DEAF1_RAT
ID DEAF1_RAT Reviewed; 565 AA.
AC O88450; Q62998;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Deformed epidermal autoregulatory factor 1 homolog;
DE AltName: Full=Nuclear DEAF-1-related transcriptional regulator;
DE Short=NUDR;
DE AltName: Full=Suppressin;
GN Name=Deaf1; Synonyms=Spn;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Sprague-Dawley; TISSUE=Pituitary;
RX PubMed=9417089; DOI=10.1074/jbc.273.1.361;
RA LeBoeuf R.D., Ban E.M.H., Green M.M., Stone A.S., Propst S.M.,
RA Blalock J.E., Tauber J.D.;
RT "Molecular cloning, sequence analysis, expression, and tissue distribution
RT of suppressin, a novel suppressor of cell cycle entry.";
RL J. Biol. Chem. 273:361-368(1998).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443 AND SER-448, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. When secreted, behaves as
CC an inhibitor of cell proliferation, by arresting cells in the G0 or G1
CC phase. Regulates epithelial cell proliferation and side-branching in
CC the mammary gland. Required for neural tube closure and skeletal
CC patterning. Controls the expression of peripheral tissue antigens in
CC pancreatic lymph nodes. Transcriptional activator of EIF4G3. May also
CC involved in behavior (By similarity). {ECO:0000250|UniProtKB:O75398,
CC ECO:0000250|UniProtKB:Q9Z1T5}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with LMO4; LMO4 blocks
CC export from nucleus. Interacts with LMO2 and CLIM2. May interact with
CC the corepressors NCOR1 and NCRO2. Identified in a complex with XRCC5
CC and XRCC6. Interacts (via the SAND domain) with the DNA-PK complex
CC subunit XRCC6; the interaction is direct and may be inhibited by DNA-
CC binding (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Secreted. Note=Secreted in some cell
CC types.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O88450-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88450-2; Sequence=VSP_005969;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in brain, spleen, adrenal,
CC lung, skeletal muscle, liver, kidney, and in developing germ cells in
CC testis. In pituitary, restricted to hormone-secreting cell types.
CC -!- PTM: May be phosphorylated by DNA-PK complex in a DNA independent
CC manner (in vitro). {ECO:0000250}.
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DR EMBL; AF055884; AAC79679.1; -; mRNA.
DR EMBL; U59659; AAC35994.1; -; mRNA.
DR AlphaFoldDB; O88450; -.
DR BMRB; O88450; -.
DR SMR; O88450; -.
DR IntAct; O88450; 1.
DR STRING; 10116.ENSRNOP00000046656; -.
DR iPTMnet; O88450; -.
DR PhosphoSitePlus; O88450; -.
DR PaxDb; O88450; -.
DR UCSC; RGD:620671; rat. [O88450-1]
DR RGD; 620671; Deaf1.
DR eggNOG; KOG4333; Eukaryota.
DR InParanoid; O88450; -.
DR PhylomeDB; O88450; -.
DR PRO; PR:O88450; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0001662; P:behavioral fear response; ISO:RGD.
DR GO; GO:0048706; P:embryonic skeletal system development; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
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 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; DNA-binding; Metal-binding;
KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Secreted;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..565
FT /note="Deformed epidermal autoregulatory factor 1 homolog"
FT /id="PRO_0000074087"
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 29..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..189
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 COMPBIAS 40..54
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007744|PubMed:22673903"
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 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9417089"
FT /id="VSP_005969"
FT CONFLICT 151
FT /note="V -> D (in Ref. 2; AAC35994)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="A -> T (in Ref. 2; AAC35994)"
FT /evidence="ECO:0000305"
FT CONFLICT 297..298
FT /note="FV -> LL (in Ref. 2; AAC35994)"
FT /evidence="ECO:0000305"
FT CONFLICT 308..313
FT /note="ELPTTP -> VSCPRL (in Ref. 2; AAC35994)"
FT /evidence="ECO:0000305"
FT CONFLICT 338..349
FT /note="SGQITTSGALTF -> FRTDHYLWSTNL (in Ref. 2; AAC35994)"
FT /evidence="ECO:0000305"
FT CONFLICT 384..386
FT /note="PCR -> LQ (in Ref. 2; AAC35994)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="V -> A (in Ref. 2; AAC35994)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="G -> R (in Ref. 2; AAC35994)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="D -> V (in Ref. 2; AAC35994)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 565 AA; 59532 MW; D9C730E80A3F8492 CRC64;
MEDSDSAAKQ LGLAEAAAVA AAAAVAAAAA AAAESEAEEP VLSRDEDSEE DADSEAERET
RRVTAVAVMA AESGHMDMGT EALPSPDEAA AAAAFAEVTT VTVANVGSSA DNVFTTSVAN
AASISGHVLS GRTALQIGDS LNTEKATLIV VHTDGSIVET TGLKGPAAPL TPGPQSPPTP
LAPGQEKGGT KYNWDPSVYD SELPVRCRNI SGTLYKSRLG SGGRGRCIKQ GENWYSPTEF
EAMAGRASSK DWKRSIRYAG RPLQCLIQDG ILNPHAASCT CAACCDDMTL SGPVRLFVPY
KRRKKENELP TTPVKKDSPK NITLLPATAA TTFTVTPSGQ ITTSGALTFD RASTVEATAV
ISESPAQGDV FAGATVQEAG VQPPCRVGHP EPHYPGYQDS CQIAPFPEAA LPTSHPKIVL
TSLPALAVPP STPTKAVSPT VVSGLEMSEH RSWLYLEEMV NSLLNTAQQL KTLFEQAKQA
SSCREAAVTQ ARMQVDAERK EQSCVNCGRE AMSECTGCHK VNYCSTFCQR KDWKDHQHVC
GQSASVTVQA DDVHVEESVI EKVAV
