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Database: UniProt
Entry: A0A7K6SIB7_CALNI
LinkDB: A0A7K6SIB7_CALNI
Original site: A0A7K6SIB7_CALNI 
ID   A0A7K6SIB7_CALNI        Unreviewed;       483 AA.
AC   A0A7K6SIB7;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   28-JAN-2026, entry version 20.
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   Name=Mdm2 {ECO:0000313|EMBL:NWW97638.1};
GN   ORFNames=CALNIC_R01323 {ECO:0000313|EMBL:NWW97638.1};
OS   Caloenas nicobarica (Nicobar pigeon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Columbimorphae; Columbiformes;
OC   Columbidae; Caloenas.
OX   NCBI_TaxID=187106 {ECO:0000313|EMBL:NWW97638.1, ECO:0000313|Proteomes:UP000546235};
RN   [1] {ECO:0000313|EMBL:NWW97638.1, ECO:0000313|Proteomes:UP000546235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OUT-0007 {ECO:0000313|EMBL:NWW97638.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:NWW97638.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-2019) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:NWW97638.1}.
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DR   EMBL; VZSB01000192; NWW97638.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7K6SIB7; -.
DR   Proteomes; UP000546235; 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:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0002039; F:p53 binding; IEA:TreeGrafter.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:TreeGrafter.
DR   CDD; cd17672; MDM2; 1.
DR   CDD; cd16783; mRING-HC-C2H2C4_MDM2; 1.
DR   FunFam; 1.10.245.10:FF:000002; E3 ubiquitin-protein ligase Mdm2; 1.
DR   FunFam; 3.30.40.10:FF:000076; E3 ubiquitin-protein ligase 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; Zn_ribbon_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   Ligase {ECO:0000313|EMBL:NWW97638.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000546235};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
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          22..105
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          338..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..154
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..401
FT                   /note="Low complexity"
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:NWW97638.1"
FT   NON_TER         483
FT                   /evidence="ECO:0000313|EMBL:NWW97638.1"
SQ   SEQUENCE   483 AA;  55045 MW;  7A4143D6292FB71F CRC64;
     MCNTKMSSLT DASSVTASEQ EALVKPKPLL LKLLKLAGAE KDTFTMKEVI FYLGQYIMSK
     QLYDEKQQHI VHCANDLLGD LFGVTSFSVK EHRRLYSMIS RNLIAINQQG STLADTPEDD
     ARFQLEEENV LKESMQELEE KQTSSNATSR PATSSRRRTH SESEENSSDD LHSDRRKRHK
     SDSISLTFDE SLSWCVVSGL CRERSNSSDS TDTFSIPDLD ASSLSENSDW FDHSSVSDQF
     SVEFEVESIY SEDYSHNEEG QELTDEDDEV YQLTIYQDED SDADSFDEDP EISLADYWKC
     PECSEMNPPL PRHCHRCWAL REDWLPDEKS DKLVKSKLES SFPVESEEGF DVPDCKKVKM
     TEDKEPAVEE NEDKAVQISE SQESEDYSQP STSSSMFFSS QEDYKEPEKR ELQDKEGSLE
     SSLPVTSIEP CVICQSRPKN GCIVHGKTGH LMSCFTCARK LKKRNKPCPV CRQPIQMIVL
     TYF
//
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