ID A0A0A0APS3_CHAVO Unreviewed; 483 AA.
AC A0A0A0APS3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=E3 ubiquitin-protein ligase Mdm2 {ECO:0000256|ARBA:ARBA00018786};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Double minute 2 protein {ECO:0000256|ARBA:ARBA00032811};
DE AltName: Full=RING-type E3 ubiquitin transferase Mdm2 {ECO:0000256|ARBA:ARBA00032614};
DE AltName: Full=p53-binding protein Mdm2 {ECO:0000256|ARBA:ARBA00030148};
DE Flags: Fragment;
GN ORFNames=N301_01485 {ECO:0000313|EMBL:KGL95563.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL95563.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL95563.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL95563.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}. Nucleus,
CC nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
CC -!- SIMILARITY: Belongs to the MDM2/MDM4 family.
CC {ECO:0000256|ARBA:ARBA00005803}.
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DR EMBL; KL872441; KGL95563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0APS3; -.
DR STRING; 50402.A0A0A0APS3; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR CDD; cd17672; MDM2; 1.
DR CDD; cd16783; mRING-HC-C2H2C4_MDM2; 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; IPR028340; Mdm2.
DR InterPro; IPR044080; MDM2_mRING-HC-C2H2C4.
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; PTHR46858:SF13; E3 UBIQUITIN-PROTEIN LIGASE MDM2; 1.
DR PANTHER; PTHR46858; OS05G0521000 PROTEIN; 1.
DR Pfam; PF02201; SWIB; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR PIRSF; PIRSF500700; MDM2; 1.
DR PIRSF; PIRSF006748; p53_MDM_2/4; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF47592; SWIB/MDM2 domain; 2.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00322}.
FT DOMAIN 25..108
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT DOMAIN 294..323
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 431..472
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 135..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL95563.1"
FT NON_TER 483
FT /evidence="ECO:0000313|EMBL:KGL95563.1"
SQ SEQUENCE 483 AA; 55268 MW; DAD7B9643065FE10 CRC64;
CRQMCNTKMS SLTDASSVTA SEQEALVKPK PLLLKLLKLA GAEKDTFTMK EVIFYLGQYI
MSKQLYDEKQ QHIVHCANDL LGDLFGVTSF SVKEHRRLYS MISRNLIAIN QQDSAPPEDD
ARFHLEEENV IKESMQELEE KQTSSNVTSR PTTSSRRRTH SESEENSSDD LHSDRRKRHK
SDSISLTFDE SLSWCVVSGL CRERSNSSDS TDSLSIPDLD ASSLSENSDW FDHSSVSDQF
SVEFEVESIY SEDYSHNEEG QELTDEDDEV YQLTIYQDED SDADSFDEDP EISLADYWKC
PECSEMNPPL PRHCHRCWAL REDWLPDEKS DKLEKSKSET SFPLESEEGF DVPDCKKVKI
TEDKEPAMEE NEDKAVQISE SQESEDYSQP STSSSMFCSS QEDYKEPEKR EMQDKEESLE
SSLPVTSIEP CVICQSRPKN GCIVHGKTGH LMSCFTCARK LKKRNKPCPV CRQPIQMIVL
TYF
//
