AP2E_MOUSE
ID AP2E_MOUSE Reviewed; 442 AA.
AC Q6VUP9; A2A883;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Transcription factor AP-2-epsilon;
DE Short=AP2-epsilon;
DE AltName: Full=Activating enhancer-binding protein 2-epsilon;
GN Name=Tfap2e; Synonyms=Tcfap2e;
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:AAQ90059.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=CD-1 {ECO:0000312|EMBL:AAQ90059.1};
RX PubMed=14636996; DOI=10.1016/s0378-1119(03)00840-0;
RA Tummala R., Romano R.-A., Fuchs E., Sinha S.;
RT "Molecular cloning and characterization of AP-2 epsilon, a fifth member of
RT the AP-2 family.";
RL Gene 321:93-102(2003).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=14572467; DOI=10.1016/s1044-7431(03)00209-4;
RA Feng W., Williams T.;
RT "Cloning and characterization of the mouse AP-2 epsilon gene: a novel
RT family member expressed in the developing olfactory bulb.";
RL Mol. Cell. Neurosci. 24:460-475(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16684505; DOI=10.1016/j.bbrc.2006.04.123;
RA Wenke A.-K., Rothhammer T., Moser M., Bosserhoff A.K.;
RT "Regulation of integrin alpha10 expression in chondrocytes by the
RT transcription factors AP-2epsilon and Ets-1.";
RL Biochem. Biophys. Res. Commun. 345:495-501(2006).
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. AP-2-epsilon
CC may play a role in the development of the CNS and in cartilage
CC differentiation. {ECO:0000269|PubMed:14572467,
CC ECO:0000269|PubMed:14636996, ECO:0000269|PubMed:16684505}.
CC -!- SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers with
CC other AP-2 family members (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16684505}.
CC -!- TISSUE SPECIFICITY: Expressed most prominently in the mitral cell layer
CC of the developing olfactory bulb and to a lesser extent in the granule
CC cell layer. Also expressed in skin, articular cartilage, primary
CC chondrocytes, and chondrosarcoma cell line SW1353.
CC {ECO:0000269|PubMed:14572467, ECO:0000269|PubMed:14636996,
CC ECO:0000269|PubMed:16684505}.
CC -!- SIMILARITY: Belongs to the AP-2 family. {ECO:0000255}.
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DR EMBL; AY325902; AAQ90059.1; -; mRNA.
DR EMBL; AL607129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18658.1; -.
DR RefSeq; NP_945198.2; NM_198960.2.
DR AlphaFoldDB; Q6VUP9; -.
DR BioGRID; 237142; 2.
DR STRING; 10090.ENSMUSP00000035902; -.
DR iPTMnet; Q6VUP9; -.
DR PhosphoSitePlus; Q6VUP9; -.
DR MaxQB; Q6VUP9; -.
DR PaxDb; Q6VUP9; -.
DR PeptideAtlas; Q6VUP9; -.
DR PRIDE; Q6VUP9; -.
DR ProteomicsDB; 296327; -.
DR Antibodypedia; 31581; 57 antibodies from 17 providers.
DR DNASU; 332937; -.
DR Ensembl; ENSMUST00000048194; ENSMUSP00000035902; ENSMUSG00000042477.
DR GeneID; 332937; -.
DR KEGG; mmu:332937; -.
DR UCSC; uc008uts.1; mouse.
DR CTD; 339488; -.
DR MGI; MGI:2679630; Tfap2e.
DR VEuPathDB; HostDB:ENSMUSG00000042477; -.
DR eggNOG; KOG3811; Eukaryota.
DR GeneTree; ENSGT00950000182848; -.
DR HOGENOM; CLU_035175_4_1_1; -.
DR InParanoid; Q6VUP9; -.
DR OMA; QEAGYPH; -.
DR OrthoDB; 641707at2759; -.
DR PhylomeDB; Q6VUP9; -.
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; 332937; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q6VUP9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6VUP9; protein.
DR Bgee; ENSMUSG00000042477; Expressed in primary oocyte and 37 other tissues.
DR Genevisible; Q6VUP9; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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 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..442
FT /note="Transcription factor AP-2-epsilon"
FT /id="PRO_0000309517"
FT REGION 287..417
FT /note="H-S-H (helix-span-helix), dimerization"
FT /evidence="ECO:0000255"
FT MOTIF 54..59
FT /note="PPxY motif"
FT /evidence="ECO:0000255"
FT MOD_RES 246
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P05549"
FT CONFLICT 269
FT /note="G -> S (in Ref. 1; AAQ90059)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 46283 MW; F069B53A483F69CB CRC64;
MLVHTYSAME RPDGLGAAAG GTRLSSLPQA AYGPAPPLCH TPAASATADY HPPYFPPPYP
QAPLPYGQGP DATAAFPHLA ADPYGGLAPL AQPQPPQAAW AAPRAAARAH DEPPGLLAPP
ARALGLDPRR DYAAAVPRLL HSLADGAHGL ADAPLGLPGL AEPPGLEELQ AIDDPGMSLL
DQSVIKKVPI PSKAGSLSTL ALSKDSLVGG ISNPSEVFCS VPGRLSLLSS TSKYKVTVGE
VQRRLSPPEC LNASLLGGVL RRAKSKNGGR CLRERLEKIG LNLPAGRRKA ANVTLLTSLV
EGEAVHLARD FGYVCETEFP AKAAAEYLCR QHADPGELHS RKSMLLAAKQ ICKEFADLMA
QDRSPLGNSR PALILEPGVQ SCLTHFSLIT HGFGGPAICA ALTAFQNYLL ESLKGLEKMF
LSGAGGGHGE SKASEKDTKH RK
