NRP1_ARATH
ID NRP1_ARATH Reviewed; 256 AA.
AC Q9CA59; A8MSD9; F4HVQ1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=NAP1-related protein 1;
DE AltName: Full=Nucleosome/chromatin assembly factor group A6;
DE AltName: Full=Protein SET homolog 1;
GN Name=NRP1; Synonyms=NFA6; OrderedLocusNames=At1g74560; ORFNames=F1M20.24;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND SUBUNIT.
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 FUNCTION.
RX PubMed=19704743; DOI=10.4161/psb.2.3.3687;
RA Zhu Y., Dong A., Shen W.H.;
RT "Chromatin remodeling in Arabidopsis root growth.";
RL Plant Signal. Behav. 2:160-162(2007).
RN [7]
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 [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: Acts as histone H2A/H2B chaperone in nucleosome assembly,
CC playing a critical role for the correct expression of genes involved in
CC root proliferation and patterning. Required with NRP2 for the
CC maintenance of cell proliferation and differentiation in postembryonic
CC root growth. Involved in both intramolecular and intermolecular somatic
CC homologous recombination. {ECO:0000269|PubMed:17122067,
CC ECO:0000269|PubMed:19704743, ECO:0000269|PubMed:22534127}.
CC -!- SUBUNIT: Can form homomeric and heteromeric protein complexes with
CC NRP2. Binds histones H2A and H2B and associates with chromatin in vivo.
CC {ECO:0000269|PubMed:17122067}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17122067}. Nucleus
CC {ECO:0000269|PubMed:17122067}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CA59-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q9CA59-3; Sequence=VSP_053257;
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.
CC {ECO:0000269|PubMed:17122067, ECO:0000269|PubMed:22534127}.
CC -!- MISCELLANEOUS: Double mutant nrp1-nrp2 shows arrest of cell cycle
CC progression at G2/M and disordered cellular organization occurred in
CC root tips resulting in a short-root phenotype (PubMed:17122067). Double
CC mutant nrp1-nrp2 also displays hypersensitive response to DNA damage
CC (PubMed:17122067) and impaired somatic homologous recombination
CC (PubMed:22534127). {ECO:0000305|PubMed:17122067,
CC ECO:0000305|PubMed:22534127}.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000305}.
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DR EMBL; AC011765; AAG52377.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35609.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35611.1; -; Genomic_DNA.
DR EMBL; AF385720; AAK60311.1; -; mRNA.
DR EMBL; AY081733; AAL87386.1; -; mRNA.
DR EMBL; AK316717; BAH19444.1; -; mRNA.
DR PIR; G96774; G96774.
DR RefSeq; NP_001077822.1; NM_001084353.1. [Q9CA59-3]
DR RefSeq; NP_177596.1; NM_106116.4. [Q9CA59-1]
DR PDB; 5DAY; X-ray; 2.33 A; A/B=19-225.
DR PDB; 7BP6; X-ray; 1.58 A; A=226-232.
DR PDB; 7C7X; X-ray; 3.00 A; E/F=19-256.
DR PDBsum; 5DAY; -.
DR PDBsum; 7BP6; -.
DR PDBsum; 7C7X; -.
DR AlphaFoldDB; Q9CA59; -.
DR SMR; Q9CA59; -.
DR BioGRID; 29016; 8.
DR IntAct; Q9CA59; 2.
DR STRING; 3702.AT1G74560.3; -.
DR PaxDb; Q9CA59; -.
DR PRIDE; Q9CA59; -.
DR ProteomicsDB; 249452; -. [Q9CA59-1]
DR EnsemblPlants; AT1G74560.1; AT1G74560.1; AT1G74560. [Q9CA59-1]
DR EnsemblPlants; AT1G74560.3; AT1G74560.3; AT1G74560. [Q9CA59-3]
DR GeneID; 843797; -.
DR Gramene; AT1G74560.1; AT1G74560.1; AT1G74560. [Q9CA59-1]
DR Gramene; AT1G74560.3; AT1G74560.3; AT1G74560. [Q9CA59-3]
DR KEGG; ath:AT1G74560; -.
DR Araport; AT1G74560; -.
DR TAIR; locus:2019075; AT1G74560.
DR eggNOG; KOG1508; Eukaryota.
DR OMA; KYTKLHQ; -.
DR OrthoDB; 1191764at2759; -.
DR PhylomeDB; Q9CA59; -.
DR PRO; PR:Q9CA59; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CA59; baseline and differential.
DR Genevisible; Q9CA59; 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:0003682; F:chromatin binding; IDA:TAIR.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:TAIR.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
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 3D-structure; Alternative splicing; Chaperone; Coiled coil; Cytoplasm;
KW Nucleus; Reference proteome.
FT CHAIN 1..256
FT /note="NAP1-related protein 1"
FT /id="PRO_0000423702"
FT REGION 220..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..64
FT /evidence="ECO:0000255"
FT COMPBIAS 226..256
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 217..256
FT /note="SNPLTYFNNDADEEDFDGDDDGDEEGEEDDDDEEEEDGEE -> MLMKRILM
FT EMMMVTKREKKTMTMKRRKMVRNDGSPKITHCWLASITDV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_053257"
FT HELIX 19..74
FT /evidence="ECO:0007829|PDB:5DAY"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:5DAY"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:5DAY"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:5DAY"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:5DAY"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:5DAY"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:5DAY"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:5DAY"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:5DAY"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:5DAY"
FT HELIX 206..213
FT /evidence="ECO:0007829|PDB:5DAY"
FT TURN 214..217
FT /evidence="ECO:0007829|PDB:5DAY"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:5DAY"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:7BP6"
SQ SEQUENCE 256 AA; 29416 MW; 9DB48574CB1D36FF CRC64;
MVADKSKKSK IEEKGEEENL EQIDAELVLS IEKLQEIQDD LEKINEKASD EVLEVEQKYN
VIRKPVYDKR NEVIQSIPGF WMTAFLSHPA LGDLLTEEDQ KIFKYLNSLE VEDAKDVKSG
YSITFHFTSN PFFEDAKLTK TFTFLEEGTT KITATPIKWK EGKGLPNGVN HDDKKGNKRA
LPEESFFTWF TDAQHKEDAG DEIHDEVADI IKEDLWSNPL TYFNNDADEE DFDGDDDGDE
EGEEDDDDEE EEDGEE
