SPTF3_CAEEL
ID SPTF3_CAEEL Reviewed; 412 AA.
AC Q9XW26;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Specificity protein transcription factor 3 {ECO:0000312|WormBase:Y40B1A.4};
GN Name=sptf-3 {ECO:0000312|WormBase:Y40B1A.4};
GN ORFNames=Y40B1A.4 {ECO:0000312|WormBase:Y40B1A.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PHE-344.
RX PubMed=21884786; DOI=10.1016/j.mod.2011.08.003;
RA Ulm E.A., Sleiman S.F., Chamberlin H.M.;
RT "Developmental functions for the Caenorhabditis elegans Sp protein SPTF-
RT 3.";
RL Mech. Dev. 128:428-441(2011).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23851392; DOI=10.1038/nature12329;
RA Hirose T., Horvitz H.R.;
RT "An Sp1 transcription factor coordinates caspase-dependent and -independent
RT apoptotic pathways.";
RL Nature 500:354-358(2013).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26434722; DOI=10.1534/genetics.115.183137;
RA Sullivan-Brown J.L., Tandon P., Bird K.E., Dickinson D.J., Tintori S.C.,
RA Heppert J.K., Meserve J.H., Trogden K.P., Orlowski S.K., Conlon F.L.,
RA Goldstein B.;
RT "Identifying Regulators of Morphogenesis Common to Vertebrate Neural Tube
RT Closure and Caenorhabditis elegans Gastrulation.";
RL Genetics 202:123-139(2016).
CC -!- FUNCTION: Transcription factor (PubMed:21884786, PubMed:23851392).
CC Binds to GC-rich DNA motifs, such as 5'-GGGCGGGG-3' (PubMed:21884786,
CC PubMed:23851392). Involved in cell autonomous neuroblast asymmetric
CC divisions that generate one precursor cell and one apoptotic cell, by
CC transcriptionally activating target genes, such as cell death activator
CC egl-1 and leucine zipper kinase pig-1, in caspase-dependent and
CC -independent apoptotic pathways (PubMed:23851392). Plays a role in the
CC regulation of apoptosis, cell lineage, cell differentiation, embryonic
CC morphogenesis, vulval development, and oocyte production
CC (PubMed:21884786, PubMed:23851392, PubMed:26434722).
CC {ECO:0000269|PubMed:21884786, ECO:0000269|PubMed:23851392,
CC ECO:0000269|PubMed:26434722}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23851392,
CC ECO:0000269|PubMed:26434722}.
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously in embryos and early larval
CC animals (PubMed:23851392). Expressed in MSpaa in embryos and in the
CC pharyngeal M4 motorneuron at the first larval stage; expression in the
CC M4 neuron and g1A cells decreases during larval development
CC (PubMed:23851392). Strongly expressed in the seam cells and the hyp7
CC cells (PubMed:23851392). {ECO:0000269|PubMed:23851392}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes defects in cell
CC fate, embryonic morphogenesis, and embryonic and larval lethality
CC (PubMed:21884786, PubMed:23851392). Defects in gastrulation; failure of
CC endodermal E cells to internalize at the 26- to 28-cell stage
CC (PubMed:26434722). Reduces cell cycle lengths significantly in
CC endodermal E cells (PubMed:26434722). Significant reduction in
CC expression of end-1 and end-3, and enhances the disruption of
CC intestinal development in an end-3 mutant background (PubMed:26434722).
CC Reduces number of offspring, and the production of oocytes is
CC compromised (PubMed:21884786). Failure of cell death in pharyngeal M4
CC motor neuron sister (PubMed:21884786). {ECO:0000269|PubMed:21884786,
CC ECO:0000269|PubMed:23851392, ECO:0000269|PubMed:26434722}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; BX284601; CAA22307.3; -; Genomic_DNA.
DR RefSeq; NP_493353.3; NM_060952.3.
DR AlphaFoldDB; Q9XW26; -.
DR SMR; Q9XW26; -.
DR STRING; 6239.Y40B1A.4; -.
DR EPD; Q9XW26; -.
DR PaxDb; Q9XW26; -.
DR PeptideAtlas; Q9XW26; -.
DR EnsemblMetazoa; Y40B1A.4.1; Y40B1A.4.1; WBGene00012735.
DR GeneID; 189783; -.
DR KEGG; cel:CELE_Y40B1A.4; -.
DR UCSC; Y40B1A.4; c. elegans.
DR CTD; 189783; -.
DR WormBase; Y40B1A.4; CE42686; WBGene00012735; sptf-3.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_809480_0_0_1; -.
DR InParanoid; Q9XW26; -.
DR OMA; EAPKRCA; -.
DR OrthoDB; 1085860at2759; -.
DR Reactome; R-CEL-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-CEL-6807505; RNA polymerase II transcribes snRNA genes.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00012735; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0003682; F:chromatin binding; IDA:WormBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:WormBase.
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:0009887; P:animal organ morphogenesis; IMP:UniProtKB.
DR GO; GO:0055059; P:asymmetric neuroblast division; IMP:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IMP:UniProtKB.
DR GO; GO:0014019; P:neuroblast development; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:WormBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase.
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; 2.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..412
FT /note="Specificity protein transcription factor 3"
FT /id="PRO_0000454566"
FT ZN_FING 316..338
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 344..368
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 374..396
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 344
FT /note="F->I: In gu85; fails to bind DNA. Defects in the
FT morphology of vulval structures, resulting in protruding
FT vulva and occasional bivulva phenotypes in adults. Reduced
FT brood size. Embryonic and L1 larval arrest and
FT morphological defects."
FT /evidence="ECO:0000269|PubMed:21884786"
SQ SEQUENCE 412 AA; 46969 MW; 85BCB20910008A66 CRC64;
MSKSGQQQQP HQQMQQQQQQ QGKMMVVHHQ RTTTPDGSQV YLLQPSQSHP QQRQVQFIPI
QVAQGEKKPQ TVMMNQMMGQ QQQQQPSSSN QQSQQQVQQQ QQQVHQVQQV QQHQMQQQNQ
TVQQQHLMME TIDQVGSGII GNSNGNNQQQ QQQQQQQQQR RDPIPIAPAG MVSGQRMQQQ
QQQPQQQQQH NNNNTGASTS NGGVNAAPVM PVMGGQQRIT LGNLHFQQDP NDPQKWIITN
EGPPVAGPSA PARKPNQIQH RQMIPQMNED GMMNMGNDYG DINGQGLGEA PKRCACTCPN
CLQQNNRQGD GKSRIHICHL CNKTYGKTSH LRAHLRGHAG NKPFACDWQH CNKKFTRSDE
LQRHRRTHTG EKRFACNHCG KKFMRSDHLT KHERTHQSNR INNINQQTLR LS
