ID   HUNB_TRICA              Reviewed;         524 AA.
AC   Q01791;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Protein hunchback;
GN   Name=hb;
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8575322; DOI=10.1242/dev.121.12.4227;
RA   Wolff C., Sommer R., Schroeder R., Glaser G., Tautz D.;
RT   "Conserved and divergent expression aspects of the Drosophila segmentation
RT   gene hunchback in the short germ band embryo of the flour beetle
RT   Tribolium.";
RL   Development 121:4227-4236(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 243-311.
RX   PubMed=1438276; DOI=10.1073/pnas.89.22.10782;
RA   Sommer R.J., Retzlaff M., Goerlich K., Sander K., Tautz D.;
RT   "Evolutionary conservation pattern of zinc-finger domains of Drosophila
RT   segmentation genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:10782-10786(1992).
CC   -!- FUNCTION: Gap class segmentation protein that controls development of
CC       head structures.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the hunchback C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; X91618; CAA62821.1; -; Genomic_DNA.
DR   EMBL; L01615; AAA30095.1; -; Genomic_DNA.
DR   RefSeq; NP_001038093.1; NM_001044628.1.
DR   AlphaFoldDB; Q01791; -.
DR   STRING; 7070.TC013553-PA; -.
DR   GeneID; 656763; -.
DR   KEGG; tca:656763; -.
DR   CTD; 15120; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_021336_0_0_1; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0040034; P:regulation of development, heterochronic; IEA:InterPro.
DR   GO; GO:0035282; P:segmentation; IEA:UniProtKB-KW.
DR   InterPro; IPR027742; Hunchback.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24392:SF33; PTHR24392:SF33; 2.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   3: Inferred from homology;
KW   Developmental protein; DNA-binding; Gap protein; Metal-binding; Nucleus;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..524
FT                   /note="Protein hunchback"
FT                   /id="PRO_0000046983"
FT   ZN_FING         202..224
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         231..253
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         259..281
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         298..311
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         471..493
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         499..523
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          42..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  59514 MW;  022EE44111BE4B9F CRC64;
     MIDKDMNSAC MRGGSVRTLN NYQQVMEPRS PHTAWQFGVS QIVKREPMDE DKNDSGVTSG
     SDFHSSSPSS DTSQDLQHSY QSPQTQPARF YSTPIVPHFA YNHNPLTPPN SEPLVSPKSE
     KEEKDMETTL TPCASPNRKP DDNQDHLRRL EMSLEKSGLF SSKTSEHSVD ELSGKSDNDA
     EEYDEQSLRV PKVNSHGKIK TFKCKQCDFV AITKLEQWNH SKVHIREDKR LTCPKCPFIT
     EYKHHLEYHL RNHAGSKPFQ CNKCDYTCVN KSMLNSHMKS HSNVYRYSCR DCSYATKYCH
     SLKIHLRRYG HTPNVVLDEE GNPCPDIIID VHGTRRGPKI KTQPKAEEAK PETLPFLNLQ
     QQLPFPGYPF FGGFPNAQLL QQLIRERQLA VGGSQEESRV LDLSKPGCSY TGEQKSRRKG
     PAFKVDPTQV ESEEEDEETS TTVFSNVEVV QEEAKKEESD SNNNNNKEEG NSCQYCNIAF
     GDAVLYTIHM GYHGFHNPFT CNMCGVECSD KVSFFLHIAR VSHS