HUNB_MANSE
ID HUNB_MANSE Reviewed; 327 AA.
AC Q25514;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Protein hunchback;
DE Flags: Fragment;
GN Name=hb;
OS Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Sphinginae; Sphingini; Manduca.
OX NCBI_TaxID=7130;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Embryo;
RX PubMed=8022829; DOI=10.1073/pnas.91.14.6634;
RA Kraft R., Jaeckle H.;
RT "Drosophila mode of metamerization in the embryogenesis of the lepidopteran
RT insect Manduca sexta.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6634-6638(1994).
CC -!- FUNCTION: Gap class segmentation protein that controls development of
CC head structures.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the anterior region of the blastoderm
CC embryo.
CC -!- SIMILARITY: Belongs to the hunchback C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; Z30281; CAA82955.1; -; Genomic_DNA.
DR AlphaFoldDB; Q25514; -.
DR PRIDE; Q25514; -.
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; 3.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; DNA-binding; Gap protein; Metal-binding; Nucleus;
KW Repeat; Zinc; Zinc-finger.
FT CHAIN <1..>327
FT /note="Protein hunchback"
FT /id="PRO_0000046976"
FT ZN_FING <1..5
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 11..33
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 39..63
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 297..319
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 325..>327
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 91..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT NON_TER 327
SQ SEQUENCE 327 AA; 36523 MW; 64871E4CB0F7C058 CRC64;
HMRNHLGSKP FQCSQCSYSC VNKSMLNSHL KSHSNVYQYR CADCNYATKY CHSLKLHLRK
YQHNPAMVLN LDGTPNPLPI IDVYGTRRGP KQKPFSKMFE PQGPVSNNNQ PQPPAPTHPI
FGNHFPVNLP YLPPLLPHSF LFPPNNNYEQ RTSPKNHEIQ TEKPQQMSPP ASILHQRLSY
TERPLESGST SPPPKSPPSI TQTPTHREMP TEHGDDALDL TNAKTSEAGT PPPPTERATP
VTPTTALKNR RKGRAFKLQP AALRLQHEDE KMRDADGSDS ESDASAEVAS SSAASSYTCQ
FCDITFGDLT MHTIHMGFHG YNDPFMC
