SQZ_DROPS
ID SQZ_DROPS Reviewed; 550 AA.
AC Q293Q2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Zinc finger protein squeeze;
GN Name=sqz; ORFNames=GA18968;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with nab; which acts as a coactivator. Interacts
CC with ap (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; CM000070; EAL29162.2; -; Genomic_DNA.
DR AlphaFoldDB; Q293Q2; -.
DR SMR; Q293Q2; -.
DR STRING; 7237.FBpp0284930; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_026739_0_0_1; -.
DR InParanoid; Q293Q2; -.
DR OMA; QRQAMND; -.
DR Proteomes; UP000001819; Genome assembly.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Developmental protein; Differentiation; Metal-binding; Neurogenesis;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..550
FT /note="Zinc finger protein squeeze"
FT /id="PRO_0000372666"
FT ZN_FING 182..204
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 210..232
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 238..262
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 268..290
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 299..321
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 73..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 424
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 494
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 496
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 550 AA; 61388 MW; 6AC12E8A057537A4 CRC64;
MAELPTAPNG VSSGDYLHRS IDQLRSLTHL TTADLRTAQL VHDYKPFNIN EFRQNVVERL
DYSLKNGLVH HQQQQQQQQQ QEMLQQQQQH QAHQEQQQQQ QQQQQQHHHQ QQQHHLKSSY
SAPSSPPTPH EQQEQKYDPN RSPQRPLMSS GSNASSPEDD RRGSGGGPGG GGGGDGDQSK
PYKCASCSKS FANSSYLSQH TRIHLGIKPY RCEICQRKFT QLSHLQQHIR THTGDKPYKC
RHAGCPKAFS QLSNLQSHSR CHQTDKPFKC NSCYKCFADE MTLLEHIPKH KDSKHLKTHI
CNLCGKSYTQ ETYLQKHLQK HAEKAEKQQQ RHSSQVAAVQ QHVPSGGIGL NLQRQAMNDV
NAAYWAKMGA DSAAASLAEA IQQQLPQTNG QTYANFATLQ QHQQQQQQQQ QDMLQQHHQR
LADTPGHSHS PHEDPAGEDL VLRQTTPQHH LQQQQQQQQP SPGPGSSAFT PLSATVPPSH
LQQHRGAPAA TAAYLYQQNA AAAAAAFPTQ LISLHQIRNY AHQPGAAGLI AGDHLTLGLS
AVQAAKEKAQ
