ID   HMGN3_PONAB             Reviewed;          99 AA.
AC   Q5R715;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=High mobility group nucleosome-binding domain-containing protein 3;
GN   Name=HMGN3;
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=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to nucleosomes, regulating chromatin structure and
CC       consequently, chromatin-dependent processes such as transcription, DNA
CC       replication and DNA repair. Affects both insulin and glucagon levels
CC       and modulates the expression of pancreatic genes involved in insulin
CC       secretion. Regulates the expression of the glucose transporter SLC2A2
CC       by binding specifically to its promoter region and recruiting PDX1 and
CC       additional transcription factors. Regulates the expression of SLC6A9, a
CC       glycine transporter which regulates the glycine concentration in
CC       synaptic junctions in the central nervous system, by binding to its
CC       transcription start site. May play a role in ocular development and
CC       astrocyte function (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the ligand binding domain of the thyroid
CC       receptor (TR) (in vitro). Requires the presence of thyroid hormone for
CC       its interaction. Interacts with transcriptional regulator SEHBP.
CC       Interacts with nucleosomes. {ECO:0000250|UniProtKB:Q15651}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HMGN family. {ECO:0000305}.
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DR   EMBL; CR860308; CAH92445.1; -; Transcribed_RNA.
DR   RefSeq; XP_009240293.1; XM_009242018.1.
DR   AlphaFoldDB; Q5R715; -.
DR   STRING; 9601.ENSPPYP00000018795; -.
DR   GeneID; 100172109; -.
DR   CTD; 9324; -.
DR   eggNOG; ENOG502S60V; Eukaryota.
DR   InParanoid; Q5R715; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0000785; C:chromatin; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031492; F:nucleosomal DNA binding; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:InterPro.
DR   InterPro; IPR031073; HMGN3.
DR   InterPro; IPR000079; HMGN_fam.
DR   PANTHER; PTHR23087:SF2; PTHR23087:SF2; 1.
DR   Pfam; PF01101; HMG14_17; 1.
DR   PRINTS; PR00925; NONHISHMG17.
DR   SMART; SM00527; HMG17; 1.
DR   PROSITE; PS00355; HMG14_17; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..99
FT                   /note="High mobility group nucleosome-binding domain-
FT                   containing protein 3"
FT                   /id="PRO_0000232576"
FT   REGION          1..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15651"
FT   MOD_RES         10
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15651"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15651"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15651"
SQ   SEQUENCE   99 AA;  10724 MW;  FFC7780651089C23 CRC64;
     MPKRKSPENT EDKDGSKVTK QEPTRRSARL SAKPAPPKPE PKPRKTSAKK EPGAKISRGA
     KGKKEEKQEA GKEGTAPSEN GETKAEEAQK TESVDNEGE