ECO1 {ECO:0000303|PubMed:10617198};
GN OrderedLocusNames=At4g31400 {ECO:0000312|Araport:AT4G31400};
GN ORFNames=F3L17.7;
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], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, ACETYLATION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija; TISSUE=Flower bud;
RX PubMed=20671110; DOI=10.1104/pp.110.157560;
RA Jiang L., Yuan L., Xia M., Makaroff C.A.;
RT "Proper levels of the Arabidopsis cohesion establishment factor CTF7 are
RT essential for embryo and megagametophyte, but not endosperm, development.";
RL Plant Physiol. 154:820-832(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=23750584; DOI=10.1111/tpj.12261;
RA Bolanos-Villegas P., Yang X., Wang H.J., Juan C.T., Chuang M.H.,
RA Makaroff C.A., Jauh G.Y.;
RT "Arabidopsis CHROMOSOME TRANSMISSION FIDELITY 7 (AtCTF7/ECO1) is required
RT for DNA repair, mitosis and meiosis.";
RL Plant J. 75:927-940(2013).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=26813623; DOI=10.1105/tpc.15.00781;
RA De K., Bolanos-Villegas P., Mitra S., Yang X., Homan G., Jauh G.-Y.,
RA Makaroff C.A.;
RT "The Opposing Actions of Arabidopsis CHROMOSOME TRANSMISSION FIDELITY7 and
RT WINGS APART-LIKE1 and 2 Differ in Mitotic and Meiotic Cells.";
RL Plant Cell 28:521-536(2016).
CC -!- FUNCTION: Acetyltransferase required for the establishment of sister
CC chromatid cohesion (PubMed:20671110). Involved in preservation of
CC genome integrity and meiosis (PubMed:23750584, PubMed:20671110).
CC Required for DNA repair and for the regulation of chromosome
CC segregation during mitotic cell division (PubMed:23750584,
CC PubMed:20671110). Knock-down mutants are extremely dwarf
CC (PubMed:20671110). Regulator of sister chromatid cohesion in meiosis
CC which negatively regulates cohesin association with chromatin, acting
CC as an antagonist of WAPL1 and WAPL2 (PubMed:26813623).
CC {ECO:0000269|PubMed:20671110, ECO:0000269|PubMed:23750584,
CC ECO:0000269|PubMed:26813623}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20671110}. Cytoplasm
CC {ECO:0000269|PubMed:20671110}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, young seedlings
CC and flower buds. Detected in the embryo, but not in the endosperm.
CC {ECO:0000269|PubMed:20671110}.
CC -!- PTM: Autoacetylated. {ECO:0000269|PubMed:20671110}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality, but normal endosperm
CC development (PubMed:20671110). No effect on pollen mitosis but minor
CC alterations in female gametophyte development (PubMed:20671110).
CC Defective microsporangenesis and anthesis (PubMed:20671110). Major
CC defects in vegetative growth and development, as well as complete
CC sterility; these phenotypes are partially restored in plants also
CC missing WAPL1 and WAPL2 (PubMed:26813623).
CC {ECO:0000269|PubMed:20671110, ECO:0000269|PubMed:26813623}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16543.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79858.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EU077499; ABU62813.1; -; mRNA.
DR EMBL; AL021633; CAA16543.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161578; CAB79858.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85905.1; -; Genomic_DNA.
DR PIR; T04507; T04507.
DR RefSeq; NP_194868.2; NM_119289.3.
DR AlphaFoldDB; A7UL74; -.
DR SMR; A7UL74; -.
DR STRING; 3702.AT4G31400.1; -.
DR iPTMnet; A7UL74; -.
DR PaxDb; A7UL74; -.
DR PRIDE; A7UL74; -.
DR ProteomicsDB; 222699; -.
DR EnsemblPlants; AT4G31400.1; AT4G31400.1; AT4G31400.
DR GeneID; 829267; -.
DR Gramene; AT4G31400.1; AT4G31400.1; AT4G31400.
DR KEGG; ath:AT4G31400; -.
DR Araport; AT4G31400; -.
DR TAIR; locus:2128126; AT4G31400.
DR eggNOG; KOG3014; Eukaryota.
DR HOGENOM; CLU_039183_1_0_1; -.
DR InParanoid; A7UL74; -.
DR OMA; AQYHLEL; -.
DR OrthoDB; 1138803at2759; -.
DR PhylomeDB; A7UL74; -.
DR PRO; PR:A7UL74; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; A7UL74; baseline and differential.
DR Genevisible; A7UL74; AT.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0016407; F:acetyltransferase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0048653; P:anther development; IMP:TAIR.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0080186; P:developmental vegetative growth; IMP:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0034089; P:establishment of meiotic sister chromatid cohesion; IMP:TAIR.
DR GO; GO:0060772; P:leaf phyllotactic patterning; IMP:TAIR.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:TAIR.
DR GO; GO:0045144; P:meiotic sister chromatid segregation; IMP:UniProtKB.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:TAIR.
DR GO; GO:0048609; P:multicellular organismal reproductive process; IMP:TAIR.
DR GO; GO:0071922; P:regulation of cohesin loading; IMP:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0007062; P:sister chromatid cohesion; IMP:TAIR.
DR InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR028009; ESCO_Acetyltransf_dom.
DR Pfam; PF13880; Acetyltransf_13; 1.
DR Pfam; PF13878; zf-C2H2_3; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Cell cycle; Cell division; Cytoplasm;
KW Meiosis; Metal-binding; Mitosis; Nucleus; Reference proteome; Transferase;
KW Zinc; Zinc-finger.
FT CHAIN 1..345
FT /note="Protein CHROMOSOME TRANSMISSION FIDELITY 7"
FT /id="PRO_0000423619"
FT ZN_FING 96..120
FT /note="CCHH-type"
FT /evidence="ECO:0000255"
SQ SEQUENCE 345 AA; 38988 MW; D96EF0BE5345A8FC CRC64;
MQAKINSFFK PSSSSSIAAS VTTDTDDGLA VWENNRNAIV NTYQRRSAIT ERSEVLKGCI
EKTLKKGSSS VPKNHKKKRN YTQFHLELGQ SDFLLRHCAE CGAKYAPGDE LDEKNHQSFH
KDYMYGLPFK GWQNEKAFTS PLFIKNRIVM VSENDSPAHR NKVQEVVKMM EVELGEDWIL
HQHCKVYLFI SSQRISGCLV AEPIKEAFKL IASPDDERQL QKESSSSPST SIQFGNIVLQ
REVSKRCRTS DDRLDNGVIV CEEEAKPAVC GIRAIWVSPS NRRKGIATWL LDTTRESFCN
NGCMLEKSQL AFSQPSSIGR SFGSKYFGTC SFLLYKAQLI DTHFS
