HMGB1_CRIGR
ID HMGB1_CRIGR Reviewed; 180 AA.
AC P07156;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=High mobility group protein B1;
DE AltName: Full=High mobility group protein 1;
DE Short=HMG-1;
DE Flags: Fragment;
GN Name=HMGB1; Synonyms=HMG-1, HMG1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3601666; DOI=10.1093/nar/15.13.5051;
RA Lee K.-L.D., Pentecost B.T., D'Anna J.A., Tobey R.A., Gurley L.R.,
RA Dixon G.H.;
RT "Characterization of cDNA sequences corresponding to three distinct HMG-1
RT mRNA species in line CHO Chinese hamster cells and cell cycle expression of
RT the HMG-1 gene.";
RL Nucleic Acids Res. 15:5051-5068(1987).
RN [2]
RP STRUCTURE BY NMR OF 57-136.
RX PubMed=8346022; DOI=10.1093/nar/21.15.3427;
RA Read C.M., Cary P.D., Crane-Robinson C., Driscoll P.C., Norman D.G.;
RT "Solution structure of a DNA-binding domain from HMG1.";
RL Nucleic Acids Res. 21:3427-3436(1993).
CC -!- FUNCTION: Multifunctional redox sensitive protein with various roles in
CC different cellular compartments. In the nucleus is one of the major
CC chromatin-associated non-histone proteins and acts as a DNA chaperone
CC involved in replication, transcription, chromatin remodeling, V(D)J
CC recombination, DNA repair and genome stability. Proposed to be an
CC universal biosensor for nucleic acids. Promotes host inflammatory
CC response to sterile and infectious signals and is involved in the
CC coordination and integration of innate and adaptive immune responses.
CC In the cytoplasm functions as sensor and/or chaperone for immunogenic
CC nucleic acids implicating the activation of TLR9-mediated immune
CC responses, and mediates autophagy. Acts as danger associated molecular
CC pattern (DAMP) molecule that amplifies immune responses during tissue
CC injury. Released to the extracellular environment can bind DNA,
CC nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE,
CC lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates
CC cells through engagement of multiple surface receptors. In the
CC extracellular compartment fully reduced HMGB1 (released by necrosis)
CC acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine,
CC and sulfonyl HMGB1 (released from apoptotic cells) promotes
CC immunological tolerance. Has proangiogenic activity. May be involved in
CC platelet activation. Binds to phosphatidylserine and
CC phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal
CC outgrowth. May play a role in accumulation of expanded polyglutamine
CC (polyQ) proteins. {ECO:0000250|UniProtKB:P09429,
CC ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}.
CC -!- FUNCTION: Nuclear functions are attributed to fully reduced HGMB1.
CC Associates with chromatin and binds DNA with a preference to non-
CC canonical DNA structures such as single-stranded DNA, DNA-containing
CC cruciforms or bent structures, supercoiled DNA and ZDNA. Can bent DNA
CC and enhance DNA flexibility by looping thus providing a mechanism to
CC promote activities on various gene promoters by enhancing transcription
CC factor binding and/or bringing distant regulatory sequences into close
CC proximity. May be involved in nucleotide excision repair (NER),
CC mismatch repair (MMR) and base excision repair (BER) pathways, and
CC double strand break repair such as non-homologous end joining (NHEJ).
CC Involved in V(D)J recombination by acting as a cofactor of the RAG
CC complex: acts by stimulating cleavage and RAG protein binding at the 23
CC bp spacer of conserved recombination signal sequences (RSS). In vitro
CC can displace histone H1 from highly bent DNA. Can restructure the
CC canonical nucleosome leading to relaxation of structural constraints
CC for transcription factor-binding. Enhances binding of sterol regulatory
CC element-binding proteins (SREBPs) such as SREBF1 to their cognate DNA
CC sequences and increases their transcriptional activities. Facilitates
CC binding of TP53 to DNA. May be involved in mitochondrial quality
CC control and autophagy in a transcription-dependent fashion implicating
CC HSPB1. Can modulate the activity of the telomerase complex and may be
CC involved in telomere maintenance. {ECO:0000250|UniProtKB:P09429,
CC ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158,
CC ECO:0000250|UniProtKB:P63159}.
CC -!- FUNCTION: In the cytoplasm proposed to dissociate the BECN1:BCL2
CC complex via competitive interaction with BECN1 leading to autophagy
CC activation. Can protect BECN1 and ATG5 from calpain-mediated cleavage
CC and thus proposed to control their proautophagic and proapoptotic
CC functions and to regulate the extent and severity of inflammation-
CC associated cellular injury. In myeloid cells has a protective role
CC against endotoxemia and bacterial infection by promoting autophagy.
CC Involved in endosomal translocation and activation of TLR9 in response
CC to CpG-DNA in macrophages. {ECO:0000250|UniProtKB:P09429,
CC ECO:0000250|UniProtKB:P63158}.
CC -!- FUNCTION: In the extracellular compartment (following either active
CC secretion or passive release) involved in regulation of the
CC inflammatory response. Fully reduced HGMB1 (which subsequently gets
CC oxidized after release) in association with CXCL12 mediates the
CC recruitment of inflammatory cells during the initial phase of tissue
CC injury; the CXCL12:HMGB1 complex triggers CXCR4 homodimerization.
CC Induces the migration of monocyte-derived immature dendritic cells and
CC seems to regulate adhesive and migratory functions of neutrophils
CC implicating AGER/RAGE and ITGAM. Can bind to various types of DNA and
CC RNA including microbial unmethylated CpG-DNA to enhance the innate
CC immune response to nucleic acids. Proposed to act in promiscuous
CC DNA/RNA sensing which cooperates with subsequent discriminative sensing
CC by specific pattern recognition receptors. Promotes extracellular DNA-
CC induced AIM2 inflammasome activation implicating AGER/RAGE. Disulfide
CC HMGB1 binds to transmembrane receptors, such as AGER/RAGE, TLR2, TLR4
CC and probably TREM1, thus activating their signal transduction pathways.
CC Mediates the release of cytokines/chemokines such as TNF, IL-1, IL-6,
CC IL-8, CCL2, CCL3, CCL4 and CXCL10.Promotes secretion of interferon-
CC gamma by macrophage-stimulated natural killer (NK) cells in concert
CC with other cytokines like IL-2 or IL-12. TLR4 is proposed to be the
CC primary receptor promoting macrophage activation and signaling through
CC TLR4 seems to implicate LY96/MD-2. In bacterial LPS- or LTA-mediated
CC inflammatory responses binds to the endotoxins and transfers them to
CC CD14 for signaling to the respective TLR4:LY96 and TLR2 complexes.
CC Contributes to tumor proliferation by association with ACER/RAGE. Can
CC bind to IL1-beta and signals through the IL1R1:IL1RAP receptor complex.
CC Binding to class A CpG activates cytokine production in plasmacytoid
CC dendritic cells implicating TLR9, MYD88 and AGER/RAGE and can activate
CC autoreactive B cells. Via HMGB1-containing chromatin immune complexes
CC may also promote B cell responses to endogenous TLR9 ligands through a
CC B-cell receptor (BCR)-dependent and ACER/RAGE-independent mechanism.
CC Inhibits phagocytosis of apoptotic cells by macrophages; the function
CC is dependent on poly-ADP-ribosylation and involves binding to
CC phosphatidylserine on the cell surface of apoptotic cells. In adaptive
CC immunity may be involved in enhancing immunity through activation of
CC effector T-cells and suppression of regulatory T (TReg) cells. In
CC contrast, without implicating effector or regulatory T-cells, required
CC for tumor infiltration and activation of T-cells expressing the
CC lymphotoxin LTA:LTB heterotrimer thus promoting tumor malignant
CC progression. Also reported to limit proliferation of T-cells. Released
CC HMGB1:nucleosome complexes formed during apoptosis can signal through
CC TLR2 to induce cytokine production. Involved in induction of
CC immunological tolerance by apoptotic cells; its pro-inflammatory
CC activities when released by apoptotic cells are neutralized by reactive
CC oxygen species (ROS)-dependent oxidation specifically on Cys-106.
CC During macrophage activation by activated lymphocyte-derived self
CC apoptotic DNA (ALD-DNA) promotes recruitment of ALD-DNA to endosomes.
CC {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103,
CC ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}.
CC -!- SUBUNIT: Interacts (fully reduced HMGB1) with CXCL12; probably in a 1:2
CC ratio involving two molecules of CXCL12, each interacting with one HMG
CC box of HMGB1; inhibited by glycyrrhizin. Associates with the TLR4:LY96
CC receptor complex. Component of the RAG complex composed of core
CC components RAG1 and RAG2, and associated component HMGB1 or HMGB2.
CC Interacts (in cytoplasm upon starvation) with BECN1; inhibits the
CC interaction of BECN1 and BCL2 leading to promotion of autophagy.
CC Interacts with KPNA1; involved in nuclear import. Interacts with
CC SREBF1, TLR2, TLR4, TLR9, PTPRZ1, APEX1, FEN1, POLB, TERT. Interacts
CC with IL1B, AGER, MSH2, XPA, XPC, HNF1A, TP53. Interacts with CD24; the
CC probable CD24:SIGLEC10 complex is proposed to inhibit HGMB1-mediated
CC tissue damage immune response. Interacts with THBD; prevents HGMB1
CC interaction with ACER/RAGE and inhibits HGMB1 pro-inflammatory
CC activity. Interacts with HAVCR2; impairs HMGB1 binding to B-DNA and
CC likely HMGB1-mediated innate immune response. Interacts with XPO1;
CC mediating nuclear export. {ECO:0000250|UniProtKB:P09429,
CC ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09429}.
CC Chromosome {ECO:0000250|UniProtKB:P10103,
CC ECO:0000250|UniProtKB:P63159}. Cytoplasm
CC {ECO:0000250|UniProtKB:P09429}. Secreted {ECO:0000250|UniProtKB:P09429,
CC ECO:0000250|UniProtKB:P63158}. Cell membrane
CC {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158,
CC ECO:0000250|UniProtKB:P63159}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158,
CC ECO:0000250|UniProtKB:P63159}; Extracellular side
CC {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158,
CC ECO:0000250|UniProtKB:P63159}. Endosome {ECO:0000250|UniProtKB:P63158}.
CC Endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000250|UniProtKB:P63158}. Note=In basal state predominantly
CC nuclear. Shuttles between the cytoplasm and the nucleus. Translocates
CC from the nucleus to the cytoplasm upon autophagy stimulation. Release
CC from macrophages in the extracellular milieu requires the activation of
CC NLRC4 or NLRP3 inflammasomes (By similarity). Passively released to the
CC extracellular milieu from necrotic cells by diffusion, involving the
CC fully reduced HGMB1 which subsequently gets oxidized. Also released
CC from apoptotic cells. Active secretion from a variety of immune and
CC non-immune cells such as macrophages, monocytes, neutrophils, dendritic
CC cells, natural killer cells and plasma cells in response to various
CC stimuli such as LPS and cytokines involves a nonconventional secretory
CC process via secretory lysosomes. Found on the surface of activated
CC platelets. {ECO:0000250|UniProtKB:P09429,
CC ECO:0000250|UniProtKB:P63158}.
CC -!- DOMAIN: HMG box 2 mediates pro-inflammatory cytokine-stimulating
CC activity and binding to TLR4. However, not involved in mediating
CC immunogenic activity in the context of apoptosis-induced immune
CC tolerance. {ECO:0000250|UniProtKB:P09429}.
CC -!- DOMAIN: The acidic C-terminal domain forms a flexible structure which
CC can reversibly interact intramolecularily with the HMG boxes and
CC modulate binding to DNA and other proteins.
CC {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63159}.
CC -!- PTM: Phosphorylated at serine residues. Phosphorylation in both NLS
CC regions is required for cytoplasmic translocation followed by
CC secretion. {ECO:0000250|UniProtKB:P09429}.
CC -!- PTM: Acetylated on multiple sites upon stimulation with LPS (By
CC similarity). Acetylation on lysine residues in the nuclear localization
CC signals (NLS 1 and NLS 2) leads to cytoplasmic localization and
CC subsequent secretion (By similarity). {ECO:0000250|UniProtKB:P09429,
CC ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}.
CC -!- PTM: Reduction/oxidation of cysteine residues and a possible
CC intramolecular disulfide bond give rise to different redox forms with
CC specific functional activities in various cellular compartments:
CC 1- fully reduced HMGB1 (HMGB1C23hC45hC106h), 2-disulfide HMGB1
CC (HMGB1C23-C45C106h) and 3- sulfonyl HMGB1 (HMGB1C23soC45soC106so).
CC {ECO:0000250|UniProtKB:P09429}.
CC -!- PTM: Poly-ADP-ribosylated by PARP1 when secreted following stimulation
CC with LPS (By similarity). {ECO:0000250|UniProtKB:P63158}.
CC -!- PTM: In vitro cleavage by CASP1 is liberating a HMG box 1-containing
CC peptide which may mediate immunogenic activity; the peptide antagonizes
CC apoptosis-induced immune tolerance. Can be proteolytically cleaved by a
CC thrombin:thrombomodulin complex; reduces binding to heparin and pro-
CC inflammatory activities (By similarity). {ECO:0000250|UniProtKB:P09429,
CC ECO:0000250|UniProtKB:P10103}.
CC -!- PTM: Forms covalent cross-links mediated by transglutaminase TGM2,
CC between a glutamine and the epsilon-amino group of a lysine residue,
CC forming homopolymers and heteropolymers.
CC {ECO:0000250|UniProtKB:P09429}.
CC -!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
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DR EMBL; Y00365; CAA68441.1; -; Genomic_DNA.
DR PIR; A27853; A27853.
DR PDB; 1HSM; NMR; -; A=58-136.
DR PDB; 1HSN; NMR; -; A=58-136.
DR PDB; 1NHM; NMR; -; A=58-136.
DR PDB; 1NHN; NMR; -; A=58-136.
DR PDBsum; 1HSM; -.
DR PDBsum; 1HSN; -.
DR PDBsum; 1NHM; -.
DR PDBsum; 1NHN; -.
DR AlphaFoldDB; P07156; -.
DR BMRB; P07156; -.
DR SMR; P07156; -.
DR STRING; 10029.XP_007630683.1; -.
DR eggNOG; KOG0381; Eukaryota.
DR EvolutionaryTrace; P07156; -.
DR GO; GO:0000793; C:condensed chromosome; ISS:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0043277; P:apoptotic cell clearance; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0017055; P:negative regulation of RNA polymerase II transcription preinitiation complex assembly; ISS:UniProtKB.
DR GO; GO:0097350; P:neutrophil clearance; ISS:UniProtKB.
DR GO; GO:0051106; P:positive regulation of DNA ligation; ISS:UniProtKB.
DR GO; GO:0034165; P:positive regulation of toll-like receptor 9 signaling pathway; ISS:UniProtKB.
DR GO; GO:0002840; P:regulation of T cell mediated immune response to tumor cell; ISS:UniProtKB.
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; IPR031076; HMGB1.
DR PANTHER; PTHR48112:SF4; PTHR48112:SF4; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Adaptive immunity; ADP-ribosylation; Autophagy;
KW Cell membrane; Chemotaxis; Chromosome; Cytoplasm; Disulfide bond;
KW DNA damage; DNA recombination; DNA repair; DNA-binding; Endosome; Immunity;
KW Inflammatory response; Innate immunity; Isopeptide bond; Membrane; Nucleus;
KW Oxidation; Phosphoprotein; Repeat; Secreted.
FT CHAIN <1..180
FT /note="High mobility group protein B1"
FT /id="PRO_0000048525"
FT DNA_BIND <1..44
FT /note="HMG box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT DNA_BIND 60..128
FT /note="HMG box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 45..61
FT /note="LPS binding (Lipid A)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT REGION 54..73
FT /note="Cytokine-stimulating activity"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT REGION 115..148
FT /note="Binding to AGER/RAGE"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT REGION 126..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..149
FT /note="NLS 2"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOTIF <1..8
FT /note="Nuclear localization signal (NLS) 1"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOTIF 143..149
FT /note="Nuclear localization signal (NLS) 2"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT COMPBIAS 126..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 32..33
FT /note="Cleavage; by CASP1"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63158"
FT MOD_RES 10
FT /note="Cysteine sulfonic acid (-SO3H)"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63158"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT MOD_RES 71
FT /note="Cysteine sulfonic acid (-SO3H)"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 93
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 106
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63158"
FT MOD_RES 137
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 138
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 142
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 145
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 146
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT MOD_RES 147
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 148
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 149
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 150
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT CROSSLNK 8
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-?)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT CROSSLNK 9
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-?)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT CROSSLNK 33
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-?)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT CROSSLNK 145
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-?)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT CROSSLNK 147
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-?)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT CROSSLNK 148
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-?)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT CROSSLNK 149
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-?)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT NON_TER 1
FT HELIX 67..81
FT /evidence="ECO:0007829|PDB:1HSM"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1HSM"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:1HSM"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1HSM"
FT HELIX 107..130
FT /evidence="ECO:0007829|PDB:1HSM"
FT TURN 131..135
FT /evidence="ECO:0007829|PDB:1HSM"
SQ SEQUENCE 180 AA; 20904 MW; F624392F41609854 CRC64;
VNFSEFSKKC SERWKTMSAK EKGKFEDMAK ADKARYEREM KTYIPPKGET KKKFKDPNAP
KRPPSAFFLF CSEYRPKIKG EHPGLSIGDV AKKLGEMWNN TAADDKQPYE KKAAKLKEKY
EKDIAAYRAK GKPDAAKKGV VKAEKSKKKK EEEDDEEDEE DEEEEEEEED EDEEEDDDDE
