HID_DROME
ID HID_DROME Reviewed; 410 AA.
AC Q24106; Q9VVP1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Cell death protein hid;
DE AltName: Full=Protein head involution defective;
DE AltName: Full=Protein wrinkled;
GN Name=hid; Synonyms=W; ORFNames=CG5123;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Canton-S; TISSUE=Eye imaginal disk;
RX PubMed=7622034; DOI=10.1101/gad.9.14.1694;
RA Grether M.E., Abrams J.M., Agapite J., White K., Steller H.;
RT "The head involution defective gene of Drosophila melanogaster functions in
RT programmed cell death.";
RL Genes Dev. 9:1694-1708(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
RP GENOME REANNOTATION.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION.
RC TISSUE=Embryo;
RX PubMed=9740659; DOI=10.1006/dbio.1998.9000;
RA Chen P., Rodriguez A., Erskine R., Thach T., Abrams J.M.;
RT "Dredd, a novel effector of the apoptosis activators reaper, grim, and hid
RT in Drosophila.";
RL Dev. Biol. 201:202-216(1998).
RN [6]
RP FUNCTION, AND INTERACTION WITH DIAP2.
RX PubMed=18166655; DOI=10.1083/jcb.200706027;
RA Ribeiro P.S., Kuranaga E., Tenev T., Leulier F., Miura M., Meier P.;
RT "DIAP2 functions as a mechanism-based regulator of drICE that contributes
RT to the caspase activity threshold in living cells.";
RL J. Cell Biol. 179:1467-1480(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP MASS 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).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF SER-121; THR-148; THR-180; THR-228 AND
RP SER-251.
RX PubMed=22615583; DOI=10.1371/journal.pgen.1002725;
RA Schoenherr J.A., Drennan J.M., Martinez J.S., Chikka M.R., Hall M.C.,
RA Chang H.C., Clemens J.C.;
RT "Drosophila activated Cdc42 kinase has an anti-apoptotic function.";
RL PLoS Genet. 8:E1002725-E1002725(2012).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22964637; DOI=10.1038/onc.2012.395;
RA Wang Y., Wang Z., Joshi B.H., Puri R.K., Stultz B., Yuan Q., Bai Y.,
RA Zhou P., Yuan Z., Hursh D.A., Bi X.;
RT "The tumor suppressor Caliban regulates DNA damage-induced apoptosis
RT through p53-dependent and -independent activity.";
RL Oncogene 32:3857-3866(2013).
RN [10] {ECO:0007744|PDB:1JD6}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 2-11.
RX PubMed=11511363; DOI=10.1016/s1097-2765(01)00282-9;
RA Wu J.W., Cocina A.E., Chai J., Hay B.A., Shi Y.;
RT "Structural analysis of a functional DIAP1 fragment bound to grim and hid
RT peptides.";
RL Mol. Cell 8:95-104(2001).
CC -!- FUNCTION: Activator of apoptosis, with grim and rpr, that acts on the
CC effector Dredd (PubMed:9740659, PubMed:22615583). Seems to act
CC genetically upstream of baculoviral anti-apoptotic p35
CC (PubMed:7622034). Blocks Diap2 from binding and inactivating the
CC effector caspase Drice (PubMed:18166655). Might regulate apoptosis
CC downstream of Clbn/NEMF (PubMed:22964637).
CC {ECO:0000269|PubMed:18166655, ECO:0000269|PubMed:22615583,
CC ECO:0000269|PubMed:22964637, ECO:0000269|PubMed:7622034,
CC ECO:0000269|PubMed:9740659}.
CC -!- SUBUNIT: Interacts with Diap2 (via BIR2 and BIR3 domains).
CC {ECO:0000269|PubMed:18166655}.
CC -!- INTERACTION:
CC Q24106; Q24306: Diap1; NbExp=8; IntAct=EBI-135509, EBI-456419;
CC -!- DEVELOPMENTAL STAGE: Expression coincides with the onset of programmed
CC cell death (PCD) at all stages of embryonic development, particularly
CC in the head. {ECO:0000269|PubMed:7622034}.
CC -!- DISRUPTION PHENOTYPE: Mutants contain extra cells in the head owing to
CC decreased levels of cell death and show a pronounced defect in the
CC morphogenetic movements of head involution (PubMed:7622034). Ectopic
CC expression in the retina results in complete eye ablation
CC (PubMed:7622034). Reduces levels of caspace-3 after exposure to
CC ionizing radiation (PubMed:22964637). Simultaneous knockout of hid and
CC Clbn/NEMF has a similar response to single mutants after exposure to
CC ionizing radiation (PubMed:22964637). {ECO:0000269|PubMed:22964637,
CC ECO:0000269|PubMed:7622034}.
CC -!- SIMILARITY: To D.melanogaster grim and rpr. {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; U31226; AAA79985.1; -; mRNA.
DR EMBL; AE014296; AAF49270.1; -; Genomic_DNA.
DR EMBL; AY075188; AAL68057.1; -; mRNA.
DR RefSeq; NP_001262010.1; NM_001275081.1.
DR RefSeq; NP_524136.2; NM_079412.4.
DR PDB; 1JD6; X-ray; 2.70 A; B=2-11.
DR PDBsum; 1JD6; -.
DR AlphaFoldDB; Q24106; -.
DR SMR; Q24106; -.
DR BioGRID; 65293; 109.
DR DIP; DIP-20052N; -.
DR ELM; Q24106; -.
DR IntAct; Q24106; 8.
DR STRING; 7227.FBpp0074899; -.
DR iPTMnet; Q24106; -.
DR PaxDb; Q24106; -.
DR DNASU; 40009; -.
DR EnsemblMetazoa; FBtr0075133; FBpp0074899; FBgn0003997.
DR EnsemblMetazoa; FBtr0332862; FBpp0305084; FBgn0003997.
DR GeneID; 40009; -.
DR KEGG; dme:Dmel_CG5123; -.
DR CTD; 40009; -.
DR FlyBase; FBgn0003997; hid.
DR VEuPathDB; VectorBase:FBgn0003997; -.
DR eggNOG; ENOG502TBS2; Eukaryota.
DR HOGENOM; CLU_671335_0_0_1; -.
DR InParanoid; Q24106; -.
DR OMA; QSFTWPT; -.
DR OrthoDB; 1273025at2759; -.
DR PhylomeDB; Q24106; -.
DR SignaLink; Q24106; -.
DR BioGRID-ORCS; 40009; 0 hits in 1 CRISPR screen.
DR ChiTaRS; w; fly.
DR GenomeRNAi; 40009; -.
DR PRO; PR:Q24106; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0003997; Expressed in head epidermis primordium (Drosophila) and 57 other tissues.
DR ExpressionAtlas; Q24106; baseline and differential.
DR Genevisible; Q24106; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:1990525; F:BIR domain binding; IPI:FlyBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:FlyBase.
DR GO; GO:0048800; P:antennal morphogenesis; IMP:FlyBase.
DR GO; GO:0006915; P:apoptotic process; IMP:FlyBase.
DR GO; GO:0097190; P:apoptotic signaling pathway; IDA:FlyBase.
DR GO; GO:0008219; P:cell death; IMP:FlyBase.
DR GO; GO:0071480; P:cellular response to gamma radiation; IMP:FlyBase.
DR GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0035072; P:ecdysone-mediated induction of salivary gland cell autophagic cell death; IEP:FlyBase.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IMP:FlyBase.
DR GO; GO:0008258; P:head involution; IMP:FlyBase.
DR GO; GO:0002165; P:instar larval or pupal development; IMP:FlyBase.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:FlyBase.
DR GO; GO:0035096; P:larval midgut cell programmed cell death; IGI:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:FlyBase.
DR GO; GO:1904747; P:positive regulation of apoptotic process involved in development; IMP:UniProtKB.
DR GO; GO:2000685; P:positive regulation of cellular response to X-ray; IMP:FlyBase.
DR GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; IDA:FlyBase.
DR GO; GO:2001272; P:positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; IDA:FlyBase.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:FlyBase.
DR GO; GO:0012501; P:programmed cell death; IMP:FlyBase.
DR GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IGI:FlyBase.
DR GO; GO:0046620; P:regulation of organ growth; IMP:FlyBase.
DR GO; GO:0010114; P:response to red light; IMP:FlyBase.
DR GO; GO:0035071; P:salivary gland cell autophagic cell death; IMP:FlyBase.
DR GO; GO:0007548; P:sex differentiation; IMP:FlyBase.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Developmental protein; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..410
FT /note="Cell death protein hid"
FT /id="PRO_0000083972"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..192
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VARIANT 171
FT /note="P -> S (in allele A22)"
FT VARIANT 261
FT /note="S -> L (in allele A206)"
FT MUTAGEN 121
FT /note="S->A: In Ala5: Induces apoptosis; when associated
FT with A-148, A-180, A-228 and A-251."
FT /evidence="ECO:0000269|PubMed:22615583"
FT MUTAGEN 148
FT /note="T->A: In Ala5: Induces apoptosis; when associated
FT with A-121, A-180, A-228 and A-251."
FT /evidence="ECO:0000269|PubMed:22615583"
FT MUTAGEN 180
FT /note="T->A: In Ala5: Induces apoptosis; when associated
FT with A-121, A-148, A-228 and A-251."
FT /evidence="ECO:0000269|PubMed:22615583"
FT MUTAGEN 228
FT /note="T->A: In Ala5: Induces apoptosis; when associated
FT with A-121, A-148, A-180 and A-251."
FT /evidence="ECO:0000269|PubMed:22615583"
FT MUTAGEN 251
FT /note="S->A: In Ala5: Induces apoptosis; when associated
FT with A-121, A-148, A-180 and A-228."
FT /evidence="ECO:0000269|PubMed:22615583"
FT CONFLICT 351
FT /note="P -> S (in Ref. 1; AAA79985)"
FT /evidence="ECO:0000305"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1JD6"
SQ SEQUENCE 410 AA; 43877 MW; 63EBF913149E27E1 CRC64;
MAVPFYLPEG GADDVASSSS GASGNSSPHN HPLPSSASSS VSSSGVSSAS ASSASSSSSA
SSDGASSAAS QSPNTTTSSA TQTPMQSPLP TDQVLYALYE WVRMYQSQQS APQIFQYPPP
SPSCNFTGGD VFFPHGHPNP NSNPHPRTPR TSVSFSSGEE YNFFRQQQPQ PHPSYPAPST
PQPMPPQSAP PMHCSHSYPQ QSAHMMPHHS APFGMGGTYY AGYTPPPTPN TASAGTSSSS
AAFGWHGHPH SPFTSTSTPL SAPVAPKMRL QRSQSDAARR KRLTSTGEDE REYQSDHEAT
WDEFGDRYDN FTAGRERLQE FNGRIPPRKK KSSNSHSSSS NNPVCHTDSQ PGGTSQAESG
AIHGHISQQR QVERERQKAK AEKKKPQSFT WPTVVTVFVL AMGCGFFAAR
