ID A0A091I976_CALAN Unreviewed; 472 AA.
AC A0A091I976;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Protein Mdm4 {ECO:0000256|PIRNR:PIRNR006748};
GN ORFNames=N300_03725 {ECO:0000313|EMBL:KFP05184.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP05184.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP05184.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP05184.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL218440; KFP05184.1; -; Genomic_DNA.
DR RefSeq; XP_008497629.1; XM_008499407.1.
DR AlphaFoldDB; A0A091I976; -.
DR STRING; 9244.A0A091I976; -.
DR OrthoDB; 2916169at2759; -.
DR Proteomes; UP000054308; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
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; 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; 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.
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:UP000054308};
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 24..107
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT DOMAIN 289..318
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 53171 MW; 99179D6BF4DB4D6B CRC64;
MTSSNSAQHP AAENASRMTL GQVNQVRPKL PLLKILQAAG AQGETFTLKE VMHYLGQYIM
VRQLYDKREQ HMVYCGGDEL GELLGLESFS VKDPSPVYDM LKRNLTSAAM ADAAQNLAQE
QSVDKPSRDQ LKVSQQEGSD TGIIEGESNA PALSTSEQKC ENYEDKDLIE NLSKSKKPKL
DLVFEEWDVA GLPWWFLGNL RSNYKSRSNG STDIQTNQDI DTAVVSDTTD DLWFLNECPA
DQSEAAGKVE TVDCEEVKEG DKKVTEDTCL HDWEDSQCLS DGTDTEATSE GCWQCTKCKK
YNSPGKRYCY RCWALRKDWY SDCPKLPHSL SLSNIDAMQK KNDDEGIDVP DCRRTISAPV
CQPKDLFMVE NKSCVDPCSS IESLDLARES KEALLHFPEH KKEEEIQSLE SIKKLLSPCF
LCHHRPRDGN IVHGRTAHLV ACFRCAKMLK KKRSPCPVCR KEIEMVIRIF MG
//
