ID G1P8J9_MYOLU Unreviewed; 492 AA.
AC G1P8J9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Protein Mdm4 {ECO:0000256|PIRNR:PIRNR006748};
GN Name=MDM4 {ECO:0000313|Ensembl:ENSMLUP00000006508.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000006508.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000006508.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000006508.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Inhibits p53- and p73-mediated cell cycle arrest and
CC apoptosis by binding its transcriptional activation domain.
CC {ECO:0000256|PIRNR:PIRNR006748}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR006748}.
CC -!- SIMILARITY: Belongs to the MDM2/MDM4 family.
CC {ECO:0000256|ARBA:ARBA00005803, ECO:0000256|PIRNR:PIRNR006748}.
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DR EMBL; AAPE02029506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1P8J9; -.
DR STRING; 59463.ENSMLUP00000006508; -.
DR Ensembl; ENSMLUT00000007131.2; ENSMLUP00000006508.2; ENSMLUG00000007129.2.
DR eggNOG; ENOG502QQNV; Eukaryota.
DR GeneTree; ENSGT00530000063539; -.
DR HOGENOM; CLU_043544_2_0_1; -.
DR InParanoid; G1P8J9; -.
DR OMA; IPDCRRT; -.
DR TreeFam; TF105306; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0017053; C:transcription repressor complex; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR CDD; cd17673; MDM4; 1.
DR CDD; cd16784; mRING-HC-C2H2C4_MDM4; 1.
DR Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12183; MITOCHONDRIAL UBIQUITIN LIGASE ACTIVATOR OF NFKB 1; 1.
DR PANTHER; PTHR12183:SF37; PROTEIN MDM4; 1.
DR Pfam; PF02201; SWIB; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR PIRSF; PIRSF500699; MDM4; 1.
DR PIRSF; PIRSF006748; p53_MDM_2/4; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR006748}; Nucleus {ECO:0000256|PIRNR:PIRNR006748};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006748};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00322}.
FT DOMAIN 26..109
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT DOMAIN 301..330
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 439..480
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 54706 MW; 4A435B74E76DEC7C CRC64;
MASLSTSAQC STTDSACRSS PRQIKQQVRP KPPLLKILQA AGAQGEIFTV TQVMHFLGQY
ITMKQLYDPR EQHMVYCSGD LLGELLGCQS FSVKDPSPLY AMLRKNLVAL TIAAADAAQT
LAIAQDQNLD IPSQDHLKQS AEESPSSRKS TEEGNIPTLP TSQNKCTHSR EEINLLKHTS
VDETSRLDLG LEEWDVAGWP WWFLGNLRNS YTPRSNGSTD LQTNQDIGTV IVSDTTDDVC
FLNESVSEQF GAGIKVEAAD IEQTSEEVGK VRDKMVIEVG TSDDLEDSKS ICDDTDVEVA
SEDEWQCTEC KKFNSPSKRY CFRCWALRKD WYSDCSKLTH SLSTSDITAI PEEKENEGID
IPDCRRTISA PVVIPKDTYK KEENPKLLDP CNSVEFLDLA HSSESQETVS SMGEQSANLF
QQRTVTGSTE DCRNLLKPCS VCEKRPRDGN IIHGRTSHLV TCFQCARRLK KTGASCPACK
KEIHLVIRVF IA
//
