NUPL_XENLA
ID NUPL_XENLA Reviewed; 200 AA.
AC P05221;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Nucleoplasmin;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2884102; DOI=10.1002/j.1460-2075.1987.tb04720.x;
RA Dingwall C., Dilworth S.M., Black S.J., Kearsey S.E., Cox L.S.,
RA Laskey R.A.;
RT "Nucleoplasmin cDNA sequence reveals polyglutamic acid tracts and a cluster
RT of sequences homologous to putative nuclear localization signals.";
RL EMBO J. 6:69-74(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-200.
RX PubMed=3428591; DOI=10.1101/gad.1.1.97;
RA Buerglin T.R., Mattaj I.W., Newmeyer D.D., Zeller R., De Robertis E.M.;
RT "Cloning of nucleoplasmin from Xenopus laevis oocytes and analysis of its
RT developmental expression.";
RL Genes Dev. 1:97-107(1987).
RN [3]
RP FUNCTION, ACETYLATION AT ALA-2, AND PHOSPHORYLATION AT SER-3; THR-4; SER-6;
RP THR-8; SER-149; SER-177; SER-178 AND SER-182.
RX PubMed=17510054; DOI=10.1074/jbc.m702842200;
RA Banuelos S., Omaetxebarria M.J., Ramos I., Larsen M.R., Arregi I.,
RA Jensen O.N., Arizmendi J.M., Prado A., Muga A.;
RT "Phosphorylation of both nucleoplasmin domains is required for activation
RT of its chromatin decondensation activity.";
RL J. Biol. Chem. 282:21213-21221(2007).
RN [4]
RP INTERACTION WITH PRMT5 AND WDR77, MUTAGENESIS OF ARG-192 AND ARG-194,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND METHYLATION AT ARG-192.
RX PubMed=22009756; DOI=10.1074/jbc.m111.303677;
RA Wilczek C., Chitta R., Woo E., Shabanowitz J., Chait B.T., Hunt D.F.,
RA Shechter D.;
RT "Protein arginine methyltransferase Prmt5-Mep50 methylates histones H2A and
RT H4 and the histone chaperone nucleoplasmin in Xenopus laevis eggs.";
RL J. Biol. Chem. 286:42221-42231(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 153-171 IN COMPLEX WITH
RP KARYOPHERIN ALPHA, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=10745017; DOI=10.1016/s0969-2126(00)00107-6;
RA Conti E., Kuriyan J.;
RT "Crystallographic analysis of the specific yet versatile recognition of
RT distinct nuclear localization signals by karyopherin alpha.";
RL Structure 8:329-338(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-124, FUNCTION, AND SUBUNIT.
RX PubMed=11684019; DOI=10.1016/s1097-2765(01)00354-9;
RA Dutta S., Akey I.V., Dingwall C., Hartman K.L., Laue T., Nolte R.T.,
RA Head J.F., Akey C.W.;
RT "The crystal structure of nucleoplasmin-core: implications for histone
RT binding and nucleosome assembly.";
RL Mol. Cell 8:841-853(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 10-120, FUNCTION, SUBUNIT, AND
RP PHOSPHORYLATION.
RX PubMed=19055325; DOI=10.1021/bi800975r;
RA Taneva S.G., Munoz I.G., Franco G., Falces J., Arregi I., Muga A.,
RA Montoya G., Urbaneja M.A., Banuelos S.;
RT "Activation of nucleoplasmin, an oligomeric histone chaperone, challenges
RT its stability.";
RL Biochemistry 47:13897-13906(2008).
CC -!- FUNCTION: Acts as a chaperone for histones, such as histone H2A-H2B,
CC and thus regulates the assembly of nucleosome cores (PubMed:11684019,
CC PubMed:19055325). Involved in chromatin remodeling, especially during
CC fertilization and early embryonic development (By similarity). May be
CC involved in sperm chromatin decondensation during fertilization
CC (PubMed:17510054). {ECO:0000250|UniProtKB:Q86SE8,
CC ECO:0000269|PubMed:11684019, ECO:0000269|PubMed:17510054,
CC ECO:0000269|PubMed:19055325}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable.;
CC -!- SUBUNIT: Homopentamer, when bound to H2A-H2B dimers only. Homodecamer
CC of two stacked pentamers, when bound to H2A-H2B dimers and H3-H4
CC tetramers simultaneously. Interacts with the heterotetramer formed by
CC wdr77 and prmt5. {ECO:0000269|PubMed:10745017,
CC ECO:0000269|PubMed:11684019, ECO:0000269|PubMed:19055325,
CC ECO:0000269|PubMed:22009756}.
CC -!- INTERACTION:
CC P05221; Q02821: SRP1; Xeno; NbExp=2; IntAct=EBI-7261813, EBI-1797;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Activated by phosphorylation of multiple serine/threonine
CC residues, along both core and tail domains. The level of
CC phosphorylation gradually increases during egg maturation, reaching an
CC average of 7-10 phosphates per monomer, so that at the time of
CC fertilization the activity of the protein is maximum.
CC {ECO:0000269|PubMed:17510054, ECO:0000269|PubMed:19055325}.
CC -!- PTM: Methylated by prmt5, yielding both monomethylated and
CC symmetrically dimethylated Arg-192. {ECO:0000269|PubMed:22009756}.
CC -!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}.
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DR EMBL; X04766; CAA28460.1; -; mRNA.
DR EMBL; Y00204; CAA68363.1; -; mRNA.
DR PIR; A26169; A26169.
DR PIR; A26630; A26630.
DR PDB; 1EE5; X-ray; 2.40 A; B=153-171.
DR PDB; 1EJY; X-ray; 2.90 A; N=155-170.
DR PDB; 1K5J; X-ray; 2.30 A; A/B/C/D/E=1-124.
DR PDB; 2VTX; X-ray; 2.50 A; A/B/C/D/E/G/H/I/J/K=1-120.
DR PDB; 3UL1; X-ray; 1.90 A; A=153-172.
DR PDB; 4BPL; X-ray; 2.30 A; B=153-172.
DR PDBsum; 1EE5; -.
DR PDBsum; 1EJY; -.
DR PDBsum; 1K5J; -.
DR PDBsum; 2VTX; -.
DR PDBsum; 3UL1; -.
DR PDBsum; 4BPL; -.
DR AlphaFoldDB; P05221; -.
DR SMR; P05221; -.
DR DIP; DIP-48470N; -.
DR ELM; P05221; -.
DR IntAct; P05221; 2.
DR MINT; P05221; -.
DR iPTMnet; P05221; -.
DR ABCD; P05221; 1 sequenced antibody.
DR EvolutionaryTrace; P05221; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005654; C:nucleoplasm; IDA:CAFA.
DR GO; GO:0031491; F:nucleosome binding; IMP:CAFA.
DR GO; GO:0031497; P:chromatin assembly; IMP:GO_Central.
DR GO; GO:0035041; P:sperm DNA decondensation; IMP:CAFA.
DR DisProt; DP00217; -.
DR IDEAL; IID50001; -.
DR InterPro; IPR004301; Nucleoplasmin.
DR InterPro; IPR024057; Nucleoplasmin_core_dom.
DR InterPro; IPR036824; Nucleoplasmin_core_dom_sf.
DR PANTHER; PTHR22747; PTHR22747; 1.
DR Pfam; PF03066; Nucleoplasmin; 1.
DR SUPFAM; SSF69203; SSF69203; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Chromatin regulator;
KW Developmental protein; Fertilization; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17510054"
FT CHAIN 2..200
FT /note="Nucleoplasmin"
FT /id="PRO_0000219486"
FT REGION 35..39
FT /note="Acidic tract A1"
FT /evidence="ECO:0000303|PubMed:11684019"
FT REGION 123..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..148
FT /note="Acidic tract A2"
FT /evidence="ECO:0000303|PubMed:11684019"
FT REGION 174..176
FT /note="Acidic tract A3"
FT /evidence="ECO:0000303|PubMed:11684019"
FT MOTIF 155..170
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:10745017"
FT COMPBIAS 124..147
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 58
FT /note="Interaction between pentamers"
FT /evidence="ECO:0000269|PubMed:11684019"
FT SITE 82
FT /note="Interaction between pentamers"
FT /evidence="ECO:0000269|PubMed:11684019"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:17510054"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17510054"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17510054"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17510054"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17510054"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17510054"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17510054"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17510054"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17510054"
FT MOD_RES 192
FT /note="Omega-N-methylarginine; by PRMT5; alternate"
FT /evidence="ECO:0000269|PubMed:22009756"
FT MOD_RES 192
FT /note="Symmetric dimethylarginine; by PRMT5; alternate"
FT /evidence="ECO:0000269|PubMed:22009756"
FT MUTAGEN 192
FT /note="R->A: Abolishes arginine methylation."
FT /evidence="ECO:0000269|PubMed:22009756"
FT MUTAGEN 194
FT /note="R->A: Reduces arginine methylation."
FT /evidence="ECO:0000269|PubMed:22009756"
FT CONFLICT 11
FT /note="L -> V (in Ref. 2; CAA68363)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="D -> N (in Ref. 2; CAA68363)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="E -> A (in Ref. 2; CAA68363)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="V -> I (in Ref. 2; CAA68363)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="N -> H (in Ref. 2; CAA68363)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="A -> K (in Ref. 2; CAA68363)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="S -> P (in Ref. 2; CAA68363)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="T -> S (in Ref. 2; CAA68363)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="L -> V (in Ref. 2; CAA68363)"
FT /evidence="ECO:0000305"
FT CONFLICT 134..137
FT /note="Missing (in Ref. 2; CAA68363)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="Q -> P (in Ref. 2; CAA68363)"
FT /evidence="ECO:0000305"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:1K5J"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1K5J"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:1K5J"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:1K5J"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:1K5J"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1K5J"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1K5J"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:1K5J"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:1K5J"
SQ SEQUENCE 200 AA; 22024 MW; A91DD110F2965812 CRC64;
MASTVSNTSK LEKPVSLIWG CELNEQDKTF EFKVEDDEEK CEHQLALRTV CLGDKAKDEF
NIVEIVTQEE GAEKSVPIAT LKPSILPMAT MVGIELTPPV TFRLKAGSGP LYISGQHVAM
EEDYSWAEEE DEGEAEGEEE EEEEEDQESP PKAVKRPAAT KKAGQAKKKK LDKEDESSEE
DSPTKKGKGA GRGRKPAAKK
