GCM_DROME
ID GCM_DROME Reviewed; 504 AA.
AC Q27403; A0AVW8; Q9VLA5;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Transcription factor glial cells missing;
DE AltName: Full=Protein glide;
GN Name=gcm; ORFNames=CG12245;
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=7553843; DOI=10.1016/0092-8674(95)90280-5;
RA Jones B.W., Fetter R.D., Tear G., Goodman C.S.;
RT "Glial cells missing: a genetic switch that controls glial versus neuronal
RT fate.";
RL Cell 82:1013-1023(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=7553844; DOI=10.1016/0092-8674(95)90281-3;
RA Hosoya T., Takizawa K., Nitta K., Hotta Y.;
RT "Glial cells missing: a binary switch between neuronal and glial
RT determination in Drosophila.";
RL Cell 82:1025-1036(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=9356176; DOI=10.1006/dbio.1997.8702;
RA Bernardoni R., Vivancos V., Giangrande A.;
RT "Glide/gcm is expressed and required in the scavenger cell lineage.";
RL Dev. Biol. 191:118-130(1997).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor that induces gliogenesis. It determines
CC the choice between glial and neuronal fates. Also has a role in the
CC differentiation of the plasmatocyte/macrophage lineage of hemocytes.
CC {ECO:0000269|PubMed:7553843, ECO:0000269|PubMed:7553844,
CC ECO:0000269|PubMed:9356176}.
CC -!- INTERACTION:
CC Q27403; Q9VN10: hkb; NbExp=2; IntAct=EBI-175874, EBI-171756;
CC Q27403; P68198: Ubi-p63E; NbExp=2; IntAct=EBI-175874, EBI-86340;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00245,
CC ECO:0000269|PubMed:7553844}.
CC -!- TISSUE SPECIFICITY: Expressed transiently in early glial cells.
CC {ECO:0000269|PubMed:7553843, ECO:0000269|PubMed:7553844}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit failure of glia to differentiate in
CC the CNS and in the PNS, glia are transformed into neurons. Ectopic
CC expression causes neurons to transform to glia.
CC {ECO:0000269|PubMed:7553843}.
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DR EMBL; U34039; AAC46912.1; -; Genomic_DNA.
DR EMBL; D64040; BAA10905.1; -; mRNA.
DR EMBL; U81164; AAC47808.1; -; mRNA.
DR EMBL; AE014134; AAF52790.1; -; Genomic_DNA.
DR EMBL; BT029286; ABK30923.1; -; mRNA.
DR PIR; A57215; A57215.
DR RefSeq; NP_001260292.1; NM_001273363.1.
DR RefSeq; NP_477108.1; NM_057760.5.
DR AlphaFoldDB; Q27403; -.
DR BMRB; Q27403; -.
DR SMR; Q27403; -.
DR BioGRID; 60376; 62.
DR DIP; DIP-20508N; -.
DR IntAct; Q27403; 12.
DR MINT; Q27403; -.
DR STRING; 7227.FBpp0079451; -.
DR PaxDb; Q27403; -.
DR DNASU; 34277; -.
DR EnsemblMetazoa; FBtr0079855; FBpp0079451; FBgn0014179.
DR EnsemblMetazoa; FBtr0335492; FBpp0307464; FBgn0014179.
DR GeneID; 34277; -.
DR KEGG; dme:Dmel_CG12245; -.
DR CTD; 34277; -.
DR FlyBase; FBgn0014179; gcm.
DR VEuPathDB; VectorBase:FBgn0014179; -.
DR eggNOG; ENOG502QU2X; Eukaryota.
DR GeneTree; ENSGT00390000006777; -.
DR HOGENOM; CLU_024014_0_0_1; -.
DR InParanoid; Q27403; -.
DR OMA; GHCRLIY; -.
DR OrthoDB; 722438at2759; -.
DR PhylomeDB; Q27403; -.
DR SignaLink; Q27403; -.
DR BioGRID-ORCS; 34277; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34277; -.
DR PRO; PR:Q27403; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0014179; Expressed in head mesoderm (Drosophila) and 53 other tissues.
DR ExpressionAtlas; Q27403; baseline and differential.
DR Genevisible; Q27403; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; TAS:FlyBase.
DR GO; GO:0035165; P:embryonic crystal cell differentiation; IMP:FlyBase.
DR GO; GO:0060857; P:establishment of glial blood-brain barrier; IMP:FlyBase.
DR GO; GO:0021782; P:glial cell development; IMP:FlyBase.
DR GO; GO:0010001; P:glial cell differentiation; IMP:FlyBase.
DR GO; GO:0007403; P:glial cell fate determination; IMP:FlyBase.
DR GO; GO:0042063; P:gliogenesis; IMP:FlyBase.
DR GO; GO:0007516; P:hemocyte development; TAS:FlyBase.
DR GO; GO:0042690; P:negative regulation of crystal cell differentiation; IMP:FlyBase.
DR GO; GO:0030182; P:neuron differentiation; IMP:FlyBase.
DR GO; GO:0042387; P:plasmatocyte differentiation; IMP:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:FlyBase.
DR GO; GO:0045687; P:positive regulation of glial cell differentiation; IMP:FlyBase.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0035289; P:posterior head segmentation; IMP:FlyBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:FlyBase.
DR GO; GO:0045610; P:regulation of hemocyte differentiation; IMP:FlyBase.
DR GO; GO:0050764; P:regulation of phagocytosis; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:FlyBase.
DR Gene3D; 2.20.25.670; -; 1.
DR Gene3D; 3.30.70.3530; -; 1.
DR InterPro; IPR039791; GCM.
DR InterPro; IPR036115; GCM_dom_sf.
DR InterPro; IPR043020; GCM_large.
DR InterPro; IPR043021; GCM_small.
DR InterPro; IPR003902; Tscrpt_reg_GCM.
DR PANTHER; PTHR12414; PTHR12414; 1.
DR Pfam; PF03615; GCM; 1.
DR SUPFAM; SSF90073; SSF90073; 1.
DR PROSITE; PS50807; GCM; 1.
PE 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..504
FT /note="Transcription factor glial cells missing"
FT /id="PRO_0000126652"
FT DNA_BIND 32..188
FT /note="GCM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00245"
FT REGION 214..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 413
FT /note="F -> I (in Ref. 1; AAC46912, 2; BAA10905 and 3;
FT AAC47808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 56202 MW; 0ED74C2D3B9BBCB0 CRC64;
MVLNGMPITM PVPMPVPMPV PSPPATKSRV AIDWDINDSK MPSVGEFDDF NDWSNGHCRL
IYSVQSDEAR KHASGWAMRN TNNHNVNILK KSCLGVLLCS AKCKLPNGAS VHLRPAICDK
ARRKQQGKQC PNRNCNGRLE IQACRGHCGY PVTHFWRRDG NGIYFQAKGT HDHPRPEAKG
STEARRLLAG GRRVRSLAVM LARESALSDK LSSLRPTKRQ AKTQSIQESK RRRMGASDVL
ETKQELVVPP TTYLPTSTPT HSTNFNQSQG SYVPAGQGSV ISQWNREIHY ETEDPCYANG
MYSYDMLHSP LSAHSSTGSY YQENKPQQLQ HSQYQQQLSP QQHVPVSYDP SQPISSSLQC
GMPSYEICDD TSSLTSSSGY CSEDYGYYNG YLPNSLDVSN GSQSQNLSQD ASFYTTSSEI
FSVFESTLNG GGTSGVDLIY DEATAYQQHQ QQGTFPHLTN YQQEPQDQMQ SADYYYSNTG
VDNSWNIQMD ATYHPVNSTD PIYC
