ID   NAP1B_TOBAC             Reviewed;         377 AA.
AC   Q70Z18;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Nucleosome assembly protein 1;2;
DE            Short=NtNAP1;2;
DE   AltName: Full=Nucleosome assembly protein 1-like 2;
DE            Short=NtNAP1_L2;
DE   Flags: Precursor;
GN   Name=NAP1;2; Synonyms=NAP1_L2;
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 histone H1 in vitro. Interacts with
CC       CYCB1;1. {ECO:0000269|PubMed:15980199}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC       {ECO:0000269|PubMed:15980199}.
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; AJ438614; CAD27461.1; -; mRNA.
DR   RefSeq; NP_001311629.1; NM_001324700.1.
DR   AlphaFoldDB; Q70Z18; -.
DR   SMR; Q70Z18; -.
DR   GeneID; 107760768; -.
DR   KEGG; nta:107760768; -.
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..374
FT                   /note="Nucleosome assembly protein 1;2"
FT                   /id="PRO_0000423697"
FT   PROPEP          375..377
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SZI2"
FT                   /id="PRO_0000423698"
FT   REGION          298..377
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..340
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         374
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SZI2"
FT   LIPID           374
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SZI2"
SQ   SEQUENCE   377 AA;  43154 MW;  FEFC60AA03B90950 CRC64;
     MSNTKDNFNV ADLTAALNAG DRADLVNVLK NKLHDLTGKH SNVTESLSPN VRKRVEALRE
     IQTEHDELEA KFFEERAALE AKYQKLYQPL YTKRFEIVNG VVEVDGATTE AAAADKQEDK
     DAVEKGVPDF WLTAMKNNEV LAEEITERDE EALKFLRDIK WSRIDDPKGF KLDFFFETNP
     YFKNSVLTKT YHMIDEDEPI LEKAIATEIE WYPGKCLTQK ILKKKPKKGS KNAKPITKTE
     QCESFFNFFS PPQVPEDEED IDEDAAEELQ NLMEQDYDIG STIRDKIIPH AVSWFTGEAA
     EDDYAELEDD EDEDDDEEDD EDEDEEEEDE EDDEDEEEDE DETKTKKKTS AVPKKSGRVP
     AAADGQSGER PPECKQQ