AP2D_MOUSE
ID AP2D_MOUSE Reviewed; 452 AA.
AC Q91ZK0; A7MCU6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Transcription factor AP-2-delta;
DE Short=AP2-delta;
DE AltName: Full=Activating enhancer-binding protein 2-delta;
GN Name=Tfap2d; Synonyms=Tcfap2d;
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] {ECO:0000305, ECO:0000312|EMBL:AAL16940.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAL16940.1};
RC TISSUE=Fetal head {ECO:0000269|PubMed:11522791};
RX PubMed=11522791; DOI=10.1074/jbc.m106284200;
RA Zhao F., Satoda M., Licht J.D., Hayashizaki Y., Gelb B.D.;
RT "Cloning and characterization of a novel mouse AP-2 transcription factor,
RT AP-2delta, with unique DNA binding and transactivation properties.";
RL J. Biol. Chem. 276:40755-40760(2001).
RN [2] {ECO:0000312|EMBL:AAI52325.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=12711551; DOI=10.1016/s1567-133x(02)00067-4;
RA Zhao F., Lufkin T., Gelb B.D.;
RT "Expression of Tfap2d, the gene encoding the transcription factor Ap-2
RT delta, during mouse embryogenesis.";
RL Gene Expr. Patterns 3:213-217(2003).
CC -!- FUNCTION: Sequence-specific DNA-binding protein that interacts with
CC inducible viral and cellular enhancer elements to regulate
CC transcription of selected genes. AP-2 factors bind to the consensus
CC sequence 5'-GCCNNNGGC-3' and activate genes involved in a large
CC spectrum of important biological functions including proper eye, face,
CC body wall, limb and neural tube development. They also suppress a
CC number of genes including MCAM/MUC18, C/EBP alpha and MYC.
CC {ECO:0000269|PubMed:11522791, ECO:0000305}.
CC -!- SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers with
CC other AP-2 family members. {ECO:0000269|PubMed:11522791}.
CC -!- INTERACTION:
CC Q91ZK0; Q91X20: Ash2l; NbExp=4; IntAct=EBI-15703453, EBI-1556554;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in both embryonic and newborn brain.
CC {ECO:0000269|PubMed:11522791}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected at 9.5 dpc in the
CC central nervous system and the developing heart. The signal detected in
CC heart persists through to 10.5 dpc. Diffusely expressed in developing
CC brain at 10.5 dpc to 11.5 dpc, but by 13.5 dpc expression is mostly
CC confined to the midbrain and forebrain. Also expressed in the spinal
CC cord at 10.5 dpc, and in retinal epithelium from 13.5 dpc to 16.5 dpc.
CC No signals detected in tissues such as the neural crest, facial
CC mesenchyme, and limbs where other Tfap2 genes are expressed.
CC {ECO:0000269|PubMed:12711551}.
CC -!- SIMILARITY: Belongs to the AP-2 family. {ECO:0000255}.
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DR EMBL; AF421891; AAL16940.1; -; mRNA.
DR EMBL; BC152324; AAI52325.1; -; mRNA.
DR EMBL; BC152325; AAI52326.1; -; mRNA.
DR CCDS; CCDS14838.1; -.
DR RefSeq; NP_694794.1; NM_153154.3.
DR AlphaFoldDB; Q91ZK0; -.
DR SMR; Q91ZK0; -.
DR BioGRID; 230568; 14.
DR DIP; DIP-46108N; -.
DR IntAct; Q91ZK0; 3.
DR STRING; 10090.ENSMUSP00000037699; -.
DR PhosphoSitePlus; Q91ZK0; -.
DR MaxQB; Q91ZK0; -.
DR PaxDb; Q91ZK0; -.
DR PeptideAtlas; Q91ZK0; -.
DR PRIDE; Q91ZK0; -.
DR ProteomicsDB; 281785; -.
DR Antibodypedia; 30864; 142 antibodies from 25 providers.
DR DNASU; 226896; -.
DR Ensembl; ENSMUST00000037294; ENSMUSP00000037699; ENSMUSG00000042596.
DR GeneID; 226896; -.
DR KEGG; mmu:226896; -.
DR UCSC; uc007akp.1; mouse.
DR CTD; 83741; -.
DR MGI; MGI:2153466; Tfap2d.
DR VEuPathDB; HostDB:ENSMUSG00000042596; -.
DR eggNOG; KOG3811; Eukaryota.
DR GeneTree; ENSGT00950000182848; -.
DR HOGENOM; CLU_035175_5_0_1; -.
DR InParanoid; Q91ZK0; -.
DR OMA; GHTNSEK; -.
DR OrthoDB; 641707at2759; -.
DR PhylomeDB; Q91ZK0; -.
DR TreeFam; TF313718; -.
DR Reactome; R-MMU-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR Reactome; R-MMU-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR BioGRID-ORCS; 226896; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q91ZK0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91ZK0; protein.
DR Bgee; ENSMUSG00000042596; Expressed in ureteric bud trunk and 58 other tissues.
DR Genevisible; Q91ZK0; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IPI:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0061379; P:inferior colliculus development; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR InterPro; IPR004979; TF_AP2.
DR InterPro; IPR013854; TF_AP2_C.
DR PANTHER; PTHR10812; PTHR10812; 1.
DR Pfam; PF03299; TF_AP-2; 1.
DR PRINTS; PR01748; AP2TNSCPFCT.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..452
FT /note="Transcription factor AP-2-delta"
FT /id="PRO_0000309514"
FT REGION 280..410
FT /note="H-S-H (helix-span-helix), dimerization"
FT /evidence="ECO:0000255"
FT REGION 416..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 239
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P05549"
FT CONFLICT 37
FT /note="T -> A (in Ref. 2; AAI52326/AAI52325)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 49548 MW; 6722342B15CDF9EB CRC64;
MSTTFPGLVH DAEIRHDGSN SYRLMQLGCL ESVANSTVAY SSSSPLTYST TGTEFASPYF
STNHQYTPLH HQSFHYEFQH SHPAVTPDAY SLNSLHHSQQ YYQQIHHGEP TDFINLHNAR
ALKSSCLDEQ RRELGCLDAY RRHDLSLMSH GSQYGMHPDQ RLLPGPSLGL AAAGADDLQG
SVEAQCGIVL NGQGGVIRRG GTCVVNPTDL FCSVPGRLSL LSSTSKYKVT IAEVKRRLSP
PECLNASLLG GILRRAKSKN GGRCLREKLD RLGLNLPAGR RKAANVTLLT SLVEGEALHL
ARDFGYTCET EFPAKAVGEH LARQHMEQKE QTARKKMILA TKQICKEFQD LLSQDRSPLG
SSRPTPILDL DIQRHLTHFS LITHGFGTPA ICAALSTFQT VLSEMLNYLE KHTTHKNGGA
ADSGQGHANS EKAPLRKASE AAVKEGKTEK TD