DEAF1_PANTR
ID DEAF1_PANTR Reviewed; 565 AA.
AC O77562;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Deformed epidermal autoregulatory factor 1 homolog;
DE AltName: Full=Nuclear DEAF-1-related transcriptional regulator;
DE Short=NUDR;
GN Name=DEAF1;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=9773984; DOI=10.1210/mend.12.10.0181;
RA Huggenvik J.I., Michelson R.J., Collard M.W., Ziemba A.J., Gurley P.,
RA Mowen K.A.;
RT "Characterization of a nuclear deformed epidermal autoregulatory factor-1
RT (DEAF-1)-related (NUDR) transcriptional regulator protein.";
RL Mol. Endocrinol. 12:1619-1639(1998).
CC -!- FUNCTION: Transcription factor that binds to sequence with multiple
CC copies of 5'-TTC[CG]G-3' present in its own promoter and that of the
CC HNRPA2B1 gene. Down-regulates transcription of these genes. Binds to
CC the retinoic acid response element (RARE) 5'-AGGGTTCACCGAAAGTTCA-3'.
CC Activates the proenkephalin gene independently of promoter binding,
CC probably through protein-protein interaction. Regulates epithelial cell
CC proliferation and side-branching in the mammary gland. Required for
CC neural tube closure and skeletal patterning. Controls the expression of
CC peripheral tissue antigens in pancreatic lymph nodes. Transcriptional
CC activator of EIF4G3. May also involved in behavior (By similarity).
CC {ECO:0000250|UniProtKB:O75398, ECO:0000250|UniProtKB:Q9Z1T5}.
CC -!- SUBUNIT: Homodimer (By similarity).Interacts with LMO4; LMO4 blocks
CC export from nucleus. Interacts with LMO2 and CLIM2 (By similarity). May
CC interact with the corepressors NCOR1 and NCRO2. Identified in a complex
CC with XRCC5 and XRCC6. Interacts (via the SAND domain) with the DNA-PK
CC complex subunit XRCC6; the interaction is direct and may be inhibited
CC by DNA-binding (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00185}.
CC -!- PTM: May be phosphorylated by DNA-PK complex in a DNA independent
CC manner (in vitro). {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF049461; AAC79678.1; -; mRNA.
DR RefSeq; NP_001008974.1; NM_001008974.1.
DR AlphaFoldDB; O77562; -.
DR BMRB; O77562; -.
DR SMR; O77562; -.
DR STRING; 9598.ENSPTRP00000005519; -.
DR PaxDb; O77562; -.
DR GeneID; 373853; -.
DR CTD; 10522; -.
DR eggNOG; KOG4333; Eukaryota.
DR InParanoid; O77562; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048706; P:embryonic skeletal system development; ISS:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
DR GO; GO:0033599; P:regulation of mammary gland epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.10.390.10; -; 1.
DR InterPro; IPR010919; SAND-like_dom_sf.
DR InterPro; IPR000770; SAND_dom.
DR InterPro; IPR024119; TF_DEAF-1.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR10237; PTHR10237; 2.
DR Pfam; PF01342; SAND; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00258; SAND; 1.
DR SUPFAM; SSF63763; SSF63763; 1.
DR PROSITE; PS50864; SAND; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; DNA-binding; Metal-binding; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..565
FT /note="Deformed epidermal autoregulatory factor 1 homolog"
FT /id="PRO_0000074086"
FT DOMAIN 193..273
FT /note="SAND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00185"
FT ZN_FING 504..540
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 34..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..478
FT /note="Interaction with LMO4"
FT /evidence="ECO:0000250"
FT MOTIF 301..316
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT BINDING 504
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 507
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 515
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 518
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 524
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 528
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 536
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 540
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT MOD_RES 171
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1T5"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75398"
FT MOD_RES 179
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1T5"
FT MOD_RES 432
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75398"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88450"
SQ SEQUENCE 565 AA; 59341 MW; CDF864D85650F1A9 CRC64;
MEDSDSAAKQ LGLAEAAAVA AAAAVAAAAA AAAGGEAEEP VLSRDEDSEE DADSEAERET
PRVTAVAVMA AEPGHMDMGA EALPGPDETA AAAAFAEVTT VTVANVGAAA DNVFTTSVAN
AASISGHVLS GRTALQIGDS LNTEKATLIV VHTDGSIVET TGLKGPAAPL TPGPQSPPTP
LAPGQEKGGT KYNWDPSVYD SELPVRCRNI SGTLYKNRLG SGGRGRCIKQ GENWYSPTEF
EAMAGRASSK DWKRSIRYAG RPLQCLIQDG ILNPHAASCT CAACCDNMTL SGPVRLFVPY
KRRKKENELP TTPVKKDSPK NITLLPATAA TTFTVTPSGQ ITTSGALTFD RASTVEATAV
ISESPAQGDV FAGATVQEAS VQPPCRASHP EPHYPGYQDS CQIAPFPEAA LPTSHPKIVL
TSLPALAVPP PTPTKAAPPA LVNGLELSEP RSWLYLEEMV NSLLTTAQQL KTLFEQAKHA
STYREAAANQ AKIHADAERK EQSCVNCGRE AMNECTGCHK VNYCSTFCQR KDWKDHQHIC
GQSAAVTVQA DEVHVAESVM EKVTV
