ID   HMGL_IPONI              Reviewed;         144 AA.
AC   P40619;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=HMG1/2-like protein;
OS   Ipomoea nil (Japanese morning glory) (Pharbitis nil).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX   NCBI_TaxID=35883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cotyledon;
RX   PubMed=8251634; DOI=10.1007/bf00021536;
RA   Zheng C.C., Bui A.Q., O'Neill S.D.;
RT   "Abundance of an mRNA encoding a high mobility group DNA-binding protein is
RT   regulated by light and an endogenous rhythm.";
RL   Plant Mol. Biol. 23:813-823(1993).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC   -!- TISSUE SPECIFICITY: Expressed at higher levels in dark-grown tissues,
CC       such as roots; and at lower levels in light-grown tissues, such as
CC       cotyledons and stems.
CC   -!- INDUCTION: Regulated by darkness and by a circadian rhythm.
CC   -!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
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DR   EMBL; L12169; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; S40302; S40302.
DR   RefSeq; XP_019182556.1; XM_019327011.1.
DR   AlphaFoldDB; P40619; -.
DR   SMR; P40619; -.
DR   GeneID; 109177607; -.
DR   KEGG; ini:109177607; -.
DR   OrthoDB; 1641977at2759; -.
DR   GO; GO:0000785; C:chromatin; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003682; F:chromatin binding; IEA:UniProt.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:UniProt.
DR   Gene3D; 1.10.30.10; -; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR031061; HMGB_plant.
DR   PANTHER; PTHR46261; PTHR46261; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus.
FT   CHAIN           1..144
FT                   /note="HMG1/2-like protein"
FT                   /id="PRO_0000048555"
FT   DNA_BIND        36..105
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..144
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   144 AA;  16057 MW;  B8DE2796FEFE3B0E CRC64;
     MKGGKSKAKS DNKLAVKKQA ADTKKTKKAV KDPNKPKRPP SAFFVFMEDF RKTYKEKHPN
     NKSVAVVGKA GGDKWKQLTA AEKAPFISKA EKRKQEYEKN LQAYNKKQAA GAAEEEESDK
     SRSEVNDDDE DQDGSGEDDS EDDD