ID   HMGN3_BOVIN             Reviewed;         100 AA.
AC   Q3ZBV4;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=High mobility group nucleosome-binding domain-containing protein 3;
GN   Name=HMGN3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND PHYLOGENY.
RX   PubMed=19393058; DOI=10.1186/1471-2164-10-183;
RA   Uzun A., Rodriguez-Osorio N., Kaya A., Wang H., Parrish J.J., Ilyin V.A.,
RA   Memili E.;
RT   "Functional genomics of HMGN3a and SMARCAL1 in early mammalian
RT   embryogenesis.";
RL   BMC Genomics 10:183-183(2009).
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   -!- TISSUE SPECIFICITY: Expressed at similar levels in mature oocytes and
CC       2-4 cell embryos, but at higher levels in 8-16 cell embryos, morulae
CC       and blastocysts. {ECO:0000269|PubMed:19393058}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout early embryogenesis.
CC       {ECO:0000269|PubMed:19393058}.
CC   -!- SIMILARITY: Belongs to the HMGN family. {ECO:0000305}.
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DR   EMBL; BC103089; AAI03090.1; -; mRNA.
DR   RefSeq; NP_001029676.1; NM_001034504.2.
DR   AlphaFoldDB; Q3ZBV4; -.
DR   STRING; 9913.ENSBTAP00000045886; -.
DR   PaxDb; Q3ZBV4; -.
DR   PRIDE; Q3ZBV4; -.
DR   GeneID; 515652; -.
DR   KEGG; bta:515652; -.
DR   CTD; 9324; -.
DR   eggNOG; ENOG502S1R1; Eukaryota.
DR   HOGENOM; CLU_141985_2_2_1; -.
DR   InParanoid; Q3ZBV4; -.
DR   OrthoDB; 1617797at2759; -.
DR   Proteomes; UP000009136; 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   2: Evidence at transcript level;
KW   Chromatin regulator; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..100
FT                   /note="High mobility group nucleosome-binding domain-
FT                   containing protein 3"
FT                   /id="PRO_0000232573"
FT   REGION          1..100
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..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..100
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         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15651"
FT   MOD_RES         94
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15651"
SQ   SEQUENCE   100 AA;  10709 MW;  5B0B81ACF054952A CRC64;
     MPKRKSPENT EGKDGSKVTK QEPTRRSARL SAKPAPPKPE PKPRKTSAKK EPAAKVSKGV
     KGKKEEKQEA GKEGTAAPSE NGDTKTEEAQ KTESVANEGE