HMGB2_CHICK
ID HMGB2_CHICK Reviewed; 207 AA.
AC P26584;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=High mobility group protein B2;
DE AltName: Full=High mobility group protein 2;
DE Short=HMG-2;
GN Name=HMGB2; Synonyms=HMG2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1572546; DOI=10.1016/0378-1119(92)90403-c;
RA Davis D.L., Burch J.B.E.;
RT "Isolation of a chicken HMG2 cDNA clone and evidence for an HMG2-specific
RT 3'-untranslated region.";
RL Gene 113:251-256(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1601311; DOI=10.1016/0378-1119(92)90590-l;
RA Sparrow D.B., Wells J.R.E.;
RT "Sequence of a cDNA encoding chicken high-mobility-group protein-2.";
RL Gene 114:289-290(1992).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14672558; DOI=10.1038/sj.cr.7290180;
RA Zhang S.B., Huang J., Zhao H., Zhang Y., Hou C.H., Cheng X.D., Jiang C.,
RA Li M.Q., Hu J., Qian R.L.;
RT "The in vitro reconstitution of nucleosome and its binding patterns with
RT HMG1/2 and HMG14/17 proteins.";
RL Cell Res. 13:351-359(2003).
CC -!- FUNCTION: Multifunctional protein with various roles in different
CC cellular compartments. May act in a redox sensitive manner (By
CC similarity). Associates with chromatin and binds DNA with a preference
CC to non-canonical DNA structures such as single-stranded DNA
CC (PubMed:14672558). Can bent DNA and enhance DNA flexibility by looping
CC thus providing a mechanism to promote activities on various gene
CC promoters. Proposed to be involved in the innate immune response to
CC nucleic acids by acting as a cytoplasmic promiscuous immunogenic
CC DNA/RNA sensor. Involved in inflammatory response to antigenic stimulus
CC coupled with pro-inflammatory activity (By similarity).
CC {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P26583,
CC ECO:0000250|UniProtKB:P30681, ECO:0000269|PubMed:14672558}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14672558}. Chromosome
CC {ECO:0000305}. Cytoplasm {ECO:0000305}. Secreted {ECO:0000305}.
CC -!- PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-
CC 106 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 HMGB2
CC (HMGB2C23hC45hC106h), 2- disulfide HMGB2 (HMGB2C23-C45C106h) and
CC 3- sulfonyl HMGB2 (HMGB2C23soC45soC106so).
CC {ECO:0000250|UniProtKB:P09429}.
CC -!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
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DR EMBL; M83235; AAA48818.1; -; mRNA.
DR EMBL; M80574; AAA48819.1; -; mRNA.
DR PIR; JC1114; JC1114.
DR PIR; JC1129; JC1129.
DR RefSeq; NP_990817.1; NM_205486.1.
DR AlphaFoldDB; P26584; -.
DR SMR; P26584; -.
DR BioGRID; 676729; 1.
DR STRING; 9031.ENSGALP00000017462; -.
DR PaxDb; P26584; -.
DR GeneID; 396482; -.
DR KEGG; gga:396482; -.
DR CTD; 3148; -.
DR VEuPathDB; HostDB:geneid_396482; -.
DR eggNOG; KOG0381; Eukaryota.
DR InParanoid; P26584; -.
DR OrthoDB; 1641977at2759; -.
DR PhylomeDB; P26584; -.
DR PRO; PR:P26584; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000793; C:condensed chromosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:AgBase.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0008301; F:DNA binding, bending; IDA:AgBase.
DR GO; GO:0000400; F:four-way junction DNA binding; IDA:AgBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:AgBase.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:AgBase.
DR GO; GO:0032392; P:DNA geometric change; IDA:AgBase.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; ISS:AgBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISS:AgBase.
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 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 Chromosome; Cytoplasm; Disulfide bond; DNA recombination; DNA-binding;
KW Immunity; Inflammatory response; Innate immunity; Nucleus; Oxidation;
KW Reference proteome; Repeat; Secreted; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..207
FT /note="High mobility group protein B2"
FT /id="PRO_0000048538"
FT DNA_BIND 9..79
FT /note="HMG box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT DNA_BIND 95..163
FT /note="HMG box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 52..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..207
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Cysteine sulfonic acid (-SO3H); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOD_RES 45
FT /note="Cysteine sulfonic acid (-SO3H); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOD_RES 106
FT /note="Cysteine sulfonic acid (-SO3H)"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT DISULFID 23..45
FT /note="In disulfide HMGB2"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT CONFLICT 24..25
FT /note="RE -> PR (in Ref. 2; AAA48819)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="L -> S (in Ref. 2; AAA48819)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 207 AA; 23828 MW; 1099C6EF3CC0B7FA CRC64;
MGKGDPNKPR GKMSSYAYFV QTCREEHKKK HPDSSVNFAE FSRKCSERWK TMSSKEKGKF
EEMAKGDKAR YDREMKNYVP PKGEKKGKKK DPNAPKRPPS AFFLFCSEHR PKIKNDHPGL
SIGDTAKKLG EMWSEQLAKD KQPYEQKAAK LKEKYEKDIA AYRAKSKSDA GKKGPGRPAG
SKKKAEPEEE EEEEEDEEEE EEEEDEE
