ID   NAP1D_TOBAC             Reviewed;         356 AA.
AC   Q70Z16;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Nucleosome assembly protein 1;4;
DE            Short=NtNAP1;4;
DE   AltName: Full=Nucleosome assembly protein 1-like 4;
DE            Short=NtNAP1_L4;
GN   Name=NAP1;4; Synonyms=NAP1_L4;
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, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
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;3 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;3. 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   -!- DEVELOPMENTAL STAGE: Highly expressed at the G1/S transition.
CC       {ECO:0000269|PubMed:12569397}.
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; AJ438616; CAD27463.1; -; mRNA.
DR   RefSeq; NP_001312718.1; NM_001325789.1.
DR   RefSeq; XP_016486317.1; XM_016630831.1.
DR   AlphaFoldDB; Q70Z16; -.
DR   SMR; Q70Z16; -.
DR   GeneID; 107806625; -.
DR   KEGG; nta:107806625; -.
DR   OMA; NSAYNDE; -.
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; Nucleus; Reference proteome.
FT   CHAIN           1..356
FT                   /note="Nucleosome assembly protein 1;4"
FT                   /id="PRO_0000423701"
FT   REGION          304..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          34..88
FT                   /evidence="ECO:0000255"
FT   MOTIF           55..70
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           230..235
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        309..342
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   356 AA;  40727 MW;  26AFA3CA6F2D6016 CRC64;
     MSNSNKDHFD MSDLGASLPA AAAALSAEDR AGLVNALKNK LQNLAGQHSD ILETLTPQVR
     KRVDVLRELQ SQHDELESHF FEERAALEAK YQKLYEPLYT KRYEIVNGVV EVEGVNEAPM
     NQEEDKEAGN EKGVPNFWLT AMKTNEILAE EISERDEEAL KYLKDIKWCK IDDRKGFKLE
     FFFDTNPFFT NSVLTKTYHM IDDDDPILEK AIGTKIDWCP GKCLTQKILK KKPKKGSKNA
     KPIIKTETCE SFFNFFKPPQ VPEDDDDDDI DEDAAEELQN LMEQDYDIGS TIRDKIIPHA
     VSWFTGEAAE GDEFEDIEDD DDDDDDDDDE DDEDEEDEDD EEEEKSKKKS SALKVE