NRP2_ARATH
ID NRP2_ARATH Reviewed; 255 AA.
AC Q8LC68; Q8GXV1; Q9M9V0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=NAP1-related protein 2;
DE AltName: Full=Nucleosome/chromatin assembly factor group A5;
DE AltName: Full=Protein SET homolog 2;
GN Name=NRP2; Synonyms=NFA5; OrderedLocusNames=At1g18800; ORFNames=F6A14.10;
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 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-227 (ISOFORM 2).
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 [6]
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 [7]
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 [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).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.42 ANGSTROMS) OF 14-222, AND SUBUNIT.
RX PubMed=31213016; DOI=10.3390/molecules24122258;
RA Kumar A., Kumar Singh A., Chandrakant Bobde R., Vasudevan D.;
RT "Structural characterization of Arabidopsis thaliana NAP1-Related Protein 2
RT (AtNRP2) and Comparison with its homolog AtNRP1.";
RL Molecules 24:0-0(2019).
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 NRP1 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 NRP1
CC (PubMed:17122067, PubMed:31213016). Binds histones H2A and H2B and
CC associates with chromatin in vivo (PubMed:17122067).
CC {ECO:0000269|PubMed:17122067, ECO:0000269|PubMed:31213016}.
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=Q8LC68-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LC68-2; Sequence=VSP_053258;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO63312.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC42657.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC011809; AAF27100.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29765.1; -; Genomic_DNA.
DR EMBL; AK118024; BAC42657.1; ALT_FRAME; mRNA.
DR EMBL; AY086761; AAM63812.1; -; mRNA.
DR EMBL; BT005248; AAO63312.1; ALT_FRAME; mRNA.
DR PIR; H86321; H86321.
DR RefSeq; NP_564063.1; NM_101738.3. [Q8LC68-2]
DR PDB; 6JQV; X-ray; 3.42 A; A/B=14-222.
DR PDBsum; 6JQV; -.
DR AlphaFoldDB; Q8LC68; -.
DR SMR; Q8LC68; -.
DR BioGRID; 23701; 8.
DR IntAct; Q8LC68; 2.
DR STRING; 3702.AT1G18800.1; -.
DR iPTMnet; Q8LC68; -.
DR PaxDb; Q8LC68; -.
DR PeptideAtlas; Q8LC68; -.
DR PRIDE; Q8LC68; -.
DR ProMEX; Q8LC68; -.
DR ProteomicsDB; 250599; -. [Q8LC68-1]
DR EnsemblPlants; AT1G18800.1; AT1G18800.1; AT1G18800. [Q8LC68-2]
DR GeneID; 838462; -.
DR Gramene; AT1G18800.1; AT1G18800.1; AT1G18800. [Q8LC68-2]
DR KEGG; ath:AT1G18800; -.
DR Araport; AT1G18800; -.
DR TAIR; locus:2034995; AT1G18800.
DR eggNOG; KOG1508; Eukaryota.
DR HOGENOM; CLU_051687_0_0_1; -.
DR InParanoid; Q8LC68; -.
DR OMA; ANTTNEF; -.
DR PRO; PR:Q8LC68; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LC68; baseline and differential.
DR Genevisible; Q8LC68; AT.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA: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:TAIR.
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..255
FT /note="NAP1-related protein 2"
FT /id="PRO_0000423703"
FT REGION 213..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 19..60
FT /evidence="ECO:0000255"
FT COMPBIAS 221..255
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 201
FT /note="E -> EQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074,
FT ECO:0000303|PubMed:14593172, ECO:0000303|Ref.4"
FT /id="VSP_053258"
FT HELIX 26..72
FT /evidence="ECO:0007829|PDB:6JQV"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:6JQV"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:6JQV"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:6JQV"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:6JQV"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:6JQV"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:6JQV"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:6JQV"
FT HELIX 202..208
FT /evidence="ECO:0007829|PDB:6JQV"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:6JQV"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:6JQV"
SQ SEQUENCE 255 AA; 29354 MW; F92ABD05C0A44BC0 CRC64;
MVTDKSKKAK TEEENVEQID AELVLSIEKL QEIQDDLEKI NEKASDEVLE VEQKYNVIRK
PVYDKRNEII KTIPDFWLTA FLSHPALGEL LTEEDQKIFK YLSSLDVEDA KDVKSGYSIT
FSFNPNPFFE DGKLTKTFTF LEEGTTKITA TPIKWKEGKG LANGVNHEKN GNKRALPEES
FFTWFSDAQH KEDVEDEMQD EVADIIKEDL WPNPLTYFNN DADEEDFDGD DDGDEEEKEG
DSDEDDDEED EVGEE
