ID   NAP1C_TOBAC             Reviewed;         377 AA.
AC   Q70Z17;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Nucleosome assembly protein 1;3;
DE            Short=NtNAP1;3;
DE   AltName: Full=Nucleosome assembly protein 1-like 3;
DE            Short=NtNAP1_L3;
DE   Flags: Precursor;
GN   Name=NAP1;3; Synonyms=NAP1_L3;
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], FUNCTION, AND SUBCELLULAR LOCATION.
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   FUNCTION, SUBUNIT, INTERACTION WITH NAP1;4 AND CYCB1;1, AND SUBCELLULAR
RP   LOCATION.
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 (By similarity). Could function together with B-
CC       type cyclins in the regulation of microtubule dynamics. {ECO:0000250,
CC       ECO:0000269|PubMed:12569397, ECO:0000269|PubMed:15980199}.
CC   -!- SUBUNIT: Can form homomeric and heteromeric protein complexes with
CC       NAP1;4. Binds histones H2A and H2B in vivo. Also able to bind histones
CC       H1 and H4 in vitro. Interacts with CYCB1;1 and with alpha tubulin.
CC       {ECO:0000269|PubMed:15980199}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC       {ECO:0000269|PubMed:12569397, 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; AJ438615; CAD27462.1; -; mRNA.
DR   RefSeq; NP_001312957.1; NM_001326028.1.
DR   AlphaFoldDB; Q70Z17; -.
DR   SMR; Q70Z17; -.
DR   GeneID; 107818745; -.
DR   KEGG; nta:107818745; -.
DR   OMA; VDTESCN; -.
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;3"
FT                   /id="PRO_0000423699"
FT   PROPEP          375..377
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SZI2"
FT                   /id="PRO_0000423700"
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        302..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;  43090 MW;  4CC19140A350DB79 CRC64;
     MSNAKDNFNV ADLTAALNAE DRDDLVNVLK NKLQGLTGKH SNVLENLSPN VRKRVEVLRE
     IQTQHDELEA KFFEERAALE AKYQKQYQPL YAKRSEIVNG VVEVDGEATQ TAAADEEEDK
     DSVEKGVPDF WVTAMKNNEV LAEEITERDE GALKFLKDIK WSRIENPKGF KLEFFFETNP
     YFTNTVLTKT YHMIDEDEPI LEKAIGTEIE WHPGKCLTQK ILKKKPKKGS KNSKPITKIE
     QCESFFNFFS PPQVPDDEED IDEDAAEELQ NLMEQDYDIG STIRDKIIPH AVSWFTGEAA
     QDEDYIDLED DEDEEDDEDE DEDEEDEEEE DEDEDDDDED EHVTKTKKKS SAGRKRSGGA
     PAADGQPGER PPECKQQ