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NAP1A_ORYSI
ID   NAP1A_ORYSI             Reviewed;         377 AA.
AC   B8B2R4; Q70Z21;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Nucleosome assembly protein 1;1;
DE            Short=OsNAP1;1;
DE   AltName: Full=Nucleosome assembly protein 1-like 1;
DE            Short=OsNAP1_L1;
DE   Flags: Precursor;
GN   Name=NAP1;1; Synonyms=NAP1_L1; ORFNames=OsI_21684;
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], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RC   TISSUE=Root;
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   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).
RN   [3]
RP   MUTAGENESIS OF PRO-348, SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL, AND
RP   NUCLEAR LOCALIZATION SIGNAL.
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. {ECO:0000250, ECO:0000269|PubMed:12569397}.
CC   -!- SUBUNIT: Binds preferentially histone H1 in vitro.
CC       {ECO:0000269|PubMed:12569397}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
CC       cytoplasm and nucleus.
CC   -!- TISSUE SPECIFICITY: Highly expressed in tissues exhibiting active cell-
CC       division activities, such as root and shoot meristems and young
CC       flowers. {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; AJ438611; CAD27458.1; -; mRNA.
DR   EMBL; CM000131; EEC80015.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8B2R4; -.
DR   SMR; B8B2R4; -.
DR   STRING; 39946.B8B2R4; -.
DR   PRIDE; B8B2R4; -.
DR   EnsemblPlants; BGIOSGA022322-TA; BGIOSGA022322-PA; BGIOSGA022322.
DR   Gramene; BGIOSGA022322-TA; BGIOSGA022322-PA; BGIOSGA022322.
DR   HOGENOM; CLU_038841_4_1_1; -.
DR   OMA; NSAYNDE; -.
DR   Proteomes; UP000007015; Chromosome 6.
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; Lipoprotein; Methylation; Nucleus;
KW   Prenylation; Reference proteome.
FT   CHAIN           1..374
FT                   /note="Nucleosome assembly protein 1;1"
FT                   /id="PRO_0000423683"
FT   PROPEP          375..377
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SZI2"
FT                   /id="PRO_0000423684"
FT   REGION          306..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          33..87
FT                   /evidence="ECO:0000255"
FT   MOTIF           54..69
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000305"
FT   MOTIF           230..235
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           347..351
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:15980199"
FT   COMPBIAS        309..342
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"
FT   MUTAGEN         348
FT                   /note="P->T: Relocation exclusively in the cytoplasm."
FT                   /evidence="ECO:0000269|PubMed:15980199"
FT   CONFLICT        309
FT                   /note="A -> S (in Ref. 1; CAD27458)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   377 AA;  42599 MW;  A8CEBBBDD88B9DE2 CRC64;
     MGGDKENLDL SDLNASLPAA AAALSAEDRA GLVNALKDKL QSLAGQHTDV LEALSPNVRK
     RVEYLREIQG QHDEIELKFF EERAALEAKY QKLYEPLYTK RYNIVNGVVE VDGGNDEPAS
     ENAAEFKDAD AKGVPDFWLT AMKTNEVLSE EIQERDEPAL KYLKDIKWAR IDDPKGFKLD
     FFFDTNPFFK NSVLTKTYHM VDEDEPILEK AIGTEIEWYP GKNLTQKILK KKPKKGSKNA
     KPITKTEVCE SFFNFFSPPQ VPDDDEDIDE DTADELQGQM EHDYDIGTTI RDKIIPHAVS
     WFTGEAVQAE DFDDMEDDEE DDEDDDEDEE EEEDEDEDED DEEEKSKPKK KSAGKPKLPS
     KGGAQGGADQ PADCKQQ
 
 
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