NAP1A_ARATH
ID NAP1A_ARATH Reviewed; 372 AA.
AC Q9SZI2; Q38809;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Nucleosome assembly protein 1;1;
DE Short=AtNAP1;1;
DE AltName: Full=Nucleosome/chromatin assembly factor group A1;
DE Flags: Precursor;
GN Name=NAP1;1; Synonyms=NFA1; OrderedLocusNames=At4g26110;
GN ORFNames=F20B18.220;
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7923358; DOI=10.1016/0092-8674(94)90282-8;
RA Mindrinos M., Katagiri F., Yu G.-L., Ausubel F.M.;
RT "The A. thaliana disease resistance gene RPS2 encodes a protein containing
RT a nucleotide-binding site and leucine-rich repeats.";
RL Cell 78:1089-1099(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
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 [6]
RP ISOPRENYLATION AT CYS-369, METHYLATION AT CYS-369, MUTAGENESIS OF CYS-369,
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=17041028; DOI=10.1104/pp.106.088344;
RA Galichet A., Gruissem W.;
RT "Developmentally controlled farnesylation modulates AtNAP1;1 function in
RT cell proliferation and cell expansion during Arabidopsis leaf
RT development.";
RL Plant Physiol. 142:1412-1426(2006).
RN [7]
RP DISRUPTION PHENOTYPE.
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 [8]
RP GENE FAMILY, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP 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 [9]
RP INTERACTION WITH PP438/PNM1.
RX PubMed=21297037; DOI=10.1105/tpc.110.081638;
RA Hammani K., Gobert A., Hleibieh K., Choulier L., Small I., Giege P.;
RT "An Arabidopsis dual-localized pentatricopeptide repeat protein interacts
RT with nuclear proteins involved in gene expression regulation.";
RL Plant Cell 23:730-740(2011).
RN [10]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21571540; DOI=10.1016/j.plaphy.2011.04.012;
RA Shigeta T., Yasuda D., Mori T., Yoshimitsu Y., Nakamura Y., Yoshida S.,
RA Asami T., Okamoto S., Matsuo T.;
RT "Characterization of brassinosteroid-regulated proteins in a nuclear-
RT enriched fraction of Arabidopsis suspension-cultured cells.";
RL Plant Physiol. Biochem. 49:985-995(2011).
RN [11]
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). Contributes to the regulation of
CC cell proliferation and cell expansion. May function in nucleotide
CC excision repair (NER). Involved in somatic homologous recombination.
CC {ECO:0000250, ECO:0000269|PubMed:17041028,
CC ECO:0000269|PubMed:22534127}.
CC -!- SUBUNIT: Can form homomeric and heteromeric protein complexes with
CC NAP1;2, NAP1;3 and NAP1;4. Binds histone H2A. Interacts with
CC PP438/PNM1. {ECO:0000269|PubMed:19228338, ECO:0000269|PubMed:21297037}.
CC -!- INTERACTION:
CC Q9SZI2; A0A178WA11: At1g08580; NbExp=3; IntAct=EBI-4424361, EBI-25520907;
CC Q9SZI2; A0A178WNP1: At1g30880; NbExp=3; IntAct=EBI-4424361, EBI-25520770;
CC Q9SZI2; Q9C8Z9: BHLH148; NbExp=3; IntAct=EBI-4424361, EBI-4434374;
CC Q9SZI2; Q9SKX1: IBH1; NbExp=4; IntAct=EBI-4424361, EBI-4433589;
CC Q9SZI2; Q9FW03: MES11; NbExp=3; IntAct=EBI-4424361, EBI-4426271;
CC Q9SZI2; Q9SGU3: MYB72; NbExp=3; IntAct=EBI-4424361, EBI-1789562;
CC Q9SZI2; Q9SZI2: NAP1;1; NbExp=5; IntAct=EBI-4424361, EBI-4424361;
CC Q9SZI2; Q9ZUP3: NAP1;2; NbExp=4; IntAct=EBI-4424361, EBI-1997989;
CC Q9SZI2; Q94K07: NAP1;3; NbExp=4; IntAct=EBI-4424361, EBI-4430887;
CC Q9SZI2; F4JEI8: NAP1;4; NbExp=2; IntAct=EBI-4424361, EBI-6913300;
CC Q9SZI2; Q9FME4: PNM1; NbExp=4; IntAct=EBI-4424361, EBI-6913662;
CC Q9SZI2; Q9LER7: PSRP5; NbExp=3; IntAct=EBI-4424361, EBI-25520884;
CC Q9SZI2; Q8VZ55: RPL35; NbExp=4; IntAct=EBI-4424361, EBI-4470631;
CC Q9SZI2; Q9LZH9: RPL7AB; NbExp=3; IntAct=EBI-4424361, EBI-9161146;
CC Q9SZI2; Q93WU8: WRKY54; NbExp=3; IntAct=EBI-4424361, EBI-15207592;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly located in
CC cytoplasm. Shuttles between cytoplasm and nucleus depending on stage of
CC the cell cycle. Farnelysation favors the location to the nucleus early
CC in leaf development.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SZI2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17122067}.
CC -!- INDUCTION: By brassinosteroids. {ECO:0000269|PubMed:21571540}.
CC -!- DOMAIN: The acidic domain is probably involved in the interaction with
CC histones.
CC -!- PTM: Prenylation of the protein is required for its function during the
CC cell proliferation phase of leaf development.
CC {ECO:0000269|PubMed:17041028}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:19228338). Enlarged
CC plants early in the development but reduced plants in size in a later
CC stage (PubMed:17041028). {ECO:0000269|PubMed:17041028,
CC ECO:0000269|PubMed:19228338, ECO:0000269|PubMed:19825649,
CC 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=AAA50234.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U12858; AAA50234.1; ALT_INIT; mRNA.
DR EMBL; AL049483; CAB39676.1; -; Genomic_DNA.
DR EMBL; AL161564; CAB79466.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85158.1; -; Genomic_DNA.
DR EMBL; AY054484; AAK96675.1; -; mRNA.
DR EMBL; AY093283; AAM13282.1; -; mRNA.
DR PIR; T04266; T04266.
DR RefSeq; NP_194341.1; NM_118744.3. [Q9SZI2-1]
DR AlphaFoldDB; Q9SZI2; -.
DR SMR; Q9SZI2; -.
DR BioGRID; 14004; 37.
DR IntAct; Q9SZI2; 22.
DR STRING; 3702.AT4G26110.1; -.
DR iPTMnet; Q9SZI2; -.
DR PaxDb; Q9SZI2; -.
DR PRIDE; Q9SZI2; -.
DR EnsemblPlants; AT4G26110.1; AT4G26110.1; AT4G26110. [Q9SZI2-1]
DR GeneID; 828717; -.
DR Gramene; AT4G26110.1; AT4G26110.1; AT4G26110. [Q9SZI2-1]
DR KEGG; ath:AT4G26110; -.
DR Araport; AT4G26110; -.
DR TAIR; locus:2120785; AT4G26110.
DR eggNOG; KOG1507; Eukaryota.
DR HOGENOM; CLU_038841_4_1_1; -.
DR InParanoid; Q9SZI2; -.
DR OrthoDB; 1216172at2759; -.
DR PhylomeDB; Q9SZI2; -.
DR PRO; PR:Q9SZI2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZI2; baseline and differential.
DR Genevisible; Q9SZI2; AT.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030154; P:cell differentiation; IMP:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IGI: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 Alternative splicing; Chaperone; Coiled coil; Cytoplasm; Lipoprotein;
KW Methylation; Nucleus; Phosphoprotein; Prenylation; Reference proteome.
FT CHAIN 1..369
FT /note="Nucleosome assembly protein 1;1"
FT /evidence="ECO:0000305|PubMed:17041028"
FT /id="PRO_0000423676"
FT PROPEP 370..372
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:17041028"
FT /id="PRO_0000423677"
FT REGION 299..372
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 301..335
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..372
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 369
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305|PubMed:17041028"
FT LIPID 369
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:17041028"
FT MUTAGEN 369
FT /note="C->S: Abolishes farnesylation and disrupts the
FT function of the protein."
FT /evidence="ECO:0000269|PubMed:17041028"
SQ SEQUENCE 372 AA; 42997 MW; 8AA1C7E84C0BC4D2 CRC64;
MSNDKDSFNV SDLTAALKDE DRAGLVNALK NKLQNLAGQR SDVLENLTPN VRKRVDALRD
IQSQHDELEA KFREERAILE AKYQTLYQPL YVKRYEIVNG TTEVELAPED DTKVDQGEEK
TAEEKGVPSF WLTALKNNDV ISEEVTERDE GALKYLKDIK WCKIEEPKGF KLEFFFDTNP
YFKNTVLTKS YHMIDEDEPL LEKAMGTEID WYPGKCLTQK ILKKKPKKGS KNTKPITKLE
DCESFFNFFS PPEVPDEDED IDEERAEDLQ NLMEQDYDIG STIREKIIPR AVSWFTGEAM
EAEDFEIDDD EEDDIDEDED EEDEEDEEDD DDEDEEESKT KKKPSIGNKK GGRSQIVGEG
KQDERPPECK QQ
