HANG_DROME
ID HANG_DROME Reviewed; 1959 AA.
AC Q9VXG1; Q9VXG2;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 4.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Zinc finger protein hangover;
GN Name=hang; ORFNames=CG32575;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Berkeley {ECO:0000269|PubMed:16094367};
RX PubMed=16094367; DOI=10.1038/nature03864;
RA Scholz H., Franz M., Heberlein U.;
RT "The hangover gene defines a stress pathway required for ethanol tolerance
RT development.";
RL Nature 436:845-847(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000305}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228; THR-246; SER-680;
RP SER-832; SER-894; SER-895; SER-898 AND SER-899, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Required for normal development of ethanol tolerance. Relies
CC on two distinct molecular pathways: a cellular stress pathway defined
CC by hang, and a parallel pathway requiring octopamine.
CC {ECO:0000269|PubMed:16094367}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16094367}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=D {ECO:0000312|FlyBase:FBgn0026575};
CC IsoId=Q9VXG1-1; Sequence=Displayed;
CC Name=A {ECO:0000312|FlyBase:FBgn0026575};
CC IsoId=Q9VXG1-3; Sequence=VSP_058187, VSP_058188;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in the nervous system, in
CC neurons not glia. {ECO:0000269|PubMed:16094367}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit defective responses to
CC environmental stressors, such as heat and the free-radical-generating
CC agent paraquat. {ECO:0000269|PubMed:16094367}.
CC -!- MISCELLANEOUS: Stress, at both the cellular and systemic levels,
CC contributes to drug- and addiction-related behaviors in mammals.
CC Function of hang suggests that this role may be conserved across
CC evolution. {ECO:0000303|PubMed:16094367}.
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DR EMBL; AE014298; AAF48611.3; -; Genomic_DNA.
DR EMBL; AE014298; AAF48612.4; -; Genomic_DNA.
DR RefSeq; NP_727979.3; NM_167520.3. [Q9VXG1-1]
DR RefSeq; NP_727980.2; NM_167521.3. [Q9VXG1-3]
DR AlphaFoldDB; Q9VXG1; -.
DR BioGRID; 58953; 8.
DR IntAct; Q9VXG1; 2.
DR iPTMnet; Q9VXG1; -.
DR PaxDb; Q9VXG1; -.
DR PRIDE; Q9VXG1; -.
DR EnsemblMetazoa; FBtr0074276; FBpp0074052; FBgn0026575. [Q9VXG1-3]
DR EnsemblMetazoa; FBtr0343571; FBpp0310171; FBgn0026575. [Q9VXG1-1]
DR GeneID; 32613; -.
DR KEGG; dme:Dmel_CG32575; -.
DR UCSC; CG32575-RA; d. melanogaster. [Q9VXG1-1]
DR CTD; 32613; -.
DR FlyBase; FBgn0026575; hang.
DR VEuPathDB; VectorBase:FBgn0026575; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164700; -.
DR InParanoid; Q9VXG1; -.
DR OMA; ECEVCSI; -.
DR SignaLink; Q9VXG1; -.
DR BioGRID-ORCS; 32613; 1 hit in 1 CRISPR screen.
DR ChiTaRS; hang; fly.
DR GenomeRNAi; 32613; -.
DR PRO; PR:Q9VXG1; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0026575; Expressed in cleaving embryo and 43 other tissues.
DR ExpressionAtlas; Q9VXG1; baseline and differential.
DR Genevisible; Q9VXG1; DM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:FlyBase.
DR GO; GO:0003676; F:nucleic acid binding; NAS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045471; P:response to ethanol; IMP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IMP:FlyBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR012934; Znf_AD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF07776; zf-AD; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00868; zf-AD; 1.
DR SMART; SM00355; ZnF_C2H2; 19.
DR SMART; SM00451; ZnF_U1; 3.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS51915; ZAD; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1959
FT /note="Zinc finger protein hangover"
FT /id="PRO_0000046924"
FT DOMAIN 79..155
FT /note="ZAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT ZN_FING 318..341
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 447..469
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 581..604
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 770..793
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 801..824
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 908..930
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1011..1034
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1042..1065
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1078..1101
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1154..1176
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1184..1207
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1318..1340
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1375..1397
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1476..1499
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1552..1574
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1873..1895
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 178..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1627..1865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1933..1959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1639..1693
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1717..1757
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1786..1828
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1831..1853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1937..1959
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 246
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 872..875
FT /note="Missing (in isoform A)"
FT /id="VSP_058187"
FT VAR_SEQ 1859..1959
FT /note="ERRKKAVDQLNDPGFTCDLCQLCFDSQELLQSHIKSHILNGPKLSTVSAAAA
FT AAAAAATASSKATALLTAAKAKPDSKSAVLANNNNSKTSSKTVAAGATN -> ASPEPH
FT QKPYPQWAKALDSVSSSSSSSSRRHSKQQGNSITNGSKGEA (in isoform A)"
FT /id="VSP_058188"
SQ SEQUENCE 1959 AA; 213792 MW; 238AB9C6E62763EC CRC64;
MCDAAAATAT TTTTAAVAAA VATTTASVAL EATATQPGTT TTTVATASAG TTSPEAAIPT
AATATSARNS NSERSARQNC CRLCIAPQTE CISIINSYAA DKEPLSTKIH NCVGIKVTPQ
DRLSQQICHA CISYLNSWQS FKNRCFSSQA KQRQWLDTNK SKLLNYLDLN SAENGGGGFF
DQHLHQQQQH HQHLENELEA EKEKATPTAA STAANILDGI HSLKKRKSLT VYPLPAMPIK
DEPIDTDDDY QMKSIDESDD MVDPTMFLER SEHEGDVPLT ASDYDYTAQH GVNASSVAAS
LPPNAVANVA AAGDSKVASC RACSLQFSTR ANARRHERNL HPNLFQLSTD SPHNTPITKP
TPALAAALEM QRAAAAAATA EANRAAGAAG GNISTQKYRQ VVMNAFIKCE GGGYDYDNPE
QYRPLLTRDK VEFIEQNDEF LEQYQTMTCR CCNKYFSTYK NFMAHVRKKY PQLPRNLCFN
CLKMNDSKAL FISHLKKRNC INLFRVLNAL RGKTTTVVVP IADDVADDGA TGSIPVADAG
AGVVAMNSPT VTASGEVVTP GGGSERPEKL RAKELLVNKL YECKLCPKGF RTKHEFRTHV
YDKHADVQRK DNNSIQCSFC GLDFADPVDR RRHYNNMDCI VRLRCMTCDA KLETHQRFLD
HVYQDHLGGV GGGAVSDNAS TTGSGMARSN SMEHSPGKRS LLGALGVGSS AEESRSSSAA
PPLTSTPKLA GGNQVGGGGS TSASAAAAAQ SSANRDASAP KSQYFSRMPQ VCPICGQQYN
NYNNVLRHME SKHPNKLPET YKCVRCGLGY PRISYLREHM INVHGVDKNR HSGGFEYIVN
ADAVKLADGS TPNVYTGRYD YVMKDLMSIT NGGTLDDEEE EPGSVAKKMR LDDSSNNSSL
VGVASQQKEC PICNAVFSNN IGLSNHMRSH YTASNAVNAA LAAANRMTPK SLTITATPAT
DSELGVGGTM SESAPATPAN VPPAMANQTP QEQAVFRRSL DQAADRRFRR MRCRICQRRF
SSKKSYRYHM LTDHQVQNVQ FIKCKLCNAE FAYEKGLKVH LFKVHGKAIK DEMIIKQFEC
DVCSIVYSSE SELQQHKRSV HKLTSASAST SASTSSKIDD DSLMDDGKPT SSDLADLSTL
AAGGSTASAP LYWYQCKYCP SNFNTNKKLA IHINSHDEFD SNDYSCKDCG NVYSGRKSLW
VHRYKKHPQV PNPAECSLCR KVFFDRQMHD NHTPTCNRKP ITSTGAHQQQ DGQLHSHHTA
KRTIFRHKTG DDDDEEDDDE QQQLEERANS DGNGTTVGVA SGSTAAAGTS LKIRIPEVAC
TICGARFTDQ EHFSKHIQKH EQELYVDNPL AAMFDDGPAD AGQFQVERQN ENGEYACDLC
AKTFPQVIAL KVHRKWHFRG DSKQNPIDGE ATQLTNNNHT TNNNNNNSMH LRELHAVGLM
PNQQQQSLNN SCNSSMNHNN NSSSNRSKSM KRKRELKCEY CASTFISNNN LRRHMYELHK
HEVSNLPEPP VIVVDDHLTC RRCQLKFDTK ELWIEHKLAD AKVVRPFCPF QWGCDLCGEY
LSRKEKLMNH INNHLKEEVI VPVATKAAIE RTAAMESAAA DANAAATLSA LGEGAETEDQ
FAEKVEAAGA TTTDKLTNPD EEDSDDLDED SSGDDDDSSG TGDDDDDDDS DDDEDGEGED
EDEEGDGGEG EDEEGVQPPA QLLPQQQHKT DLNLNQDDDD LVEEVISSDD DEDDDGEVES
DDDDEDDDDE EDDVEEPEPV GLTVRPLMNG KSKMPPLIVA SSDDEDDGVM PIEDIIEEEF
DEDADPDPED AIEEVDEDDL DEGEVEDEPN VVSTASFSES ESSTTTTSNS HSHSHSTGER
RKKAVDQLND PGFTCDLCQL CFDSQELLQS HIKSHILNGP KLSTVSAAAA AAAAAATASS
KATALLTAAK AKPDSKSAVL ANNNNSKTSS KTVAAGATN
