ID   NAP1A_TOBAC             Reviewed;         374 AA.
AC   Q70Z19;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Nucleosome assembly protein 1;1;
DE            Short=NtNAP1;1;
DE   AltName: Full=Nucleosome assembly protein 1-like 1;
DE            Short=NtNAP1_L1;
DE   Flags: Precursor;
GN   Name=NAP1;1; Synonyms=NAP1_L1;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. Bright Yellow 2;
RX   PubMed=12569397; DOI=10.1007/s00425-002-0910-6;
RA   Dong A., Zhu Y., Yu Y., Cao K., Sun C., Shen W.H.;
RT   "Regulation of biosynthesis and intracellular localization of rice and
RT   tobacco homologues of nucleosome assembly protein 1.";
RL   Planta 216:561-570(2003).
RN   [2]
RP   INTERACTION WITH CYCB1;1, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=15980199; DOI=10.1104/pp.105.060509;
RA   Dong A., Liu Z., Zhu Y., Yu F., Li Z., Cao K., Shen W.H.;
RT   "Interacting proteins and differences in nuclear transport reveal specific
RT   functions for the NAP1 family proteins in plants.";
RL   Plant Physiol. 138:1446-1456(2005).
CC   -!- FUNCTION: May modulate chromatin structure by regulation of nucleosome
CC       assembly/disassembly. Could function together with B-type cyclins in
CC       the regulation of microtubule dynamics. {ECO:0000250,
CC       ECO:0000269|PubMed:12569397, ECO:0000269|PubMed:15980199}.
CC   -!- SUBUNIT: Binds preferentially histones H4 and H1 in vitro. Interacts
CC       with CYCB1;1. {ECO:0000269|PubMed:15980199}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15980199}. Cytoplasm
CC       {ECO:0000269|PubMed:15980199}. Note=Shuttles between cytoplasm and
CC       nucleus.
CC   -!- DOMAIN: The acidic domain is probably involved in the interaction with
CC       histones.
CC   -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC       {ECO:0000305}.
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DR   EMBL; AJ438613; CAD27460.1; -; mRNA.
DR   RefSeq; NP_001312631.1; NM_001325702.2.
DR   AlphaFoldDB; Q70Z19; -.
DR   SMR; Q70Z19; -.
DR   GeneID; 107801712; -.
DR   KEGG; nta:107801712; -.
DR   OMA; RWGHEEL; -.
DR   PhylomeDB; Q70Z19; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProt.
DR   GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR   InterPro; IPR037231; NAP-like_sf.
DR   InterPro; IPR002164; NAP_family.
DR   PANTHER; PTHR11875; PTHR11875; 1.
DR   Pfam; PF00956; NAP; 1.
DR   SUPFAM; SSF143113; SSF143113; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Coiled coil; Cytoplasm; Lipoprotein; Methylation; Nucleus;
KW   Prenylation; Reference proteome.
FT   CHAIN           1..371
FT                   /note="Nucleosome assembly protein 1;1"
FT                   /id="PRO_0000423695"
FT   PROPEP          372..374
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SZI2"
FT                   /id="PRO_0000423696"
FT   REGION          299..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          26..80
FT                   /evidence="ECO:0000255"
FT   MOTIF           47..62
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           223..228
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        301..338
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         371
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SZI2"
FT   LIPID           371
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SZI2"
SQ   SEQUENCE   374 AA;  42579 MW;  F6A9196063721D95 CRC64;
     MSNTKDNFNV ADLTAALGAG DREDLVNALK NKLQDITGKP TNVLECLSPN VRKRVEVLKE
     IQSQHDELEA KFYEERAVLE AKYQKLYQPL YTKRFDIVNG VVEVNTSETE AAAMDQDEDE
     DAVGKGVPDF WLIAMKNNDV LSEEITERDE GALKFLKDIK WAKIDNPKGF KLEFFFDTNP
     YFTNTVLTKT YHMIDEDEPI LEKALGTEIE WYPGKCLTQK ILKKKPKKGS KNAKPITKTE
     QCESFFNFFS PPQVPEDEED IDEDAAEELQ SLMEQDYDIG STIRDKIISH AVSWFTGEAA
     EDDFADLEDD DDDDEEDDDD EDEEEEDDED DEDEEDEDDT NTKKKSSAVR KRGVRAHAPA
     GGQAGERPPE CKQQ