HMGB3_BOVIN
ID HMGB3_BOVIN Reviewed; 200 AA.
AC Q32L31;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=High mobility group protein B3;
GN Name=HMGB3;
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=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Multifunctional protein with various roles in different
CC cellular compartments. May act in a redox sensitive manner. Associates
CC with chromatin and binds DNA with a preference to non-canonical DNA
CC structures such as single-stranded DNA. Can bent DNA and enhance DNA
CC flexibility by looping thus providing a mechanism to promote activities
CC on various gene promoters. Proposed to be involved in the innate immune
CC response to nucleic acids by acting as a cytoplasmic promiscuous
CC immunogenic DNA/RNA sensor. Negatively regulates B-cell and myeloid
CC cell differentiation. In hematopoietic stem cells may regulate the
CC balance between self-renewal and differentiation. Involved in negative
CC regulation of canonical Wnt signaling (By similarity).
CC {ECO:0000250|UniProtKB:O54879, ECO:0000250|UniProtKB:P09429,
CC ECO:0000250|UniProtKB:P40618}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40618,
CC ECO:0000255|PROSITE-ProRule:PRU00267}. Chromosome {ECO:0000305}.
CC Cytoplasm {ECO:0000250|UniProtKB:O54879}.
CC -!- PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-
CC 104 and a possible intramolecular disulfide bond involving Cys-23 and
CC Cys-45 give rise to different redox forms with specific functional
CC activities in various cellular compartments: 1- fully reduced HMGB3
CC (HMGB3C23hC45hC104h), 2- disulfide HMGB3 (HMGB3C23-C45C104h) and
CC 3- sulfonyl HMGB3 (HMGB3C23soC45soC104so).
CC {ECO:0000250|UniProtKB:P09429}.
CC -!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI09794.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC109793; AAI09794.1; ALT_INIT; mRNA.
DR RefSeq; NP_001069753.2; NM_001076285.2.
DR RefSeq; NP_001106728.1; NM_001113257.2.
DR AlphaFoldDB; Q32L31; -.
DR SMR; Q32L31; -.
DR STRING; 9913.ENSBTAP00000006785; -.
DR PaxDb; Q32L31; -.
DR PeptideAtlas; Q32L31; -.
DR PRIDE; Q32L31; -.
DR GeneID; 613729; -.
DR KEGG; bta:613729; -.
DR CTD; 3149; -.
DR eggNOG; KOG0381; Eukaryota.
DR HOGENOM; CLU_082854_0_0_1; -.
DR InParanoid; Q32L31; -.
DR OrthoDB; 1641977at2759; -.
DR TreeFam; TF105371; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008301; F:DNA binding, bending; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0000400; F:four-way junction DNA binding; ISS:AgBase.
DR GO; GO:0032392; P:DNA geometric change; ISS:AgBase.
DR GO; GO:0006310; P:DNA recombination; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.30.10; -; 2.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR017967; HMG_boxA_CS.
DR InterPro; IPR031077; HMGB3.
DR PANTHER; PTHR48112:SF14; PTHR48112:SF14; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF09011; HMG_box_2; 1.
DR SMART; SM00398; HMG; 2.
DR SUPFAM; SSF47095; SSF47095; 2.
DR PROSITE; PS00353; HMG_BOX_1; 1.
DR PROSITE; PS50118; HMG_BOX_2; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Chromosome; Cytoplasm; Disulfide bond; DNA-binding; Immunity;
KW Innate immunity; Nucleus; Oxidation; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..200
FT /note="High mobility group protein B3"
FT /id="PRO_0000286355"
FT DNA_BIND 9..79
FT /note="HMG box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT DNA_BIND 93..161
FT /note="HMG box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 71..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..200
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOD_RES 23
FT /note="Cysteine sulfonic acid (-SO3H); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63158"
FT MOD_RES 45
FT /note="Cysteine sulfonic acid (-SO3H); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT MOD_RES 104
FT /note="Cysteine sulfonic acid (-SO3H)"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30681"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63158"
FT DISULFID 23..45
FT /note="In disulfide HMGB3; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63159"
SQ SEQUENCE 200 AA; 22896 MW; DF9A3404FA242EFC CRC64;
MAKGDPKKPK GKMSAYAFFV QTCREEHKKK NPEVPVNFAE FSKKCSERWK TMSGKEKSKF
DEMAKADKVR YDREMKDYGP AKGGKKKKDP NAPKRPPSGF FLFCSEFRPK IKSANPGISI
GDVAKKLGEM WNNLSDSEKQ PYINKAAKLK EKYEKDVADY KSKGKFDGAK GAAKVARKKV
EEEDEEDEEE EEEEEEEEDE
