ID   NAP1C_ORYSI             Reviewed;         301 AA.
AC   Q5MGA9; A2WUC9;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 2.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Nucleosome assembly protein 1;3;
DE            Short=OsNAP1;3;
DE   AltName: Full=Nucleosome assembly protein 1-like 3;
DE            Short=OsNAP1_L3;
GN   Name=NAP1;3; Synonyms=NAP1_L3; ORFNames=OsI_03479;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP   SER-297, AND MUTAGENESIS OF SER-297.
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: May modulate chromatin structure by regulation of nucleosome
CC       assembly/disassembly. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15980199}. 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAY75575.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY830122; AAV88624.1; -; mRNA.
DR   EMBL; CM000126; EAY75575.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q5MGA9; -.
DR   SMR; Q5MGA9; -.
DR   STRING; 39946.Q5MGA9; -.
DR   iPTMnet; Q5MGA9; -.
DR   Proteomes; UP000007015; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProt.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
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; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..301
FT                   /note="Nucleosome assembly protein 1;3"
FT                   /id="PRO_0000423691"
FT   REGION          279..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          15..69
FT                   /evidence="ECO:0000255"
FT   MOTIF           36..51
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        281..301
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         297
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000269|PubMed:15980199"
FT   MUTAGEN         297
FT                   /note="S->A: Abolishes phosphorylation by CK2."
FT                   /evidence="ECO:0000269|PubMed:15980199"
FT   CONFLICT        7
FT                   /note="S -> L (in Ref. 1; AAV88624)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   301 AA;  34946 MW;  B11A6BFF20261BAD CRC64;
     MSNPELSSEK KASLVETLKN KLQALAEQHV DVLESLAPVV RKRVDVLIEI QSQHDELEAK
     FLEEKSALEA KYHKLYGPLY SKRSEIVSGV LEVEGETEER EEKGVPDFWL KAMKNNEILA
     EEIHESDEEA LKYLKDIKWC RIDDLKGFKF EFFFDTNPFF KNQVLTKTYH MIDEDDEPIL
     EKAIGTEIEW HPGNCLTQEV LTKESLESTK PITKTEEYES FFNFFSPPQV PEDDAKIDEN
     TVEELQNQME RDYDIASTLR DKIIPHAVSW FTGEAVQDED YGASWVDDEE DDDDEYSDEE
     A