HUNB_MUSDO
ID HUNB_MUSDO Reviewed; 817 AA.
AC Q01778;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Protein hunchback;
GN Name=hb;
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Cooper;
RA Bonneton F., Shaw P.J., Fazakerley C., Shi M., Dover G.A.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 328-396.
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; Y13050; CAA73487.1; -; Genomic_DNA.
DR EMBL; L01601; AAA29296.1; -; Genomic_DNA.
DR AlphaFoldDB; Q01778; -.
DR STRING; 7370.XP_005188978.1; -.
DR PRIDE; Q01778; -.
DR VEuPathDB; VectorBase:MDOA009167; -.
DR eggNOG; KOG1721; Eukaryota.
DR Proteomes; UP000095301; Whole Genome Shotgun Assembly.
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; 2.
PE 3: Inferred from homology;
KW Developmental protein; DNA-binding; Gap protein; Metal-binding; Nucleus;
KW Repeat; Zinc; Zinc-finger.
FT CHAIN 1..817
FT /note="Protein hunchback"
FT /id="PRO_0000046977"
FT ZN_FING 287..309
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 316..338
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 344..366
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 372..396
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 764..786
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 792..816
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 51..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..598
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 817 AA; 90530 MW; F070AE2CEC63C027 CRC64;
MQNWDTATNN NSNNNKSPAL TMQQTAANSN NFLEHNTWYN QMFAANIKQE PGTINPHHQH
PQQHSSMMAS QPQHSPLTHS ANHLENYLKQ HAHNGGGAHH LQFSDNSGAM TPSPNTNVGG
QDFGFESNTS SALNPSLQQH QLYQQHFQQA QQAAAQNQVS SHLPLGFNPL TPPGLPNAVL
PAMNHYYSQQ QQQQQQRQLQ QTPSPSACLS DAHEKSSALT PRHTPPMDIT PPKSPKTTVQ
AMDHQQHPED QDLISNSSED LKYIAESEDD ESIRMPIYNS HGKMKNHKCK SCGMVAITKM
AFWEHARTHM KPEKILQCPK CPFVTELKHH LEYHIRKHKN LKPFQCDKCS YSCVNKSMLN
SHRKSHSSVY QYRCADCDYA TKYCHSFKLH LRKYEHKPGM VLDEEGIPNP SVVIDVYGTR
RGPKNKSAAN AALKKACSDL KIPPTSQLSA ALQGFPLQQQ QQPQQPASPA KSSSSVASEL
PALTLNMSLQ QNLAQQQQQQ QQSPGAQSHS SQQQINNLLP PLASLLQQNR NMAFFPYWNL
NLQMLAAQQQ AAVLAQLSPR MREQLQQQQQ NKQANENGEE DEEDNDEVDE DEEEFDGKSV
DSAMDLSQGT PTKEEQQTPE LAMNLKLSEE HGETPLFSSS AAARRKGRVL KLDQEKTAGH
LQIASAPTSP QHHLHHNNEM PPTTSSPIHP SQVNGVAAGA ADHSSADESM ETGHHHHHHN
PTTANTSASS TASSSGNSSN SSSTSTSSNS NSSSAGNSPN TTMYECKYCD IFFKDAVLYT
IHMGYHSCDD VFKCNMCGEK CDGPVGLFVH MARNAHS
