FAS1_ARATH
ID FAS1_ARATH Reviewed; 815 AA.
AC Q9SXY0; O04466; O80817;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Chromatin assembly factor 1 subunit FAS1;
DE Short=CAF-1 subunit FAS1;
DE AltName: Full=CAF-1 p150 homolog;
DE AltName: Full=Protein FASCIATA 1;
GN Name=FAS1; Synonyms=NFB2; OrderedLocusNames=At1g65470;
GN ORFNames=F5I14.2, T8F5.24;
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 [GENOMIC DNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11163246; DOI=10.1016/s0092-8674(01)00197-0;
RA Kaya H., Shibahara K., Taoka K., Iwabuchi M., Stillman B., Araki T.;
RT "FASCIATA genes for chromatin assembly factor-1 in Arabidopsis maintain the
RT cellular organization of apical meristems.";
RL Cell 104:131-142(2001).
RN [2]
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 [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=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).
RN [5]
RP FUNCTION.
RX PubMed=17021044; DOI=10.1242/dev.02599;
RA Exner V., Taranto P., Schoenrock N., Gruissem W., Hennig L.;
RT "Chromatin assembly factor CAF-1 is required for cellular differentiation
RT during plant development.";
RL Development 133:4163-4172(2006).
RN [6]
RP FUNCTION.
RX PubMed=17110925; DOI=10.1038/sj.emboj.7601434;
RA Endo M., Ishikawa Y., Osakabe K., Nakayama S., Kaya H., Araki T.,
RA Shibahara K., Abe K., Ichikawa H., Valentine L., Hohn B., Toki S.;
RT "Increased frequency of homologous recombination and T-DNA integration in
RT Arabidopsis CAF-1 mutants.";
RL EMBO J. 25:5579-5590(2006).
RN [7]
RP FUNCTION.
RX PubMed=16452472; DOI=10.1074/jbc.m513426200;
RA Schoenrock N., Exner V., Probst A., Gruissem W., Hennig L.;
RT "Functional genomic analysis of CAF-1 mutants in Arabidopsis thaliana.";
RL J. Biol. Chem. 281:9560-9568(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. C24;
RX PubMed=16980538; DOI=10.1105/tpc.106.045088;
RA Kirik A., Pecinka A., Wendeler E., Reiss B.;
RT "The chromatin assembly factor subunit FASCIATA1 is involved in homologous
RT recombination in plants.";
RL Plant Cell 18:2431-2442(2006).
RN [9]
RP FUNCTION.
RX PubMed=17351056; DOI=10.1104/pp.106.094979;
RA Ramirez-Parra E., Gutierrez C.;
RT "E2F regulates FASCIATA1, a chromatin assembly gene whose loss switches on
RT the endocycle and activates gene expression by changing the epigenetic
RT status.";
RL Plant Physiol. 144:105-120(2007).
RN [10]
RP FUNCTION.
RX PubMed=18045841; DOI=10.1242/dev.010108;
RA Chen Z., Tan J.L., Ingouff M., Sundaresan V., Berger F.;
RT "Chromatin assembly factor 1 regulates the cell cycle but not cell fate
RT during male gametogenesis in Arabidopsis thaliana.";
RL Development 135:65-73(2008).
RN [11]
RP FUNCTION.
RX PubMed=20699390; DOI=10.1105/tpc.110.076182;
RA Mozgova I., Mokros P., Fajkus J.;
RT "Dysfunction of chromatin assembly factor 1 induces shortening of telomeres
RT and loss of 45S rDNA in Arabidopsis thaliana.";
RL Plant Cell 22:2768-2780(2010).
RN [12]
RP INTERACTION WITH CYP71.
RX PubMed=21596687; DOI=10.1093/mp/ssr036;
RA Li H., Luan S.;
RT "The cyclophilin AtCYP71 interacts with CAF-1 and LHP1 and functions in
RT multiple chromatin remodeling processes.";
RL Mol. Plant 4:748-758(2011).
CC -!- FUNCTION: Component of the chromatin assembly factor complex (CAF-1)
CC involved in chromatin assembly following DNA replication and DNA
CC repair. Assembles histone octamers onto replicating DNA in vitro.
CC Required for several aspects of development, including seedling growth
CC and leaf hair differentiation. Plays a critical role in the
CC organization of shoot apical meristem (SAM) and root apical meristem
CC (RAM) during postembryonic development by facilitating stable
CC maintenance of gene expression states. Seems not required to maintain
CC transcriptional repression of heterochromatic genes. Involved in
CC heterologous recombination. May repress endocycle.
CC {ECO:0000269|PubMed:11163246, ECO:0000269|PubMed:16452472,
CC ECO:0000269|PubMed:16980538, ECO:0000269|PubMed:17021044,
CC ECO:0000269|PubMed:17110925, ECO:0000269|PubMed:17351056,
CC ECO:0000269|PubMed:18045841, ECO:0000269|PubMed:20699390}.
CC -!- SUBUNIT: Component of the chromatin assembly factor 1 (CAF-1) complex,
CC composed of FAS1, FAS2 and MSI1. Interacts with CYP71.
CC {ECO:0000269|PubMed:11163246, ECO:0000269|PubMed:21596687}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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=Q9SXY0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in the shoot apical meristem, young leaf
CC primordia, root tip and first lateral root primordium at the
CC hypocotyl/root junction. {ECO:0000269|PubMed:11163246}.
CC -!- INDUCTION: Cell cycle-regulated, showing a peak in the S-phase.
CC {ECO:0000269|PubMed:11163246}.
CC -!- DISRUPTION PHENOTYPE: Fasciated plants with broad, flat stems and
CC disrupted phyllotaxy. Shoot apical meristem enlargement and altered
CC floral development. Reduced heterochromatin content, more open
CC conformation of euchromatin and dramatic increase of homologous
CC recombination. {ECO:0000269|PubMed:11163246,
CC ECO:0000269|PubMed:16980538}.
CC -!- SIMILARITY: Belongs to the CHAF1A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB60903.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC27156.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB027229; BAA77811.1; -; Genomic_DNA.
DR EMBL; AC001229; AAB60903.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC004512; AAC27156.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34379.1; -; Genomic_DNA.
DR EMBL; AY126994; AAM83221.1; -; mRNA.
DR PIR; E96679; E96679.
DR PIR; F96679; F96679.
DR PIR; T02369; T02369.
DR RefSeq; NP_176725.1; NM_105221.3. [Q9SXY0-1]
DR AlphaFoldDB; Q9SXY0; -.
DR SMR; Q9SXY0; -.
DR BioGRID; 28079; 2.
DR STRING; 3702.AT1G65470.1; -.
DR PaxDb; Q9SXY0; -.
DR PRIDE; Q9SXY0; -.
DR ProteomicsDB; 230958; -. [Q9SXY0-1]
DR EnsemblPlants; AT1G65470.1; AT1G65470.1; AT1G65470. [Q9SXY0-1]
DR GeneID; 842858; -.
DR Gramene; AT1G65470.1; AT1G65470.1; AT1G65470. [Q9SXY0-1]
DR KEGG; ath:AT1G65470; -.
DR Araport; AT1G65470; -.
DR TAIR; locus:2034183; AT1G65470.
DR eggNOG; KOG4364; Eukaryota.
DR InParanoid; Q9SXY0; -.
DR OMA; SETALWC; -.
DR OrthoDB; 438497at2759; -.
DR PhylomeDB; Q9SXY0; -.
DR PRO; PR:Q9SXY0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SXY0; baseline and differential.
DR Genevisible; Q9SXY0; AT.
DR GO; GO:0033186; C:CAF-1 complex; IPI:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; ISS:TAIR.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0006325; P:chromatin organization; IDA:TAIR.
DR GO; GO:0006310; P:DNA recombination; IMP:TAIR.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:TAIR.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
DR GO; GO:0006334; P:nucleosome assembly; IDA:TAIR.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0045787; P:positive regulation of cell cycle; IGI:TAIR.
DR GO; GO:0009934; P:regulation of meristem structural organization; IMP:TAIR.
DR GO; GO:0010026; P:trichome differentiation; IMP:TAIR.
DR InterPro; IPR022043; CAF1A.
DR Pfam; PF12253; CAF1A; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Coiled coil; DNA damage;
KW DNA repair; DNA replication; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..815
FT /note="Chromatin assembly factor 1 subunit FAS1"
FT /id="PRO_0000420143"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 244..336
FT /evidence="ECO:0000255"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..568
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 815 AA; 93347 MW; 023C01421D0F6017 CRC64;
MDEVSTVNEN ENRKTMIEPK KLNKRKREPT AIENLTSEEK ESQISSLNLE MKGLFDYFRE
VMDKSKRTDL FSGFSECSSL NSMVALLMEE MSLPLSKLVD EIYLKLKEKT ESVTMVAVKS
AVVSVGQRVS YGVLNVDADV LEDDSESCLW CWETRDLKIM PSSVRGVLKL RRTCRKKIHE
RITAVSAMLA ALQREETEKL WRSDLSKAAE KLGKILSEVD IRSFMDNMMQ KNSSEMAEKD
SKREEKLLLK QLEKNRCEAE KEKKRMERQV LKEKLQQEKE QKLLQKAIVD ENNKEKEETE
SRKRIKKQQD ESEKEQKRRE KEQAELKKQL QVQKQASIME RFLKKSKDSS LTQPKLPSSE
VTAQELSCTK HENEIGKVVQ AIDNAFSTTC EATVDDIRRE HFASWRQLGH LLSSSKKHWG
MRRQPKSELF PKLKLSTNSG VTSDGEPNME KQGDGCEENN FDGRQCKPSS SNRKKSRRVK
QLLQFDKSCR PGFYGIWPSQ SQVVKPRRPL QKDPELDYEV DSDEEWEEEE AGESLSDCEK
DEDESLEEGC SKADDEDDSE DDFMVPDGYL SEDEGVQVDR MDIDPSEQDA NTTSSKQDQE
SPEFCALLQQ QKHLQNLTDH ALKKTQPLII CNLTHEKVSL LAAKDLEGTQ KVEQICLRAL
MVRQFPWSSL IEISINDIQD EDQEASKFSC SQSTPPSNSK AKIIPDSDLL TVVSTIQSCS
QGINRVVETL QQKFPDVPKT KLRQKVREIS DFEDSRWQVK KEVLTKLGLS PSPDKGGKRL
PKTISTFFSK RCLPPSTKPQ PAVEDAAERL ENENA
