CAF1A_BOVIN
ID CAF1A_BOVIN Reviewed; 964 AA.
AC A6QLA6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Chromatin assembly factor 1 subunit A;
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; Synonyms=CAF, CAF1P150;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CHAF1A family. {ECO:0000305}.
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DR EMBL; BC147896; AAI47897.1; -; mRNA.
DR RefSeq; NP_001095312.1; NM_001101842.2.
DR AlphaFoldDB; A6QLA6; -.
DR STRING; 9913.ENSBTAP00000010763; -.
DR PaxDb; A6QLA6; -.
DR PRIDE; A6QLA6; -.
DR GeneID; 504535; -.
DR KEGG; bta:504535; -.
DR CTD; 10036; -.
DR eggNOG; KOG4364; Eukaryota.
DR HOGENOM; CLU_014846_0_0_1; -.
DR InParanoid; A6QLA6; -.
DR OrthoDB; 1362011at2759; -.
DR TreeFam; TF350377; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0033186; C:CAF-1 complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0006334; P:nucleosome assembly; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell cycle; Chaperone; Coiled coil; DNA damage; DNA repair;
KW DNA replication; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..964
FT /note="Chromatin assembly factor 1 subunit A"
FT /id="PRO_0000373881"
FT REGION 1..316
FT /note="Binds to CBX1 chromo shadow domain"
FT /evidence="ECO:0000250"
FT REGION 1..49
FT /note="Binds to PCNA"
FT /evidence="ECO:0000250"
FT REGION 146..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..680
FT /note="Necessary for homodimerization and competence for
FT chromatin assembly"
FT REGION 662..964
FT /note="Binds to p60"
FT /evidence="ECO:0000250"
FT REGION 769..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 329..453
FT /evidence="ECO:0000255"
FT MOTIF 236..249
FT /note="PxVxL motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 154..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..635
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT MOD_RES 723
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT MOD_RES 811
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT MOD_RES 959
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13111"
SQ SEQUENCE 964 AA; 107258 MW; CE457E41928CD6DB CRC64;
MLEEPECGAP GARGEAAAMD CKDRPAFPVK KLIQARLPFK RLNLVPKEKI DDGLDDTGGS
RAGPVQTQLH NLETSLDHLE NCHMGSDIDF RPKLVNGKGP LDNFLRSQVE TSIGQAVVII
DLTEDSSNPP DNMVGHNKLN SAASSAQKNI NGVPDKAGDD RGLPKARQKD ELASPEEALS
EVPCKTEAGG ADSGGADRRG LTQRGSPQNC PKLTGDLSMW SEKDRDGWSE AGGILFKGKM
PVVVLQDILA LRPPARSPPA TPPSQAVPSE SETPESSPEE DLALSHSSLS SSSPTSSPEG
QSVPTKLHTG PSPFPASTPV CRITKKLVRG SAEKNKMKLQ RDKERLRRQL KLRAEKEEKE
KLREEAKRAK EEARKKREEE KELKEKERRE KREKDEKEKA EKQRLKEERR KERQEALEAK
LEEKRKKEEE KRLREEEKRI KAEKAEITRF FQKPKTPQAP KTLAGSCGKF APFEIKEHMV
LAPRCRTAFD QDLCDQLDQL LQQQSSEFSF LQDLKSRRPL RSGPTVVSNR NTDLSNSDVV
IVESSKVDGV PERRKFGRMK LLQFSENHRP AYWGTWNKKT TVIRPRDPWA QDRDLLDYEV
DSDEEWEEEE PGESLSHSEG DDDDDVGEDE DEDDGFFVPH GYLSEDEGVT EECADPENHK
VRQKLKAKEW DEFLAKGKRF RILQPVKIGC IWAADKDGGA DLKVLQQFTA CLLETVPPEE
EQTPKASKRE KRDQQILAQL LPLLHGNVNG SKVIIREFQE CCRRGLLSRD AGSPEDSAAS
PPSPGPARPQ TPTASEDVAV PSKARLKRII SENSVYEKRP DFRMCWYVHP QVLKSFAQEH
LPVPCQWSYV TAVPSATRED SGSVPAPGPG QGMPVSLKRK SAGSMCITQF MKKRRHDGQV
GTGDLDDFQA DTEEEDDDEG DCVIMDISDV GDIQAPCGTT SGAGGSVGMD TSESFVSPSS
LRLS
