ID   NPM3_PONAB              Reviewed;         180 AA.
AC   Q5RC37;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Nucleoplasmin-3;
GN   Name=NPM3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in the regulation of diverse cellular processes
CC       such as ribosome biogenesis, chromatin remodeling or protein
CC       chaperoning. Modulates the histone chaperone function and the RNA-
CC       binding activity of nucleolar phosphoprotein B23/NPM. Efficiently
CC       mediates chromatin remodeling when included in a pentamer containing
CC       NPM3 and NPM. {ECO:0000250|UniProtKB:O75607}.
CC   -!- SUBUNIT: Interacts with NPM (via N-terminus). Forms a pentamer with NPM
CC       at a ratio 4:1 (NPM3/NPM). Two pentamers form a decamer.
CC       {ECO:0000250|UniProtKB:O75607}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75607}. Nucleus,
CC       nucleolus {ECO:0000250|UniProtKB:O75607}. Note=Mainly found in the
CC       granular component of the nucleolus. {ECO:0000250|UniProtKB:O75607}.
CC   -!- PTM: Phosphorylated. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}.
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DR   EMBL; CR858444; CAH90673.1; -; mRNA.
DR   RefSeq; NP_001125366.1; NM_001131894.2.
DR   AlphaFoldDB; Q5RC37; -.
DR   SMR; Q5RC37; -.
DR   STRING; 9601.ENSPPYP00000003010; -.
DR   Ensembl; ENSPPYT00000003114; ENSPPYP00000003010; ENSPPYG00000002589.
DR   GeneID; 100172269; -.
DR   KEGG; pon:100172269; -.
DR   CTD; 10360; -.
DR   eggNOG; ENOG502S1E6; Eukaryota.
DR   GeneTree; ENSGT00940000158796; -.
DR   HOGENOM; CLU_058838_1_0_1; -.
DR   InParanoid; Q5RC37; -.
DR   OrthoDB; 1485080at2759; -.
DR   Proteomes; UP000001595; Chromosome 10.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006364; P:rRNA processing; IEA:Ensembl.
DR   GO; GO:0009303; P:rRNA transcription; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Acetylation; Chaperone; Methylation; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O75607"
FT   CHAIN           2..180
FT                   /note="Nucleoplasmin-3"
FT                   /id="PRO_0000219491"
FT   REGION          141..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..166
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O75607"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75607"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75607"
FT   MOD_RES         27
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O75607"
FT   MOD_RES         147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75607"
FT   MOD_RES         151
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75607"
FT   MOD_RES         160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75607"
SQ   SEQUENCE   180 AA;  19574 MW;  68D4AF3255E6C4DE CRC64;
     MAAGTAAALA FLSQESRTRA GGVGGLRVPA PVTMDSFFFG CELSGHTRSF TFKVEEEDDA
     EHVLALTMLC LTEGAKDECN VVEVVARNHD HQEIAVPVAN LKLSCQPMLS LDDFQLQPPV
     TFRLKSGSGP VRITGRHQIV TMSNDVSEEE SEEEEEEEDS DEEEAELCPI LPAKKQGGRP