AP2A_SHEEP
ID AP2A_SHEEP Reviewed; 491 AA.
AC Q9N0N3; Q9N0N4; Q9N0N5;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Transcription factor AP-2-alpha;
DE Short=AP2-alpha;
DE AltName: Full=AP-2 transcription factor;
DE AltName: Full=Activating enhancer-binding protein 2-alpha;
DE AltName: Full=Activator protein 2;
DE Short=AP-2;
GN Name=TFAP2A;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RX PubMed=11298758; DOI=10.1046/j.1432-1327.2001.02124.x;
RA Limesand S.W., Anthony R.V.;
RT "Novel activator protein-2alpha splice-variants function as transactivators
RT of the ovine placental lactogen gene.";
RL Eur. J. Biochem. 268:2390-2401(2001).
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-alpha
CC is the only AP-2 protein required for early morphogenesis of the lens
CC vesicle. Together with the CITED2 coactivator, stimulates the PITX2 P1
CC promoter transcription activation. Associates with chromatin to the
CC PITX2 P1 promoter region (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers with
CC other AP-2 family members. Interacts with WWOX. Interacts with CITED4.
CC Interacts with UBE2I. Interacts with RALBP1 in a complex also
CC containing EPN1 and NUMB during interphase and mitosis. Interacts with
CC KCTD1; this interaction represses transcription activation. Interacts
CC (via C-terminus) with CITED2 (via C-terminus); the interaction
CC stimulates TFAP2A-transcriptional activation. Interacts (via N-
CC terminus) with EP300 (via N-terminus); the interaction requires CITED2
CC (By similarity). Interacts with KCTD15; this interaction inhibits
CC TFAP2A transcriptional activation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Variant 4;
CC IsoId=Q9N0N3-1; Sequence=Displayed;
CC Name=2; Synonyms=Variant 6;
CC IsoId=Q9N0N3-2; Sequence=VSP_006405;
CC Name=3; Synonyms=Variant 7;
CC IsoId=Q9N0N3-3; Sequence=VSP_006406, VSP_006407;
CC -!- DOMAIN: The PPxY motif mediates interaction with WWOX. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AP-2 family. {ECO:0000305}.
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DR EMBL; AF260570; AAF70347.1; -; mRNA.
DR EMBL; AF260569; AAF70346.1; -; mRNA.
DR EMBL; AF260568; AAF70345.1; -; mRNA.
DR RefSeq; NP_001009745.1; NM_001009745.1. [Q9N0N3-1]
DR AlphaFoldDB; Q9N0N3; -.
DR STRING; 9940.ENSOARP00000017604; -.
DR PRIDE; Q9N0N3; -.
DR GeneID; 443109; -.
DR KEGG; oas:443109; -.
DR CTD; 7020; -.
DR eggNOG; KOG3811; Eukaryota.
DR OrthoDB; 641707at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0060349; P:bone morphogenesis; ISS:UniProtKB.
DR GO; GO:0071281; P:cellular response to iron ion; ISS:UniProtKB.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISS:UniProtKB.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; ISS:UniProtKB.
DR GO; GO:0061029; P:eyelid development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0042472; P:inner ear morphogenesis; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0021623; P:oculomotor nerve formation; ISS:UniProtKB.
DR GO; GO:0003409; P:optic cup structural organization; ISS:UniProtKB.
DR GO; GO:0003404; P:optic vesicle morphogenesis; ISS:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0070172; P:positive regulation of tooth mineralization; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0060021; P:roof of mouth development; ISS:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR GO; GO:0021559; P:trigeminal nerve development; ISS:UniProtKB.
DR InterPro; IPR004979; TF_AP2.
DR InterPro; IPR008121; TF_AP2_alpha_N.
DR InterPro; IPR013854; TF_AP2_C.
DR PANTHER; PTHR10812; PTHR10812; 1.
DR Pfam; PF03299; TF_AP-2; 1.
DR PRINTS; PR01749; AP2ATNSCPFCT.
DR PRINTS; PR01748; AP2TNSCPFCT.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..491
FT /note="Transcription factor AP-2-alpha"
FT /id="PRO_0000184799"
FT REGION 74..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..464
FT /note="H-S-H (helix-span-helix), dimerization"
FT /evidence="ECO:0000250|UniProtKB:P05549"
FT REGION 468..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 111..116
FT /note="PPxY motif"
FT COMPBIAS 80..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..121
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 293
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P05549"
FT CROSSLNK 231
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05549"
FT CROSSLNK 238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05549"
FT VAR_SEQ 1..69
FT /note="MPPRLASVKIPYDWGRKGPFRFWRIFCQSRAVGWFLAAACGRAGRFRTQPAE
FT WPTPDAVFSPLGLALFQ -> MSILAKMGDWQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11298758"
FT /id="VSP_006405"
FT VAR_SEQ 1..69
FT /note="MPPRLASVKIPYDWGRKGPFRFWRIFCQSRAVGWFLAAACGRAGRFRTQPAE
FT WPTPDAVFSPLGLALFQ -> MLVHSFSAM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11298758"
FT /id="VSP_006406"
FT VAR_SEQ 88..135
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11298758"
FT /id="VSP_006407"
SQ SEQUENCE 491 AA; 53927 MW; 1DB0137C13268865 CRC64;
MPPRLASVKI PYDWGRKGPF RFWRIFCQSR AVGWFLAAAC GRAGRFRTQP AEWPTPDAVF
SPLGLALFQD RHDGASNGTA RLPQLGTVGQ SPYTSAPPLS HTPNADFQPP YFPPPYQPIY
PQSQDPYSHV NDPYSLNPLH AQPQPQHPGW PGQRQSQESG LLHTHRGLPH QLSGLDPRRD
YRRHEDLLHG PHGLGSGLGD LPIHSLPHAI EDVPHVEDPG INIPDQTVIK KGPVSLSKSN
SNAVSSIPIN KDNLFGGVVN PNEVFCSVPG RLSLLSSTSK YKVTVAEVQR RLSPPECLNA
SLLGGVLRRA KSKNGGRSLR EKLDKIGLNL PAGRRKAANV TLLTSLVEGE AVHLARDFGY
VCETEFPAKA VAEFLNRQHS DPNEQVTRKN MLLATKQICK EFTDLLAQDR SPLGNSRPNP
ILEPGIQSCL THFNLISHGF GSPAVCAAVT ALQNYLTEAL KAMDKMYLSN NPNSHTDNSA
KSSDKEEKHR K
