MDM4_DANRE
ID MDM4_DANRE Reviewed; 496 AA.
AC Q7ZUW7; Q4V944;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Protein Mdm4;
DE AltName: Full=Double minute 4 protein;
DE AltName: Full=Mdm2-like p53-binding protein;
DE AltName: Full=Protein Mdmx;
DE AltName: Full=p53-binding protein Mdm4;
GN Name=mdm4; Synonyms=mdmx;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 15-140 IN COMPLEX WITH P53.
RX PubMed=17938582; DOI=10.4161/cc.6.19.4740;
RA Popowicz G.M., Czarna A., Rothweiler U., Szwagierczak A., Krajewski M.,
RA Weber L., Holak T.A.;
RT "Molecular basis for the inhibition of p53 by Mdmx.";
RL Cell Cycle 6:2386-2392(2007).
CC -!- FUNCTION: Inhibits p53- and p73-mediated cell cycle arrest and
CC apoptosis by binding its transcriptional activation domain.
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds to p73 (By similarity). Interacts directly with p53.
CC {ECO:0000250, ECO:0000269|PubMed:17938582}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7ZUW7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7ZUW7-2; Sequence=VSP_033237;
CC -!- SIMILARITY: Belongs to the MDM2/MDM4 family. {ECO:0000305}.
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DR EMBL; BC047801; AAH47801.1; -; mRNA.
DR EMBL; BC097069; AAH97069.1; -; mRNA.
DR PDB; 2Z5S; X-ray; 2.30 A; M/N/O=15-140.
DR PDB; 2Z5T; X-ray; 2.30 A; M/N/O=15-140.
DR PDB; 3DAC; X-ray; 1.80 A; A/M=15-129.
DR PDB; 4N5T; X-ray; 1.70 A; A=17-106.
DR PDB; 6V4E; X-ray; 1.62 A; A/B=15-106.
DR PDB; 6V4F; X-ray; 1.35 A; A=15-106.
DR PDB; 6V4G; X-ray; 1.25 A; A=15-106.
DR PDB; 6V4H; X-ray; 1.53 A; A/C=15-106.
DR PDBsum; 2Z5S; -.
DR PDBsum; 2Z5T; -.
DR PDBsum; 3DAC; -.
DR PDBsum; 4N5T; -.
DR PDBsum; 6V4E; -.
DR PDBsum; 6V4F; -.
DR PDBsum; 6V4G; -.
DR PDBsum; 6V4H; -.
DR AlphaFoldDB; Q7ZUW7; -.
DR SMR; Q7ZUW7; -.
DR BioGRID; 85461; 1.
DR STRING; 7955.ENSDARP00000074651; -.
DR PaxDb; Q7ZUW7; -.
DR ZFIN; ZDB-GENE-030131-6872; mdm4.
DR eggNOG; ENOG502QQNV; Eukaryota.
DR InParanoid; Q7ZUW7; -.
DR PhylomeDB; Q7ZUW7; -.
DR Reactome; R-DRE-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DRE-2559585; Oncogene Induced Senescence.
DR Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR Reactome; R-DRE-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DRE-6804757; Regulation of TP53 Degradation.
DR Reactome; R-DRE-69541; Stabilization of p53.
DR EvolutionaryTrace; Q7ZUW7; -.
DR PRO; PR:Q7ZUW7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.245.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR IDEAL; IID50094; -.
DR InterPro; IPR015458; MDM4.
DR InterPro; IPR016495; p53_neg-reg_MDM_2/4.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13844:SF20; PTHR13844:SF20; 1.
DR Pfam; PF02201; SWIB; 1.
DR PIRSF; PIRSF500699; MDM4; 1.
DR PIRSF; PIRSF006748; p53_MDM_2/4; 1.
DR SUPFAM; SSF47592; SSF47592; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..496
FT /note="Protein Mdm4"
FT /id="PRO_0000331517"
FT DOMAIN 22..105
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT ZN_FING 305..334
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 443..484
FT /note="RING-type; degenerate"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 448..451
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 220..224
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_033237"
FT CONFLICT 254
FT /note="I -> M (in Ref. 1; AAH47801)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="E -> G (in Ref. 1; AAH47801)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="L -> P (in Ref. 1; AAH47801)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="F -> L (in Ref. 1; AAH47801)"
FT /evidence="ECO:0000305"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:6V4G"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:6V4G"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:4N5T"
FT HELIX 46..60
FT /evidence="ECO:0007829|PDB:6V4G"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6V4G"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6V4G"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:6V4G"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:6V4G"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:6V4G"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6V4G"
SQ SEQUENCE 496 AA; 55241 MW; BACE83EDE11112B5 CRC64;
MTSLASSSQL PGSCRTLPGE GTQVHPRAPL LQILKVAGAQ EEVFTLKEVM HYLGQYIMMK
QLYDKQRQHI VHCHDDPLGE LLEVGSFSVK NPSPVYEMLK RNLVILNNSD AAKNLSVGKD
SNESPSEDPG QVSSGSINSA QPLIAGSSST GTTQSCSQRR PRDPDEDSSD GLPRSACKRP
KLDVTLEEWD LSGLPWWFLG NLRSNYTRRS NGSTDIHTNQ LSPGQDEDTA IVSDTTDDLW
FLNEAESEQV SVEIKEAVLE QGSDGESPHE DEDTGKDSKD DGKMQEEQEE DSQCLSDDTD
TEISTQDAWQ CSECRKFNTP LQRYCMRCWA LRKDWYKDCP RLVHSISVPD IPACSSRPER
DEDEEEEDDD GIDMPDCLRT VSDPVVLPSH RVSRNIPSSS ASSSKGKGPS QIHHHFQETS
EGDSQDTLDM ETEYQPEALL EPCKLCRVRP RNGNIIHGRT AHLITCFPCA RKLHKFHAPC
PGCGQVIQKV IKTFIA
