ID A0A1U7QVD7_MESAU Unreviewed; 990 AA.
AC A0A1U7QVD7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=Rnf111 {ECO:0000313|RefSeq:XP_005075529.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005075529.1};
RN [1] {ECO:0000313|RefSeq:XP_005075529.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}.
CC -!- SIMILARITY: Belongs to the Arkadia family.
CC {ECO:0000256|ARBA:ARBA00007622}.
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DR RefSeq; XP_005075529.1; XM_005075472.3.
DR RefSeq; XP_012972896.1; XM_013117442.1.
DR AlphaFoldDB; A0A1U7QVD7; -.
DR STRING; 10036.ENSMAUP00000012511; -.
DR GeneID; 101832287; -.
DR KEGG; maua:101832287; -.
DR CTD; 54778; -.
DR eggNOG; KOG0800; Eukaryota.
DR OrthoDB; 5474929at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032184; F:SUMO polymer binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0007389; P:pattern specification process; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR CDD; cd16681; RING-H2_RNF111; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR029306; RNF111_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR16200:SF1; E3 UBIQUITIN-PROTEIN LIGASE PLR-1-RELATED; 1.
DR PANTHER; PTHR16200; RING ZINC FINGER; 1.
DR Pfam; PF15303; RNF111_N; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 938..979
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 63..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..521
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..739
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 990 AA; 107685 MW; 60B21CEC59AEA7C1 CRC64;
MSQWTPECNE IYTLKVAMKS GTPPDAPTTQ ESLKGVLLHP QPLGATKSFP AEVEMINGKV
GNEFSHLCDD SKQEKDMNGN QQEQEKSGVV RKKRKSQQAG PSYVQNCVKE NQGILGLRQH
LETPSDEEND SSFSECLSSP SSSLHFGDSD TVTSDEDKEV SVRHSQPVLS AKSRSHSSRS
QKWPRTEAES VSGLLMKRPC FHGGALRRLP CRKRLMKNSS SQRTQKQKER LLVQRKKREV
LAQRKYALLP SSSSSSENDL SSDSSSSSST DGEEDLCASA SENPSNPAAP SGSIDEDVVV
IEASFTPQVT ANEEINVTST DSEVEIVTVG ESYRSRSTLG HSRSHWSQGS SSHTGRPQEP
RNRSRISTVI QPLRQNAAEV VDLTVDEDEP TVVPTTSARM ESQTPSASIS NSNPSTSEQA
SDATSAVASS QPSTASETAA TLTSNSAAGS SVGDDSRRTA SSAVPETGPP AMPRLPSCCP
QHSPCGGTSQ SHHALAHPHS SCFQQHGHHF QHHHHHHHTP HPAVPVSPSF SDPACPVERP
PQVQAPCGAN SSSGSSYHDQ QALPVDLSSS ALRTHGSGSF HGASAFDPCC PVSSSRAAVF
GHQAAAAPTQ PLAIDGYGSS MVAQPQPQPP PQPSLSSCRH YMPPPYASLT RTLHHQASGC
PHSHGNAPPQ TQPPPQVDYV IPHPVHAFHS QITSHAASHP VAPPPPTHLG STAAPIPQHL
PPAHQPISHH IPAPAPPAQR LHPHEVMQRM EVQRRRMMQH PTRAHERPPP HPHRMHPNYG
HGHHIHVPQT MSSHPRQAPE RTAWELGIEA GVTAATYTPG ALHPHLAHYH APPRLHHLQL
GALPLMVPDM AGYPHIRYIS SGLDGTSFRG PFRGNFEELI HLEERLGNVN RGASQGTIER
CTYPHKYKKV TTDWFSQRKL HCKQDGEEGT EEDTEEKCTI CLSILEEGED VRRLPCMHLF
HQVCVDQWLI TNKKCPICRV DIEAQLPSES
//
