SQZ_DROME
ID SQZ_DROME Reviewed; 535 AA.
AC Q9VDZ3; Q8MT44; Q9U9A8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Zinc finger protein squeeze;
GN Name=sqz; ORFNames=CG5557;
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].
RA Barta J.L., Percival-Smith A.;
RT "GH22029 putative Zn finger transcription factor in 91F.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
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=Embryo;
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, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=12679036; DOI=10.1016/s0092-8674(03)00204-6;
RA Allan D.W., St Pierre S.E., Miguel-Aliaga I., Thor S.;
RT "Specification of neuropeptide cell identity by the integration of
RT retrograde BMP signaling and a combinatorial transcription factor code.";
RL Cell 113:73-86(2003).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=14568107; DOI=10.1016/s0925-4773(03)00159-x;
RA McGovern V.L., Pacak C.A., Sewell S.T., Turski M.L., Seeger M.A.;
RT "A targeted gain of function screen in the embryonic CNS of Drosophila.";
RL Mech. Dev. 120:1193-1207(2003).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH AP.
RX PubMed=15748845; DOI=10.1016/j.neuron.2005.01.026;
RA Allan D.W., Park D., St Pierre S.E., Taghert P.H., Thor S.;
RT "Regulators acting in combinatorial codes also act independently in single
RT differentiating neurons.";
RL Neuron 45:689-700(2005).
RN [8]
RP FUNCTION.
RX PubMed=17276922; DOI=10.1016/j.cub.2006.11.067;
RA Komiyama T., Luo L.;
RT "Intrinsic control of precise dendritic targeting by an ensemble of
RT transcription factors.";
RL Curr. Biol. 17:278-285(2007).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH NAB.
RX PubMed=17428824; DOI=10.1242/dev.003830;
RA Terriente Felix J., Magarinos M., Diaz-Benjumea F.J.;
RT "Nab controls the activity of the zinc-finger transcription factors Squeeze
RT and Rotund in Drosophila development.";
RL Development 134:1845-1852(2007).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=17442544; DOI=10.1016/j.mod.2007.03.001;
RA Herrero P., Magarinos M., Molina I., Benito J., Dorado B., Turiegano E.,
RA Canal I., Torroja L.;
RT "Squeeze involvement in the specification of Drosophila leucokinergic
RT neurons: Different regulatory mechanisms endow the same neuropeptide
RT selection.";
RL Mech. Dev. 124:427-440(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475; TYR-479 AND TYR-481, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-395; SER-399 AND SER-401, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Transcription factor involved in neuronal fate specification.
CC First required in embryonic CNS development to define the number of
CC cells that express apterous (ap) in the ap thoracic cluster of
CC interneurons. Later on, it plays a central role in the combinatorial
CC code of transcription factors that specifies the fate of the Tv neuron
CC in the ap cluster by participating in the transcription regulation of
CC FMRFa in Tv cells. Also required for projection neuron dendritic
CC targeting. {ECO:0000269|PubMed:12679036, ECO:0000269|PubMed:14568107,
CC ECO:0000269|PubMed:15748845, ECO:0000269|PubMed:17276922,
CC ECO:0000269|PubMed:17428824}.
CC -!- SUBUNIT: Interacts with nab; which acts as a coactivator. Interacts
CC with ap. {ECO:0000269|PubMed:15748845, ECO:0000269|PubMed:17428824}.
CC -!- INTERACTION:
CC Q9VDZ3; Q94527: Rel; NbExp=3; IntAct=EBI-2565022, EBI-869024;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Largely restricted to subsets of cells in the CNS
CC throughout embryonic and first instar larval (L1) development.
CC Expressed in a population of lateral interneurons, primarily projecting
CC axons in the anterior and posterior commissures. Overlaps with ap
CC within the thoracic ap cluster. By stage 17, it is restricted to 2
CC neurons within the ap-cluster, with one neuron typically continuing to
CC display higher levels of expression. Selectively expressed at higher
CC levels within the FMRFa Tv neurons. Expressed in all leucokinergic
CC cells. {ECO:0000269|PubMed:12679036, ECO:0000269|PubMed:14568107,
CC ECO:0000269|PubMed:15748845, ECO:0000269|PubMed:17428824,
CC ECO:0000269|PubMed:17442544}.
CC -!- DISRUPTION PHENOTYPE: Death at larval stage. Larvae display a motility
CC defect whereby the body wall musculature overcontract radially during
CC the peristaltic wave typical of insect larval motility, apparent as a
CC 'squeezing' of intestine. {ECO:0000269|PubMed:12679036,
CC ECO:0000269|PubMed:14568107}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF173847; AAD48878.1; -; mRNA.
DR EMBL; AE014297; AAF55644.2; -; Genomic_DNA.
DR EMBL; AY118393; AAM48422.1; -; mRNA.
DR RefSeq; NP_524403.1; NM_079679.3.
DR AlphaFoldDB; Q9VDZ3; -.
DR SMR; Q9VDZ3; -.
DR BioGRID; 67298; 11.
DR IntAct; Q9VDZ3; 7.
DR STRING; 7227.FBpp0083147; -.
DR iPTMnet; Q9VDZ3; -.
DR PaxDb; Q9VDZ3; -.
DR EnsemblMetazoa; FBtr0083733; FBpp0083147; FBgn0010768.
DR GeneID; 42300; -.
DR KEGG; dme:Dmel_CG5557; -.
DR UCSC; CG5557-RA; d. melanogaster.
DR CTD; 42300; -.
DR FlyBase; FBgn0010768; sqz.
DR VEuPathDB; VectorBase:FBgn0010768; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_026739_0_0_1; -.
DR InParanoid; Q9VDZ3; -.
DR OMA; QRQAMND; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9VDZ3; -.
DR BioGRID-ORCS; 42300; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42300; -.
DR PRO; PR:Q9VDZ3; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0010768; Expressed in wing disc and 21 other tissues.
DR ExpressionAtlas; Q9VDZ3; baseline and differential.
DR Genevisible; Q9VDZ3; DM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0070983; P:dendrite guidance; IMP:FlyBase.
DR GO; GO:0014019; P:neuroblast development; IMP:FlyBase.
DR GO; GO:0048666; P:neuron development; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Metal-binding; Neurogenesis;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..535
FT /note="Zinc finger protein squeeze"
FT /id="PRO_0000372665"
FT ZN_FING 158..180
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 186..208
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 214..238
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 244..266
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 275..297
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 70..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 395
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 479
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 481
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT CONFLICT 62
FT /note="G -> S (in Ref. 4; AAM48422)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="Q -> K (in Ref. 4; AAM48422)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="Q -> R (in Ref. 4; AAM48422)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 59549 MW; DEE682B62CDA486E CRC64;
MAELPTAPNG VPSGDYLHRS IDQLRSLGHL TTAQLVHDYK PFNISEFRQN VAERLDYSLK
NGLVQHQQQM VMEQQPHPDQ QQQQHLHHPQ QQQHPPQLKV SYSAPNSPPT PHEQQEQKYD
PNRSPPRQQM SSASGSGSNG SSPEEESRRG DGDQAKPYKC GSCSKSFANS SYLSQHTRIH
LGIKPYRCEI CQRKFTQLSH LQQHIRTHTG DKPYKCRHAG CPKAFSQLSN LQSHSRCHQT
DKPFKCNSCY KCFSDEMTLL EHIPKHKDSK HLKTHICNLC GKSYTQETYL QKHLQKHAEK
AEKQQHRHTA QVAAHQQHVP ASGIGLNLQR QAMNDVNAAY WAKMGADSAA ASLAEAIQQQ
LPQAGGQPYG NFASLQQQHQ QQQQELLHHQ RLADTPGHSH SPHEEAAGED LVLRQSTPQH
HLQQQQQQQQ QQQAQQQQQA QHQPSPGPGN SAFTPLSATV APPPHLQQHR GPPGSAAAYL
YQQNAAAAAA AFPTQLISLH QIRNYAHQPG AAGLIAGDHL ALGLSAVNAA KEKAQ
