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Transcription factor AP-2-alpha (AP2-alpha) (AP-2 transcription factor) (Activating enhancer-binding protein 2-alpha) (Activator protein 2) (AP-2)

 AP2A_BOVIN              Reviewed;         437 AA.
A1A4R9;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 1.
22-NOV-2017, entry version 76.
RecName: Full=Transcription factor AP-2-alpha;
Short=AP2-alpha;
AltName: Full=AP-2 transcription factor;
AltName: Full=Activating enhancer-binding protein 2-alpha;
AltName: Full=Activator protein 2;
Short=AP-2;
Name=TFAP2A;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Fetal skin;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Sequence-specific DNA-binding protein that interacts
with inducible viral and cellular enhancer elements to regulate
transcription of selected genes. AP-2 factors bind to the
consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in
a large spectrum of important biological functions including
proper eye, face, body wall, limb and neural tube development.
They also suppress a number of genes including MCAM/MUC18, C/EBP
alpha and MYC. AP-2-alpha is the only AP-2 protein required for
early morphogenesis of the lens vesicle. Together with the CITED2
coactivator, stimulates the PITX2 P1 promoter transcription
activation. Associates with chromatin to the PITX2 P1 promoter
region (By similarity). {ECO:0000250}.
-!- SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers
with other AP-2 family members. Interacts with WWOX. Interacts
with CITED4. Interacts with UBE2I. Interacts with RALBP1 in a
complex also containing EPN1 and NUMB during interphase and
mitosis. Interacts with KCTD1; this interaction represses
transcription activation. Interacts (via C-terminus) with CITED2
(via C-terminus); the interaction stimulates TFAP2A-
transcriptional activation. Interacts (via N-terminus) with EP300
(via N-terminus); the interaction requires CITED2 (By similarity).
Interacts with KCTD15; this interaction inhibits TFAP2A
transcriptional activation (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- DOMAIN: The PPxY motif mediates interaction with WWOX.
{ECO:0000250}.
-!- PTM: Sumoylated on Lys-10; which inhibits transcriptional
activity. {ECO:0000305}.
-!- SIMILARITY: Belongs to the AP-2 family. {ECO:0000305}.
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EMBL; BC126845; AAI26846.1; -; mRNA.
RefSeq; NP_001073697.1; NM_001080228.1.
UniGene; Bt.2750; -.
STRING; 9913.ENSBTAP00000001651; -.
PaxDb; A1A4R9; -.
PRIDE; A1A4R9; -.
Ensembl; ENSBTAT00000001651; ENSBTAP00000001651; ENSBTAG00000001250.
GeneID; 505849; -.
KEGG; bta:505849; -.
CTD; 7020; -.
eggNOG; KOG3811; Eukaryota.
eggNOG; ENOG410XR9E; LUCA.
GeneTree; ENSGT00550000074577; -.
HOGENOM; HOG000231737; -.
HOVERGEN; HBG002455; -.
InParanoid; A1A4R9; -.
KO; K09176; -.
OMA; PNEQVQR; -.
OrthoDB; EOG091G0PR6; -.
TreeFam; TF313718; -.
Reactome; R-BTA-8864260; Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors.
Reactome; R-BTA-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
Reactome; R-BTA-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
Reactome; R-BTA-8869496; TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation.
Proteomes; UP000009136; Chromosome 23.
Bgee; ENSBTAG00000001250; -.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
GO; GO:0000982; F:transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISS:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISS:UniProtKB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISS:UniProtKB.
GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
GO; GO:0060349; P:bone morphogenesis; ISS:UniProtKB.
GO; GO:0071281; P:cellular response to iron ion; ISS:UniProtKB.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISS:UniProtKB.
GO; GO:0035115; P:embryonic forelimb morphogenesis; ISS:UniProtKB.
GO; GO:0061029; P:eyelid development in camera-type eye; ISS:UniProtKB.
GO; GO:0042472; P:inner ear morphogenesis; ISS:UniProtKB.
GO; GO:0001822; P:kidney development; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0021623; P:oculomotor nerve formation; ISS:UniProtKB.
GO; GO:0003409; P:optic cup structural organization; ISS:UniProtKB.
GO; GO:0003404; P:optic vesicle morphogenesis; ISS:UniProtKB.
GO; GO:0060021; P:palate development; ISS:UniProtKB.
GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0070172; P:positive regulation of tooth mineralization; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0045595; P:regulation of cell differentiation; IEA:Ensembl.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0010842; P:retina layer formation; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
GO; GO:0021559; P:trigeminal nerve development; ISS:UniProtKB.
InterPro; IPR004979; TF_AP2.
InterPro; IPR008121; TF_AP2_alpha_N.
InterPro; IPR013854; TF_AP2_C.
PANTHER; PTHR10812; PTHR10812; 1.
PANTHER; PTHR10812:SF8; PTHR10812:SF8; 1.
Pfam; PF03299; TF_AP-2; 1.
PRINTS; PR01749; AP2ATNSCPFCT.
PRINTS; PR01748; AP2TNSCPFCT.
2: Evidence at transcript level;
Activator; Complete proteome; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 437 Transcription factor AP-2-alpha.
/FTId=PRO_0000285968.
REGION 280 410 H-S-H (helix-span-helix), dimerization.
{ECO:0000250}.
MOTIF 57 62 PPxY motif.
COMPBIAS 29 117 Gln/Pro-rich (transactivation domain).
MOD_RES 239 239 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P05549}.
CROSSLNK 10 10 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 10 10 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P05549}.
CROSSLNK 177 177 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05549}.
CROSSLNK 184 184 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05549}.
SEQUENCE 437 AA; 47984 MW; 1C7D10571D4C2226 CRC64;
MLWKLTDNIK YEDCEDRHDG ASNGTARLPQ LGTVGQSPYT SAPPLSHTPN ADFQPPYFPP
PYQPIYPQSQ DPYSHVNDPY SLNPLHAQPQ PQHPGWPGQR QSQESGLLHT HRGLPHQLSG
LDPRRDYRRH EDLLHGPHGL GSGLGDLPIH SLPHAIEDVP HVEDPGINIP DQTVIKKGPV
SLSKSNSNAV SAIPINKDNL FGGVVNPNEV FCSVPGRLSL LSSTSKYKVT VAEVQRRLSP
PECLNASLLG GVLRRAKSKN GGRSLREKLD KIGLNLPAGR RKAANVTLLT SLVEGEAVHL
ARDFGYVCET EFPAKAVAEF LNRQHSDPNE QVTRKNMLLA TKQICKEFTD LLAQDRSPLG
NSRPNPILEP GIQSCLTHFN LISHGFGSPA VCAAVTALQN YLTEALKAMD KMYLSNNPNS
HTDNNAKSSD KEEKHRK


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