HUNB_DROVI
ID HUNB_DROVI Reviewed; 816 AA.
AC P13361; B4LZN5;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein hunchback {ECO:0000250|UniProtKB:P05084};
GN Name=hb {ECO:0000250|UniProtKB:P05084};
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2504581; DOI=10.1002/j.1460-2075.1989.tb03536.x;
RA Treier M., Pfeifle C., Tautz D.;
RT "Comparison of the gap segmentation gene hunchback between Drosophila
RT melanogaster and Drosophila virilis reveals novel modes of evolutionary
RT change.";
RL EMBO J. 8:1517-1525(1989).
RN [2]
RP HOMOLOGY.
RX PubMed=12572604; DOI=10.1093/oxfordjournals.molbev.a025868;
RA Tautz D., Nigro L.;
RT "Microevolutionary divergence pattern of the segmentation gene hunchback in
RT Drosophila.";
RL Mol. Biol. Evol. 15:1403-1411(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Gap class segmentation protein that controls development of
CC head structures. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the hunchback C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X15359; CAA33419.1; -; Genomic_DNA.
DR EMBL; CH940650; EDW68204.1; -; Genomic_DNA.
DR PIR; S05548; S05548.
DR RefSeq; XP_002054684.1; XM_002054648.2.
DR AlphaFoldDB; P13361; -.
DR STRING; 7244.FBpp0239005; -.
DR EnsemblMetazoa; FBtr0240513; FBpp0239005; FBgn0013116.
DR GeneID; 6629267; -.
DR KEGG; dvi:6629267; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_021336_0_0_1; -.
DR OMA; QNSLQHF; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000008792; Unassembled WGS sequence.
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 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 Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..816
FT /note="Protein hunchback"
FT /id="PRO_0000046965"
FT ZN_FING 261..283
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 290..312
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 318..340
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 346..364
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 763..785
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 791..815
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 33..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05084"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05084"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05084"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05084"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05084"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05084"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05084"
FT CONFLICT 533
FT /note="R -> A (in Ref. 1; CAA33419)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 816 AA; 89159 MW; C3D69BD21A0C11BA CRC64;
MPNWETSTAA PSYEQHNAWY SSMFAANIKQ EPLSHHHHHH GQQHHDNHSN SNSGASSPRQ
SPLPSPIPPS TQLEQYLKQQ QQQQQQQQQP MDTLCAAAMT PSPSNNDQNS LQHFDATLQQ
QLLQQQQYQQ HFQAAQHQQQ QHHHLALGGF NPLTPPGLPN PMQHYYGGNM RPSPQPTPTA
APTAVAAAIQ TGDKLQALTP PMDVTPPKSP AKSQQSSAEP EKEHDLMSNS SEDMKYMAES
EDDDSNIRMP IYNSHGKMKN YKCKTCGVVA ITKVDFWAHT RTHMKPDKIL QCAKCPFVTE
FKHHLEYHIR KHKNQKPFQC DKCSYTCVNK SMLNSHRKSH SSVYQYRCAD CDYATKYCHS
FKLHLRKYGH KPGMVLDEDG TPNPSLVIDV YGTRRGPKSK SFSGSGSSCS STSKRSNASA
AAAQQQQQPV ATSQLSAALQ GFPMPAAAAG TAAGAAGTAA PAAVAPVSPP SPAKSVASVE
QAPSLPSALL PPLASLLQQN RNMAFFPYWN LNLQVLAAQQ QAAVLAQLSP RMRDQLQQQQ
QQQHQQQQQQ QQQQQQQQQQ LPAHSENEED EEEEEHEDDF ERKSVDSAMD LSQGTPVKEE
PQQQQQQQQL PHSNHMAINL KLKDEDTPLI SSSSASRRKG RVLKLDTLLQ LKSAAMSSPE
QQLKLPASVL PTASSPIAGS SANKQLADDP CSGASSADES METGRVPQVN ISASSTASSS
GNSSNASSST SNPTAAATVA TSGTVSSSSS SSTTTSSSAP AIYECKYCDI YFKDAVLYTI
HMGYHSCDDV FKCNMCGEKC DGPVGLFVHM ARNAHS
