SUHW_DROVI
ID SUHW_DROVI Reviewed; 899 AA.
AC Q08876;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein suppressor of hairy wing;
GN Name=su(Hw);
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 [MRNA].
RX PubMed=7916729; DOI=10.1101/gad.7.10.1966;
RA Harrison D.A., Gdula D.A., Coyne R.S., Corces V.G.;
RT "A leucine zipper domain of the suppressor of Hairy-wing protein mediates
RT its repressive effect on enhancer function.";
RL Genes Dev. 7:1966-1978(1993).
CC -!- FUNCTION: Su(Hw) controls the phenotypic effect of the gypsy
CC transposable element. Binds specifically to a region of the gipsy
CC element located 3' of the 5'LTR. It is probably a transcription factor.
CC Could play a role in the establishment of chromatin domains.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; Z25520; CAA80976.1; -; mRNA.
DR PIR; B48586; B48586.
DR AlphaFoldDB; Q08876; -.
DR SMR; Q08876; -.
DR STRING; 7244.FBpp0228730; -.
DR PRIDE; Q08876; -.
DR eggNOG; KOG1721; Eukaryota.
DR ChiTaRS; su(Hw); fly.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblMetazoa.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005700; C:polytene chromosome; IEA:EnsemblMetazoa.
DR GO; GO:0043035; F:chromatin insulator sequence binding; IEA:EnsemblMetazoa.
DR GO; GO:1990188; F:euchromatin binding; IEA:EnsemblMetazoa.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:EnsemblMetazoa.
DR GO; GO:0033696; P:heterochromatin boundary formation; IEA:EnsemblMetazoa.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:EnsemblMetazoa.
DR GO; GO:1905632; P:protein localization to euchromatin; IEA:EnsemblMetazoa.
DR GO; GO:0035075; P:response to ecdysone; IEA:EnsemblMetazoa.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..899
FT /note="Protein suppressor of hairy wing"
FT /id="PRO_0000047054"
FT ZN_FING 218..240
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 288..311
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 318..340
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 347..365
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 379..401
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..434
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 440..462
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 468..490
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 496..518
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 522..544
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 552..576
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 594..617
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..197
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 100592 MW; 7CCD1AC6C9928546 CRC64;
MSAQEDALPA TPPASSSIKI SDGDKPKEKR TGTRMKLLND VAAKAAVASK GASVSPRLKP
EKRTSIKILN NNNNDEAQTS TKGGDSVPRP KPPAPASRYR TRSSAPASSA VETAKIKTSP
SKKKKMDHYV LQAIKSENNK AENTTSVVVV EDEDTIDFIL ADDEVELGAG AKENGEEFVV
SGVDEDDDDD DDDEDEGVVE GGAKRRSGNN ELKEMVEHVC GKCYKTFRRV KSLKKHLEFC
RYDSGYHLRK ADMLKNLEKI EKDAVVMEKK DISFCCSESY DTFHLGHINC PDCPKSFKTQ
TSYERHIFIT HSWSCNDYPC SICNAKLRSG ALLKLHEQQH QLRGKPFACK ICGKDFMCSY
HLKCHQKYSS CSANENDTMS CKVCDRVFYR LDNLCAHLKQ HLGTQVVKKP EYMCHVCKNC
FYSLSTLNIH IRTHTGEKPF DCDLCDKKFS ALVALKKHRR YHTGEKPYTC TVCSQSFAVK
EVLNRHMKRH TGERPHKCNE CGKSFIQATQ LRTHSKTHLR PYACSLCIQK FKTEKQLERH
VKDHTRQKRA SFACTECTRS FRTSALLKEH LDAGDHSPVK STRAKRSAKM IERTDCAICD
KNFDTTETLR NHIRSVHECD PDDIFGTEPP AKRKAKKTVV AAVAEEQKEQ EDDVPARNTS
AGSLISSKTD GNGVVVREFL VDEGDGNAQT IDLRKRGLHH LPLEGDKATE STAETDIKAE
SSKEKPSVSP VVKKEQRKSL AASLAAAIAD NLEEPSSDDE FSGEVLTEED LKLKENIAKL
IDMLVDPQTL KKYGWPNSSE ESVLCKVIEN CGHDLAKGSE AYAELDYGSR MPILQLLFTV
VIHNDSIKAL LNNFPIDDVI EYVLGDEDQD QDQETDKGKD READNTDTDT REDAVESEA
