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High mobility group protein B1 (High mobility group protein 1) (HMG-1)

 HMGB1_PIG               Reviewed;         215 AA.
P12682;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
31-JAN-2018, entry version 135.
RecName: Full=High mobility group protein B1;
AltName: Full=High mobility group protein 1;
Short=HMG-1;
Name=HMGB1; Synonyms=HMG1;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3191113; DOI=10.1021/bi00416a050;
Tsuda K., Kikuchi M., Mori K., Waga S., Yoshida M.;
"Primary structure of non-histone protein HMG1 revealed by the
nucleotide sequence.";
Biochemistry 27:6159-6163(1988).
[2]
FUNCTION.
PubMed=14660645; DOI=10.1074/jbc.M306793200;
Park J.S., Svetkauskaite D., He Q., Kim J.Y., Strassheim D.,
Ishizaka A., Abraham E.;
"Involvement of toll-like receptors 2 and 4 in cellular activation by
high mobility group box 1 protein.";
J. Biol. Chem. 279:7370-7377(2004).
-!- FUNCTION: Multifunctional redox sensitive protein with various
roles in different cellular compartments. In the nucleus is one of
the major chromatin-associated non-histone proteins and acts as a
DNA chaperone involved in replication, transcription, chromatin
remodeling, V(D)J recombination, DNA repair and genome stability.
Proposed to be an universal biosensor for nucleic acids. Promotes
host inflammatory response to sterile and infectious signals and
is involved in the coordination and integration of innate and
adaptive immune responses. In the cytoplasm functions as sensor
and/or chaperone for immunogenic nucleic acids implicating the
activation of TLR9-mediated immune responses, and mediates
autophagy. Acts as danger associated molecular pattern (DAMP)
molecule that amplifies immune responses during tissue injury.
Released to the extracellular environment can bind DNA,
nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE,
lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and
activates cells through engagement of multiple surface receptors.
In the extracellular compartment fully reduced HMGB1 (released by
necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted)
as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells)
promotes immunological tolerance. Has proangiogenic activity. May
be involved in platelet activation. Binds to phosphatidylserine
and phosphatidylethanolamide. Bound to RAGE mediates signaling for
neuronal outgrowth. May play a role in accumulation of expanded
polyglutamine (polyQ) proteins (By similarity).
{ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103,
ECO:0000250|UniProtKB:P63159, ECO:0000305}.
-!- FUNCTION: Nuclear functions are attributed to fully reduced HGMB1.
Associates with chromatin and binds DNA with a preference to non-
canonical DNA structures such as single-stranded DNA, DNA-
containing cruciforms or bent structures, supercoiled DNA and
ZDNA. Can bent DNA and enhance DNA flexibility by looping thus
providing a mechanism to promote activities on various gene
promoters by enhancing transcription factor binding and/or
bringing distant regulatory sequences into close proximity. May be
involved in nucleotide excision repair (NER), mismatch repair
(MMR) and base excision repair (BER) pathways, and double strand
break repair such as non-homologous end joining (NHEJ). Involved
in V(D)J recombination by acting as a cofactor of the RAG complex:
acts by stimulating cleavage and RAG protein binding at the 23 bp
spacer of conserved recombination signal sequences (RSS). In vitro
can displace histone H1 from highly bent DNA. Can restructure the
canonical nucleosome leading to relaxation of structural
constraints for transcription factor-binding. Enhances binding of
sterol regulatory element-binding proteins (SREBPs) such as SREBF1
to their cognate DNA sequences and increases their transcriptional
activities. Facilitates binding of TP53 to DNA. May be involved in
mitochondrial quality control and autophagy in a transcription-
dependent fashion implicating HSPB1. Can modulate the activity of
the telomerase complex and may be involved in telomere maintenance
(By similarity). {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158,
ECO:0000250|UniProtKB:P63159}.
-!- FUNCTION: In the cytoplasm proposed to dissociate the BECN1:BCL2
complex via competitive interaction with BECN1 leading to
autophagy activation. Can protect BECN1 and ATG5 from calpain-
mediated cleavage and thus proposed to control their proautophagic
and proapoptotic functions and to regulate the extent and severity
of inflammation-associated cellular injury. In myeloid cells has a
protective role against endotoxemia and bacterial infection by
promoting autophagy. Involved in endosomal translocation and
activation of TLR9 in response to CpG-DNA in macrophages (By
similarity). {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P63158}.
-!- FUNCTION: In the extracellular compartment (following either
active secretion or passive release) involved in regulation of the
inflammatory response. Fully reduced HGMB1 (which subsequently
gets oxidized after release) in association with CXCL12 mediates
the recruitment of inflammatory cells during the initial phase of
tissue injury; the CXCL12:HMGB1 complex triggers CXCR4
homodimerization. Induces the migration of monocyte-derived
immature dendritic cells and seems to regulate adhesive and
migratory functions of neutrophils implicating AGER/RAGE and
ITGAM. Can bind to various types of DNA and RNA including
microbial unmethylated CpG-DNA to enhance the innate immune
response to nucleic acids. Proposed to act in promiscuous DNA/RNA
sensing which cooperates with subsequent discriminative sensing by
specific pattern recognition receptors (By similarity). Promotes
extracellular DNA-induced AIM2 inflammasome activation implicating
AGER/RAGE. Disulfide HMGB1 binds to transmembrane receptors, such
as AGER/RAGE, TLR2, TLR4 and probably TREM1, thus activating their
signal transduction pathways (PubMed:14660645). Mediates the
release of cytokines/chemokines such as TNF, IL-1, IL-6, IL-8,
CCL2, CCL3, CCL4 and CXCL10. Promotes secretion of interferon-
gamma by macrophage-stimulated natural killer (NK) cells in
concert with other cytokines like IL-2 or IL-12. TLR4 is proposed
to be the primary receptor promoting macrophage activation and
signaling through TLR4 seems to implicate LY96/MD-2. In bacterial
LPS- or LTA-mediated inflammatory responses binds to the
endotoxins and transfers them to CD14 for signaling to the
respective TLR4:LY96 and TLR2 complexes. Contributes to tumor
proliferation by association with ACER/RAGE. Can bind to IL1-beta
and signals through the IL1R1:IL1RAP receptor complex. Binding to
class A CpG activates cytokine production in plasmacytoid
dendritic cells implicating TLR9, MYD88 and AGER/RAGE and can
activate autoreactive B cells. Via HMGB1-containing chromatin
immune complexes may also promote B cell responses to endogenous
TLR9 ligands through a B-cell receptor (BCR)-dependent and
ACER/RAGE-independent mechanism. Inhibits phagocytosis of
apoptotic cells by macrophages; the function is dependent on poly-
ADP-ribosylation and involves binding to phosphatidylserine on the
cell surface of apoptotic cells. In adaptive immunity may be
involved in enhancing immunity through activation of effector T
cells and suppression of regulatory T (TReg) cells. In contrast,
without implicating effector or regulatory T-cells, required for
tumor infiltration and activation of T-cells expressing the
lymphotoxin LTA:LTB heterotrimer thus promoting tumor malignant
progression. Also reported to limit proliferation of T-cells.
Released HMGB1:nucleosome complexes formed during apoptosis can
signal through TLR2 to induce cytokine production. Involved in
induction of immunological tolerance by apoptotic cells; its pro-
inflammatory activities when released by apoptotic cells are
neutralized by reactive oxygen species (ROS)-dependent oxidation
specifically on Cys-106. During macrophage activation by activated
lymphocyte-derived self apoptotic DNA (ALD-DNA) promotes
recruitment of ALD-DNA to endosomes (By similarity).
{ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103,
ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159,
ECO:0000269|PubMed:14660645}.
-!- SUBUNIT: Interacts (fully reduced HMGB1) with CXCL12; probably in
a 1:2 ratio involving two molecules of CXCL12, each interacting
with one HMG box of HMGB1; inhibited by glycyrrhizin. Associates
with the TLR4:LY96 receptor complex. Component of the RAG complex
composed of core components RAG1 and RAG2, and associated
component HMGB1 or HMGB2. Interacts (in cytoplasm upon starvation)
with BECN1; inhibits the interaction of BECN1 and BCL2 leading to
promotion of autophagy. Interacts with KPNA1; involved in nuclear
import. Interacts with SREBF1, TLR2, TLR4, TLR9, PTPRZ1, APEX1,
FEN1, POLB, TERT. Interacts with IL1B, AGER, MSH2, XPA, XPC,
HNF1A, TP53. Interacts with CD24; the probable CD24:SIGLEC10
complex is proposed to inhibit HGMB1-mediated tissue damage immune
response. Interacts with THBD; prevents HGMB1 interaction with
ACER/RAGE and inhibits HGMB1 proinflammatory activity. Interacts
with HAVCR2; impairs HMGB1 binding to B-DNA and likely HMGB1-
mediated innate immume response. Interacts with XPO1; mediating
nuclear export. {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09429}.
Chromosome {ECO:0000250|UniProtKB:P10103,
ECO:0000250|UniProtKB:P63159}. Cytoplasm
{ECO:0000250|UniProtKB:P09429}. Secreted
{ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}. Cell
membrane {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159};
Peripheral membrane protein {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159};
Extracellular side {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}.
Endosome {ECO:0000250|UniProtKB:P63158}. Endoplasmic reticulum-
Golgi intermediate compartment {ECO:0000250|UniProtKB:P63158}.
Note=In basal state predominantly nuclear. Shuttles between the
cytoplasm and the nucleus. Translocates from the nucleus to the
cytoplasm upon autophagy stimulation. Release from macrophages in
the extracellular milieu requires the activation of NLRC4 or NLRP3
inflammasomes (By similarity). Passively released to the
extracellular milieu from necrotic cells by diffusion, involving
the fully reduced HGMB1 which subsequently gets oxidized. Also
released from apoptotic cells. Active secretion from a variety of
immune and non-immune cells such as macrophages, monocytes,
neutrophils, dendritic cells, natural killer cells and plasma
cells in response to various stimuli such as LPS and cytokines
involves a nonconventional secretory process via secretory
lysosomes. Found on the surface of activated platelets.
{ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}.
-!- DOMAIN: HMG box 2 mediates proinflammatory cytokine-stimulating
activity and binding to TLR4. However, not involved in mediating
immunogenic activity in the context of apoptosis-induced immune
tolerance. {ECO:0000250|UniProtKB:P09429}.
-!- DOMAIN: The acidic C-terminal domain forms a flexible structure
which can reversibly interact intramolecularily with the HMG boxes
and modulate binding to DNA and other proteins.
{ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63159}.
-!- PTM: Phosphorylated at serine residues. Phosphorylation in both
NLS regions is required for cytoplasmic translocation followed by
secretion. {ECO:0000250|UniProtKB:P09429}.
-!- PTM: Acetylated on multiple sites upon stimulation with LPS (By
similarity). Acetylation on lysine residues in the nuclear
localization signals (NLS 1 and NLS 2) leads to cytoplasmic
localization and subsequent secretion. Acetylation on Lys-3
results in preferential binding to DNA ends and impairs DNA
bending activity. {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}.
-!- PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and
Cys-106 and a possible intramolecular disulfide bond involving
Cys-23 and Cys-45 give rise to different redox forms with specific
functional activities in various cellular compartments: 1- fully
reduced HMGB1 (HMGB1C23hC45hC106h), 2- disulfide HMGB1 (HMGB1C23-
C45C106h) and 3- sulfonyl HMGB1 (HMGB1C23soC45soC106so).
{ECO:0000250|UniProtKB:P09429}.
-!- PTM: Poly-ADP-ribosylated by PARP1 when secreted following
stimulation with LPS. {ECO:0000250|UniProtKB:P63158}.
-!- PTM: In vitro cleavage by CASP1 is liberating a HMG box 1-
containing peptide which may mediate immunogenic activity; the
peptide antagonizes apoptosis-induced immune tolerance. Can be
proteolytically cleaved by a thrombin:thrombomodulin complex;
reduces binding to heparin and proinflammatory activities (By
similarity). {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P10103}.
-!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
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EMBL; M21683; AAA31050.1; -; mRNA.
PIR; A28897; A28897.
RefSeq; NP_001004034.1; NM_001004034.1.
UniGene; Ssc.22696; -.
ProteinModelPortal; P12682; -.
SMR; P12682; -.
IntAct; P12682; 2.
STRING; 9823.ENSSSCP00000009955; -.
PaxDb; P12682; -.
PeptideAtlas; P12682; -.
PRIDE; P12682; -.
GeneID; 445521; -.
KEGG; ssc:445521; -.
CTD; 3146; -.
eggNOG; KOG0381; Eukaryota.
eggNOG; COG5648; LUCA.
HOGENOM; HOG000197861; -.
HOVERGEN; HBG009000; -.
InParanoid; P12682; -.
KO; K10802; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0005623; C:cell; IDA:AgBase.
GO; GO:0000793; C:condensed chromosome; ISS:UniProtKB.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0000790; C:nuclear chromatin; IDA:AgBase.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0000405; F:bubble DNA binding; ISS:AgBase.
GO; GO:0000400; F:four-way junction DNA binding; ISS:AgBase.
GO; GO:0044378; F:non-sequence-specific DNA binding, bending; IDA:AgBase.
GO; GO:0097100; F:supercoiled DNA binding; ISS:AgBase.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0043277; P:apoptotic cell clearance; ISS:UniProtKB.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
GO; GO:0032392; P:DNA geometric change; ISS:AgBase.
GO; GO:0051103; P:DNA ligation involved in DNA repair; IDA:UniProtKB.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IDA:UniProtKB.
GO; GO:0017055; P:negative regulation of RNA polymerase II transcriptional preinitiation complex assembly; ISS:UniProtKB.
GO; GO:0097350; P:neutrophil clearance; ISS:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; IDA:AgBase.
GO; GO:0051106; P:positive regulation of DNA ligation; ISS:UniProtKB.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0034165; P:positive regulation of toll-like receptor 9 signaling pathway; ISS:UniProtKB.
GO; GO:0002840; P:regulation of T cell mediated immune response to tumor cell; ISS:UniProtKB.
GO; GO:0034134; P:toll-like receptor 2 signaling pathway; IDA:UniProtKB.
GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IDA:UniProtKB.
Gene3D; 1.10.30.10; -; 2.
InterPro; IPR009071; HMG_box_dom.
InterPro; IPR036910; HMG_box_dom_sf.
InterPro; IPR017967; HMG_boxA_CS.
Pfam; PF00505; HMG_box; 1.
Pfam; PF09011; HMG_box_2; 1.
SMART; SM00398; HMG; 2.
SUPFAM; SSF47095; SSF47095; 2.
PROSITE; PS00353; HMG_BOX_1; 1.
PROSITE; PS50118; HMG_BOX_2; 2.
2: Evidence at transcript level;
Acetylation; Adaptive immunity; ADP-ribosylation; Autophagy;
Cell membrane; Chemotaxis; Chromosome; Complete proteome; Cytoplasm;
Disulfide bond; DNA damage; DNA recombination; DNA repair;
DNA-binding; Endosome; Immunity; Inflammatory response;
Innate immunity; Membrane; Nucleus; Oxidation; Phosphoprotein;
Reference proteome; Repeat; Secreted.
CHAIN 1 215 High mobility group protein B1.
/FTId=PRO_0000048529.
DNA_BIND 9 79 HMG box 1. {ECO:0000255|PROSITE-
ProRule:PRU00267}.
DNA_BIND 95 163 HMG box 2. {ECO:0000255|PROSITE-
ProRule:PRU00267}.
REGION 1 97 Sufficient for interaction with HAVCR2.
{ECO:0000250|UniProtKB:P63158}.
REGION 1 10 Heparin-binding.
{ECO:0000250|UniProtKB:P10103}.
REGION 3 15 LPS binding (delipidated).
{ECO:0000250|UniProtKB:P09429}.
REGION 80 96 LPS binding (Lipid A).
{ECO:0000250|UniProtKB:P09429}.
REGION 89 108 Cytokine-stimulating activity.
{ECO:0000250|UniProtKB:P09429}.
REGION 150 183 Binding to AGER/RAGE.
{ECO:0000250|UniProtKB:P63159}.
MOTIF 27 43 Nuclear localization signal (NLS) 1.
{ECO:0000250|UniProtKB:P63159}.
MOTIF 178 184 Nuclear localization signal (NLS) 2.
{ECO:0000250|UniProtKB:P63159}.
COMPBIAS 186 215 Asp/Glu-rich (acidic).
SITE 10 11 Cleavage; by thrombin:thrombomodulin.
{ECO:0000250|UniProtKB:P10103}.
SITE 67 68 Cleavage; by CASP1.
{ECO:0000250|UniProtKB:P09429}.
MOD_RES 3 3 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 7 7 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 8 8 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 12 12 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 23 23 Cysteine sulfonic acid (-SO3H);
alternate.
{ECO:0000250|UniProtKB:P63159}.
MOD_RES 28 28 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 29 29 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 30 30 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000250|UniProtKB:P09429}.
MOD_RES 43 43 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63158}.
MOD_RES 45 45 Cysteine sulfonic acid (-SO3H);
alternate.
{ECO:0000250|UniProtKB:P63159}.
MOD_RES 90 90 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63158}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000250|UniProtKB:P09429}.
MOD_RES 106 106 Cysteine sulfonic acid (-SO3H).
{ECO:0000250|UniProtKB:P63159}.
MOD_RES 127 127 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 128 128 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 141 141 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63158}.
MOD_RES 172 172 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 173 173 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 177 177 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 180 180 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 181 181 ADP-ribosylserine.
{ECO:0000250|UniProtKB:P09429}.
MOD_RES 182 182 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 183 183 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 184 184 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 185 185 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
DISULFID 23 45 In disulfide HMGB1; alternate.
{ECO:0000250|UniProtKB:P63159}.
SEQUENCE 215 AA; 24917 MW; 8BDCAECF68F62AB5 CRC64;
MGKGDPKKPR GKMSSYAFFV QTCREEHKKK HPDASVNFSE FSKKCSERWK TMSAKEKGKF
EDMAKADKAR YEREMKTYIP PKGETKKKFK DPNAPKRPPS AFFLFCSEYR PKIKGEHPGL
SIGDVAKKLG EMWNNTAADD KHPYEKKAAK LKEKYEKDIA AYRAKGKPDA AKKGVVKAEK
SKKKKEEEED EEDEEDEEEE EDEEDEEEEE DDDDE


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