ID G5C4W5_HETGA Unreviewed; 352 AA.
AC G5C4W5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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|EMBL:JAN97456.1};
GN ORFNames=GW7_01842 {ECO:0000313|EMBL:EHB16576.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB16576.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB16576.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
RN [2] {ECO:0000313|EMBL:JAN97456.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Kidney {ECO:0000313|EMBL:JAN97456.1};
RA Bens M., Sahm A., Jahn N., Morhart M., Holtze S., Hildebrandt T.B.,
RA Platzer M., Szafranski K.;
RT "FRAMA: From RNA-seq data to annotated mRNA assemblies.";
RL Submitted (OCT-2015) 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: Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004374}.
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DR EMBL; JH173393; EHB16576.1; -; Genomic_DNA.
DR EMBL; GEBF01006176; JAN97456.1; -; Transcribed_RNA.
DR RefSeq; XP_004850520.1; XM_004850463.1.
DR RefSeq; XP_004850521.1; XM_004850464.1.
DR RefSeq; XP_004850523.1; XM_004850466.2.
DR RefSeq; XP_004850524.1; XM_004850467.2.
DR RefSeq; XP_004850525.1; XM_004850468.1.
DR RefSeq; XP_012929810.1; XM_013074356.1.
DR RefSeq; XP_012929811.1; XM_013074357.1.
DR AlphaFoldDB; G5C4W5; -.
DR STRING; 10181.G5C4W5; -.
DR Ensembl; ENSHGLT00000075353; ENSHGLP00000056650; ENSHGLG00000036585.
DR KEGG; hgl:101713474; -.
DR eggNOG; KOG1571; Eukaryota.
DR InParanoid; G5C4W5; -.
DR OrthoDB; 5475152at2759; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR Bgee; ENSHGLG00000016867; Expressed in heart and 10 other cell types or tissues.
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:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Ligase {ECO:0000313|EMBL:EHB16576.1};
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:UP000006813};
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; 39938 MW; 77CAEBA6E2B144AE CRC64;
MDSGGRPSLG QVILLGTSSV VTAILYSVYR QKAQVAQELK GAKKIHLGED LKNILSEAPG
KCVPYAVIEG AVRSVKETLN SQFVENCKGV IQRLTLQEHK MVWNRTTHLW NDYSKIIHQR
TNTVPFDLVP HEDGVDVAVR VLKPLESVNL GLETVYEKFH PSVQSFTDVI GHYISGERPK
GIQETEEMLK VGATLTGVGE LVLDNNSVRL QPPKQGMQYY LSSQDFDSLL QRQESSVKLW
KILALVFGFA TCATLFFILR RQYLQWQERL RLEQMQEEFR EREAQLLSQA SPEDRESLKS
ACVMCLSSFK SCVFLECGHV CSCHECYRAL PEPKKCPICR RKITRVVPLY NS
//
