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Database: UniProt
Entry: H0X8E4_OTOGA
LinkDB: H0X8E4_OTOGA
Original site: H0X8E4_OTOGA 
ID   H0X8E4_OTOGA            Unreviewed;       352 AA.
AC   H0X8E4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=MUL1 {ECO:0000313|Ensembl:ENSOGAP00000011754.2};
OS   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000011754.2, ECO:0000313|Proteomes:UP000005225};
RN   [1] {ECO:0000313|Proteomes:UP000005225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA   Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA   Walker B.J., Sharpe T., Hall G.;
RT   "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSOGAP00000011754.2}
RP   IDENTIFICATION.
RG   Ensembl;
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   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004374}.
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DR   EMBL; AAQR03020734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003783880.1; XM_003783832.2.
DR   AlphaFoldDB; H0X8E4; -.
DR   STRING; 30611.ENSOGAP00000011754; -.
DR   Ensembl; ENSOGAT00000013122.2; ENSOGAP00000011754.2; ENSOGAG00000013119.2.
DR   GeneID; 100956030; -.
DR   KEGG; oga:100956030; -.
DR   CTD; 79594; -.
DR   eggNOG; KOG1571; Eukaryota.
DR   GeneTree; ENSGT00390000012141; -.
DR   HOGENOM; CLU_050604_1_0_1; -.
DR   InParanoid; H0X8E4; -.
DR   OMA; YILWKQY; -.
DR   OrthoDB; 5475152at2759; -.
DR   TreeFam; TF325195; -.
DR   Proteomes; UP000005225; Unassembled WGS sequence.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005777; C:peroxisome; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR   GO; GO:0019789; F:SUMO transferase activity; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0071360; P:cellular response to exogenous dsRNA; IEA:Ensembl.
DR   GO; GO:0000266; P:mitochondrial fission; IEA:Ensembl.
DR   GO; GO:0051646; P:mitochondrion localization; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0071650; P:negative regulation of chemokine (C-C motif) ligand 5 production; IEA:Ensembl.
DR   GO; GO:0050689; P:negative regulation of defense response to virus by host; IEA:Ensembl.
DR   GO; GO:0010637; P:negative regulation of mitochondrial fusion; IEA:Ensembl.
DR   GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:1904925; P:positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization; IEA:Ensembl.
DR   GO; GO:1903861; P:positive regulation of dendrite extension; IEA:Ensembl.
DR   GO; GO:0090141; P:positive regulation of mitochondrial fission; IEA:Ensembl.
DR   GO; GO:0033235; P:positive regulation of protein sumoylation; IEA:Ensembl.
DR   GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
DR   GO; GO:1901028; P:regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IEA:Ensembl.
DR   CDD; cd16648; mRING-HC-C3HC5_MAPL; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR022170; MUL1-like.
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:SF4; MITOCHONDRIAL UBIQUITIN LIGASE ACTIVATOR OF NFKB 1; 1.
DR   Pfam; PF12483; GIDE; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
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:PRU00175}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          302..340
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   352 AA;  39687 MW;  54275D6AF191184B CRC64;
     MESGGRPSLG QFILLGTSSV VTAFLYSVYR QKAQVAQELK GAKKIHLGDD LKSILSEAPG
     KCVPYAVIEG AVRSVKETLN SQFVENCKGV IQRLTLQEHK IVWNRTTHLW NDCSKIIHQR
     TNTVPFDLVP HEDGVAVAVR VLKPLDSVDL GLETVYEKFH PSIQSFTDVI GHYISGERPK
     GIQETEEMLK VGATLTGVGE LVLDNNSVRL QPPKQGMQYY LSSQDFDSLL QKQEASVRLW
     KVLALVFGFT ACATLFFILR KQYLQRQERL RLKQMQEEFL EHEAQLLRQA KPEDRESLKS
     ACVVCLSSFK SCVFLECGHV CSCSECYHAL PEPKRCPICR QAITRVIPLY NS
//
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