NAP1C_ARATH
ID NAP1C_ARATH Reviewed; 374 AA.
AC Q94K07; Q9LTS5;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Nucleosome assembly protein 1;3;
DE Short=AtNAP1;3;
DE AltName: Full=Nucleosome/chromatin assembly factor group A3;
DE Flags: Precursor;
GN Name=NAP1;3; Synonyms=NFA3; OrderedLocusNames=At5g56950; ORFNames=MHM17.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17122067; DOI=10.1105/tpc.106.046490;
RA Zhu Y., Dong A., Meyer D., Pichon O., Renou J.P., Cao K., Shen W.H.;
RT "Arabidopsis NRP1 and NRP2 encode histone chaperones and are required for
RT maintaining postembryonic root growth.";
RL Plant Cell 18:2879-2892(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19825649; DOI=10.1093/mp/ssp026;
RA Liu Z.Q., Gao J., Dong A.W., Shen W.H.;
RT "A truncated Arabidopsis NUCLEOSOME ASSEMBLY PROTEIN 1, AtNAP1;3T, alters
RT plant growth responses to abscisic acid and salt in the Atnap1;3-2
RT mutant.";
RL Mol. Plant 2:688-699(2009).
RN [7]
RP GENE FAMILY, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, FUNCTION,
RP AND INTERACTION WITH HISTONE H2A.
RX PubMed=19228338; DOI=10.1111/j.1365-313x.2009.03844.x;
RA Liu Z., Zhu Y., Gao J., Yu F., Dong A., Shen W.H.;
RT "Molecular and reverse genetic characterization of NUCLEOSOME ASSEMBLY
RT PROTEIN1 (NAP1) genes unravels their function in transcription and
RT nucleotide excision repair in Arabidopsis thaliana.";
RL Plant J. 59:27-38(2009).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22534127; DOI=10.1105/tpc.112.096792;
RA Gao J., Zhu Y., Zhou W., Molinier J., Dong A., Shen W.H.;
RT "NAP1 family histone chaperones are required for somatic homologous
RT recombination in Arabidopsis.";
RL Plant Cell 24:1437-1447(2012).
CC -!- FUNCTION: May modulate chromatin structure by regulation of nucleosome
CC assembly/disassembly (By similarity). May function in nucleotide
CC excision repair (NER). Involved in somatic homologous recombination.
CC Could be involved in response to abscisic acid (ABA) and to salt
CC stress. {ECO:0000250, ECO:0000269|PubMed:19228338,
CC ECO:0000269|PubMed:19825649, ECO:0000269|PubMed:22534127}.
CC -!- SUBUNIT: Can form homomeric and heteromeric protein complexes with
CC NAP1;1, NAP1;2 and NAP1;4. Binds histone H2A and associates with
CC chromatin in vivo. {ECO:0000269|PubMed:19228338}.
CC -!- INTERACTION:
CC Q94K07; Q9SZI2: NAP1;1; NbExp=4; IntAct=EBI-4430887, EBI-4424361;
CC Q94K07; Q9ZUP3: NAP1;2; NbExp=5; IntAct=EBI-4430887, EBI-1997989;
CC Q94K07; Q94K07: NAP1;3; NbExp=3; IntAct=EBI-4430887, EBI-4430887;
CC Q94K07; F4JEI8: NAP1;4; NbExp=3; IntAct=EBI-4430887, EBI-6913300;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:19228338}. Note=Predominantly located in cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17122067}.
CC -!- DOMAIN: The acidic domain is probably involved in the interaction with
CC histones.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Exhibits hyposensitive
CC response to abscisic acid (ABA) with defects in stomata closure, and a
CC decreased tolerance to salt stress. {ECO:0000269|PubMed:19228338,
CC ECO:0000269|PubMed:19825649, ECO:0000269|PubMed:22534127}.
CC -!- MISCELLANEOUS: Triple mutant nap1;1-nap1;2-nap1;3 has no obvious
CC visible phenotype but exhibits hypersensitivity to DNA damage after UV-
CC radiation, affected transcription of NER related genes
CC (PubMed:19228338), slight hypersensitive response to abscisic acid
CC (ABA) in seedling growth (PubMed:19825649) and impaired somatic
CC homologous recombination (PubMed:22534127).
CC {ECO:0000305|PubMed:19228338, ECO:0000305|PubMed:19825649,
CC ECO:0000305|PubMed:22534127}.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97025.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB024035; BAA97025.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96826.1; -; Genomic_DNA.
DR EMBL; AF370487; AAK43864.1; -; mRNA.
DR EMBL; AY064641; AAL47354.1; -; mRNA.
DR RefSeq; NP_568844.1; NM_125077.4.
DR AlphaFoldDB; Q94K07; -.
DR SMR; Q94K07; -.
DR BioGRID; 21041; 24.
DR IntAct; Q94K07; 10.
DR STRING; 3702.AT5G56950.1; -.
DR iPTMnet; Q94K07; -.
DR PaxDb; Q94K07; -.
DR PRIDE; Q94K07; -.
DR ProteomicsDB; 238525; -.
DR EnsemblPlants; AT5G56950.1; AT5G56950.1; AT5G56950.
DR GeneID; 835797; -.
DR Gramene; AT5G56950.1; AT5G56950.1; AT5G56950.
DR KEGG; ath:AT5G56950; -.
DR Araport; AT5G56950; -.
DR TAIR; locus:2164595; AT5G56950.
DR eggNOG; KOG1507; Eukaryota.
DR HOGENOM; CLU_038841_4_1_1; -.
DR InParanoid; Q94K07; -.
DR OMA; DEDDNHR; -.
DR OrthoDB; 1216172at2759; -.
DR PhylomeDB; Q94K07; -.
DR PRO; PR:Q94K07; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94K07; baseline and differential.
DR Genevisible; Q94K07; AT.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006281; P:DNA repair; IGI:TAIR.
DR GO; GO:0009294; P:DNA-mediated transformation; IMP:TAIR.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:TAIR.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR GO; GO:0016444; P:somatic cell DNA recombination; IMP:UniProtKB.
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 Phosphoprotein; Prenylation; Reference proteome.
FT CHAIN 1..371
FT /note="Nucleosome assembly protein 1;3"
FT /id="PRO_0000423680"
FT PROPEP 372..374
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9SZI2"
FT /id="PRO_0000423681"
FT REGION 299..374
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 222..227
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 300..338
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ZUP3"
FT MOD_RES 371
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9SZI2"
FT LIPID 371
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9SZI2"
SQ SEQUENCE 374 AA; 43294 MW; 2B605ED9807A6343 CRC64;
MSNDKDSFNV SDLTSALKDE DRAGLVNALK NKLQNLAGQH SDVLENLTPK IRRRVEVLRE
IQGKHDEIET KFREERAALE AKYQKLYQPL YNKRYEIVNG ATEVEGAPED AKMDQGDEKT
AEEKGVPSFW LTALKNNDVI SEEITERDEG ALIYLKDIKW CKIEEPKGFK LEFFFDQNPY
FKNTLLTKAY HMIDEDEPLL EKAIGTEIDW YPGKCLTQKI LKKKPKKGAK NAKPITKTED
CESFFNFFNP PQVPDDDEDI DEERAEELQN LMEQDYDIGS TIREKIIPHA VSWFTGEAIE
GEEFEIDNDD EDDIDEDEDE DEEDEDEDEE EDDEDEEEEV SKTKKKPSVL HKKGGRPQVT
DDQQGERPPE CKQQ
