SCRT1_MOUSE
ID SCRT1_MOUSE Reviewed; 348 AA.
AC Q99M85;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Transcriptional repressor scratch 1;
DE AltName: Full=Scratch homolog 1 zinc finger protein;
DE Short=SCRT;
DE Short=Scratch 1;
DE Short=mScrt;
GN Name=Scrt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=11274425; DOI=10.1073/pnas.051014098;
RA Nakakura E.K., Watkins D.N., Schuebel K.E., Sriuranpong V., Borges M.W.,
RA Nelkin B.D., Ball D.W.;
RT "Mammalian scratch: a neural-specific snail family transcriptional
RT repressor.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4010-4015(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Fetal brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=11687288; DOI=10.1016/s0169-328x(01)00246-7;
RA Nakakura E.K., Watkins D.N., Sriuranpong V., Borges M.W., Nelkin B.D.,
RA Ball D.W.;
RT "Mammalian scratch participates in neuronal differentiation in P19
RT embryonal carcinoma cells.";
RL Brain Res. Mol. Brain Res. 95:162-166(2001).
RN [4]
RP INTERACTION WITH LIMD1; WTIP AND AJUBA.
RX PubMed=18331720; DOI=10.1016/j.devcel.2008.01.005;
RA Langer E.M., Feng Y., Zhaoyuan H., Rauscher F.J. III, Kroll K.L.,
RA Longmore G.D.;
RT "Ajuba LIM proteins are snail/slug corepressors required for neural crest
RT development in Xenopus.";
RL Dev. Cell 14:424-436(2008).
CC -!- FUNCTION: Transcriptional repressor that binds E-box motif CAGGTG (By
CC similarity). Appears to function downstream of proneural bHLH proteins
CC in promoting neural differentiation. {ECO:0000250,
CC ECO:0000269|PubMed:11687288}.
CC -!- SUBUNIT: Interacts (via SNAG domain) with LIMD1 (via LIM domains), WTIP
CC (via LIM domains) and AJUBA (via LIM domains).
CC {ECO:0000269|PubMed:18331720}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Detected throughout the spinal cord except in the
CC ventricular zone surrounding the central canal, which contains
CC proliferating neurons, and dorsal root ganglia at 11.5 dpc. At 12.5
CC dpc, detected in the telencephalon, and by 14.5 dpc a distinct laminar
CC pattern of expression was seen in regions adjacent to the ventricular
CC zone. In the developing eye, expression was detected in the inner
CC nuclear layer of the retina beginning at 13.5 dpc.
CC {ECO:0000269|PubMed:11274425}.
CC -!- DOMAIN: The N-terminal non zinc-finger region mediates the repressor
CC activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the snail C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AY014997; AAK01468.1; -; mRNA.
DR EMBL; BC057562; AAH57562.1; -; mRNA.
DR CCDS; CCDS37123.1; -.
DR RefSeq; NP_570963.1; NM_130893.3.
DR AlphaFoldDB; Q99M85; -.
DR SMR; Q99M85; -.
DR STRING; 10090.ENSMUSP00000094093; -.
DR iPTMnet; Q99M85; -.
DR PhosphoSitePlus; Q99M85; -.
DR MaxQB; Q99M85; -.
DR PaxDb; Q99M85; -.
DR PRIDE; Q99M85; -.
DR ProteomicsDB; 256939; -.
DR Antibodypedia; 59727; 29 antibodies from 13 providers.
DR DNASU; 170729; -.
DR Ensembl; ENSMUST00000096365; ENSMUSP00000094093; ENSMUSG00000048385.
DR Ensembl; ENSMUST00000164703; ENSMUSP00000131152; ENSMUSG00000048385.
DR GeneID; 170729; -.
DR KEGG; mmu:170729; -.
DR UCSC; uc007wko.1; mouse.
DR CTD; 83482; -.
DR MGI; MGI:2176606; Scrt1.
DR VEuPathDB; HostDB:ENSMUSG00000048385; -.
DR eggNOG; KOG2462; Eukaryota.
DR GeneTree; ENSGT00940000154491; -.
DR HOGENOM; CLU_002678_42_3_1; -.
DR InParanoid; Q99M85; -.
DR OMA; RCHKAFA; -.
DR OrthoDB; 1332418at2759; -.
DR PhylomeDB; Q99M85; -.
DR TreeFam; TF315515; -.
DR BioGRID-ORCS; 170729; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Scrt1; mouse.
DR PRO; PR:Q99M85; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q99M85; protein.
DR Bgee; ENSMUSG00000048385; Expressed in cerebellar cortex and 90 other tissues.
DR Genevisible; Q99M85; MM.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:2001222; P:regulation of neuron migration; IMP:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR029794; SCRATCH1/2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24388:SF60; PTHR24388:SF60; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..348
FT /note="Transcriptional repressor scratch 1"
FT /id="PRO_0000047037"
FT ZN_FING 191..213
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 222..244
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 248..270
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 276..298
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 304..327
FT /note="C2H2-type 5; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..20
FT /note="SNAG domain"
FT /evidence="ECO:0000250"
FT REGION 130..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 35919 MW; 98734743D56C204F CRC64;
MPRSFLVKKV KLDTFSSADL DSSYGRARSD LGVRLQDKGY LSDYVGPASV YDGDAEAALL
KGPSPEPMYA AAVRGELGPA ASGSAPPPTP RPELATAAGG YINGDAAVSE GYAADAFFIT
DGRSRRKAAN ANAAAAPSTA SVAAPDSDAG GGGGPGTRGS GSGSASRGGT RVGAGTEARA
GSGATGAGGR HACGECGKTY ATSSNLSRHK QTHRSLDSQL ARRCPTCGKV YVSMPAMAMH
LLTHDLRHKC GVCGKAFSRP WLLQGHMRSH TGEKPFGCAH CGKAFADRSN LRAHMQTHSA
FKHFQCKRCK KSFALKSYLN KHYESACFKG GASGPATPAP PQLSPVQA
