HUNB_CLOAL
ID HUNB_CLOAL Reviewed; 485 AA.
AC O96785;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Protein hunchback;
DE Flags: Fragment;
GN Name=hb;
OS Clogmia albipunctata (Mothmidge).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Psychodoidea; Psychodidae;
OC Clogmia.
OX NCBI_TaxID=85120;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10079357; DOI=10.1007/s004270050238;
RA Rohr K.B., Tautz D., Sander K.;
RT "Segmentation gene expression in the mothmidge Clogmia albipunctata
RT (Diptera, psychodidae) and other primitive dipterans.";
RL Dev. Genes Evol. 209:145-154(1999).
CC -!- FUNCTION: Gap class segmentation protein that controls development of
CC head structures. {ECO:0000250}.
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; AJ131041; CAA10281.1; -; mRNA.
DR AlphaFoldDB; O96785; -.
DR SMR; O96785; -.
DR PRIDE; O96785; -.
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; 1.
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; 3.
PE 2: Evidence at transcript level;
KW Developmental protein; DNA-binding; Gap protein; Metal-binding; Nucleus;
KW Repeat; Zinc; Zinc-finger.
FT CHAIN <1..485
FT /note="Protein hunchback"
FT /id="PRO_0000046972"
FT ZN_FING 87..109
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 116..138
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 144..166
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 172..196
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 432..454
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 460..484
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
SQ SEQUENCE 485 AA; 55367 MW; 8BEAC3B3C3B0C37C CRC64;
TSSTARKTPE KDSLKQDQNQ LLKTPIQTNG NQQSTFDSGE DSHSMPDSDL LEPVITDGAD
VDDENDAEED DDIRTPKINS HGKMKTYKCK QCDFIAVTKL SFWEHNRIHI KPEKMLKCQK
CPFITEYKHH LEYHLRNHNG SKPFQCKQCN YSCVNKSMLN SHMKSHSNIY QYRCKDCNYA
TKYCHSLKLH LRKYSHNPPM VLNYDGTPNP LRIIDVYGTR RGPKVKFHKD EGGHNLLNSN
INTSRRSKSG KRDSFPNFEQ SQHVPTPPSS QALAMLPNLA NIFQQSPSMP LFPYLNLNFH
HILAQQKAAL SQISPSINGW QNEENCNEEE TPEKEEDPKR MSALDLSSNP STPSTVSQVK
HKRKGRAFKL ELMKESSDDD EGQTIRTLGE IRSELETPKP VQLQLPTSST TTPLKTTSED
DSTSVEPLQN LYECKFCDIS FKHAVLYTIH MGYHGYNDVF KCNACGKKCE DRVAFFLHIA
RDAHA