CAF1A_MOUSE
ID CAF1A_MOUSE Reviewed; 911 AA.
AC Q9QWF0; Q3TU22; Q544M2;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Chromatin assembly factor 1 subunit A {ECO:0000305};
DE Short=CAF-1 subunit A;
DE AltName: Full=Chromatin assembly factor I p150 subunit;
DE Short=CAF-I 150 kDa subunit;
DE Short=CAF-I p150;
GN Name=Chaf1a {ECO:0000312|MGI:MGI:1351331}; Synonyms=Caip150;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS, AND INTERACTION WITH HP1 PROTEINS.
RX PubMed=10549285; DOI=10.1016/s1097-2765(00)80204-x;
RA Murzina N.V., Verreault A., Laue E.D., Stillman B.;
RT "Heterochromatin dynamics in mouse cells: interaction between chromatin
RT assembly factor 1 and HP1 proteins.";
RL Mol. Cell 4:529-540(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH MBD1.
RX PubMed=12697822; DOI=10.1128/mcb.23.9.3226-3236.2003;
RA Reese B.E., Bachman K.E., Baylin S.B., Rountree M.R.;
RT "The methyl-CpG binding protein MBD1 interacts with the p150 subunit of
RT chromatin assembly factor 1.";
RL Mol. Cell. Biol. 23:3226-3236(2003).
CC -!- FUNCTION: Core component of the CAF-1 complex, a complex that is
CC thought to mediate chromatin assembly in DNA replication and DNA
CC repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1
CC performs the first step of the nucleosome assembly process, bringing
CC newly synthesized histones H3 and H4 to replicating DNA; histones
CC H2A/H2B can bind to this chromatin precursor subsequent to DNA
CC replication to complete the histone octamer. It may play a role in
CC heterochromatin maintenance in proliferating cells by bringing newly
CC synthesized cbx proteins to heterochromatic DNA replication foci.
CC {ECO:0000250|UniProtKB:Q5R1T0}.
CC -!- SUBUNIT: Homodimer. Part of the CAF-1 complex that contains RBBP4,
CC CHAF1B and CHAF1A. CHAF1A binds directly to CHAF1B. Only minor amounts
CC of RBBP4 are complexed with CHAF1A and CHAF1B in G1 phase. CHAF1A binds
CC directly to PCNA and to CBX1. Interacts with MBD1. Interacts directly
CC with CBX5 via the PxVxL motif. Interacts with CBX5. Interacts with
CC histones H3.1, H3.2 and H3.1t (By similarity).
CC {ECO:0000250|UniProtKB:Q13111}.
CC -!- INTERACTION:
CC Q9QWF0; P83917: Cbx1; NbExp=3; IntAct=EBI-639217, EBI-78119;
CC Q9QWF0; P70338: Gfi1; NbExp=5; IntAct=EBI-639217, EBI-3954754;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13111}. Note=DNA
CC replication foci. {ECO:0000250|UniProtKB:Q13111}.
CC -!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
CC required for interaction with chromoshadow domains. This motif requires
CC additional residues -7, -6, +4 and +5 of the central Val which contact
CC the chromoshadow domain.
CC -!- SIMILARITY: Belongs to the CHAF1A family. {ECO:0000305}.
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DR EMBL; AJ132771; CAB55497.2; -; mRNA.
DR EMBL; AK034839; BAC28848.1; -; mRNA.
DR EMBL; AK161016; BAE36149.1; -; mRNA.
DR EMBL; CH466559; EDL23708.1; -; Genomic_DNA.
DR EMBL; BC053740; AAH53740.1; -; mRNA.
DR CCDS; CCDS28892.1; -.
DR RefSeq; NP_038761.1; NM_013733.3.
DR PDB; 1S4Z; NMR; -; C=210-238.
DR PDBsum; 1S4Z; -.
DR AlphaFoldDB; Q9QWF0; -.
DR SMR; Q9QWF0; -.
DR BioGRID; 205142; 163.
DR ComplexPortal; CPX-570; Chromatin assembly factor 1 complex.
DR ELM; Q9QWF0; -.
DR IntAct; Q9QWF0; 17.
DR STRING; 10090.ENSMUSP00000002914; -.
DR iPTMnet; Q9QWF0; -.
DR PhosphoSitePlus; Q9QWF0; -.
DR EPD; Q9QWF0; -.
DR jPOST; Q9QWF0; -.
DR MaxQB; Q9QWF0; -.
DR PaxDb; Q9QWF0; -.
DR PeptideAtlas; Q9QWF0; -.
DR PRIDE; Q9QWF0; -.
DR ProteomicsDB; 265501; -.
DR Antibodypedia; 4198; 243 antibodies from 33 providers.
DR DNASU; 27221; -.
DR Ensembl; ENSMUST00000002914; ENSMUSP00000002914; ENSMUSG00000002835.
DR GeneID; 27221; -.
DR KEGG; mmu:27221; -.
DR UCSC; uc008dar.1; mouse.
DR CTD; 10036; -.
DR MGI; MGI:1351331; Chaf1a.
DR VEuPathDB; HostDB:ENSMUSG00000002835; -.
DR eggNOG; KOG4364; Eukaryota.
DR GeneTree; ENSGT00440000034888; -.
DR HOGENOM; CLU_014846_0_0_1; -.
DR InParanoid; Q9QWF0; -.
DR OMA; CKWTYLT; -.
DR OrthoDB; 1362011at2759; -.
DR PhylomeDB; Q9QWF0; -.
DR TreeFam; TF350377; -.
DR BioGRID-ORCS; 27221; 14 hits in 112 CRISPR screens.
DR ChiTaRS; Chaf1a; mouse.
DR EvolutionaryTrace; Q9QWF0; -.
DR PRO; PR:Q9QWF0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9QWF0; protein.
DR Bgee; ENSMUSG00000002835; Expressed in primary oocyte and 90 other tissues.
DR ExpressionAtlas; Q9QWF0; baseline and differential.
DR GO; GO:0033186; C:CAF-1 complex; ISS:UniProtKB.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0070087; F:chromo shadow domain binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0031497; P:chromatin assembly; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; ISO:MGI.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR IDEAL; IID50294; -.
DR InterPro; IPR029105; CAF1-p150_C2.
DR InterPro; IPR029091; CAF1_p150_N.
DR InterPro; IPR022043; CAF1A.
DR Pfam; PF15539; CAF1-p150_C2; 1.
DR Pfam; PF15557; CAF1-p150_N; 1.
DR Pfam; PF12253; CAF1A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Chaperone; DNA damage; DNA repair;
KW DNA replication; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..911
FT /note="Chromatin assembly factor 1 subunit A"
FT /id="PRO_0000089277"
FT REGION 1..31
FT /note="Binds PCNA"
FT /evidence="ECO:0000250"
FT REGION 166..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..327
FT /note="Binds CBX1 and CBX3 chromo shadow domains"
FT REGION 250..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..657
FT /note="Necessary for homodimerization and competence for
FT chromatin assembly"
FT /evidence="ECO:0000250"
FT REGION 639..911
FT /note="Binds to p60"
FT /evidence="ECO:0000250"
FT REGION 819..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 217..230
FT /note="PxVxL motif"
FT COMPBIAS 183..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..612
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT MOD_RES 838
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT MUTAGEN 224
FT /note="V->N,E: Prevents binding to CBX1 and CBX5."
FT /evidence="ECO:0000269|PubMed:10549285"
FT MUTAGEN 224
FT /note="V->S,D: Prevents binding to CBX1 and CBX5."
FT /evidence="ECO:0000269|PubMed:10549285"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1S4Z"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1S4Z"
SQ SEQUENCE 911 AA; 101936 MW; 67B3340010425C95 CRC64;
MLEEPEAATR TAAAVDCKDR PGFPVKRLIQ ARLPFKRLNL VPKEKVEEDT SPKAAVESKV
PDLQLSLGTF ESQCHTGSHV GLSTKLVGGQ GPIDSFLRAT IKPVPSVVII DLTENCSDIP
DSPEGHSELS PDTAGVVTTV EGAAKQQEHS AAELCLLETP SDITCHMEEE PGSPGDPKRT
GDCQAGSLQS CPELTPGSRT CPTKELSSWS KAGDLLFIEK VPVVVLEDIL ATKPSIASLP
MMSLDRSVTS ESEILESCPE DDSILSHSST NSSSPTSSPE GPSTPPEHRG GRSSPSTPAC
RVAKNFVKGS TEKGRSKLHR DREQQREEKE KLREEIRRAK EEARKKKEEE KELKEKERRE
KREKDEKEKA EKQRLKEEKR KERQEALEAK LEEKRKKEEE KRLREEEKRL REEEKRIKAE
KAEITRFFQK PKTPQAPKTL AGSCGKFAPF EIKEHMVLAP RCRAALDQDL CDQLDQLLQQ
QSVASTFLSD LKSRLPLRSG PTRVCGHDTD IMNRDVVIVE SSKVDGVSER KKFGRMKLLQ
FSENHRPAYW GTWNKKTAII RPRNPWAQDK DLLDYEVDSD DEWEEEEPGE SLSHSEGDED
DDVGEDEDED DGFFVPHGYL SEDEGVTEEC ADPENHKVHQ KLKAKEWDEL LAKGKRFRVL
QPVHVGCVWA SEAANCTSSD LKLLQQFTAC LLDVASPDEP EPGASRREKR DQHILAQLLP
LLHGNVNGSK VIIHEFQEQC RRGLLTLPSP TPHLQMPNLE DAVAVPSKAR LKRLISENSA
YEKRPNFRMC WYVHPEVLKS FGQECLPVPC QWTYITTMPS APREDSGSAS TEGPGQSTPM
LLKRKPAATM CITQFMKKRR YDGQVGSGDM DGFQADTEED EEDDTDCMII DVPDVGSDVS
EAPIPAPTLC K
