ID   MUL1_XENLA              Reviewed;         353 AA.
AC   Q6NTT6;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Mitochondrial ubiquitin ligase activator of nfkb 1;
DE            EC=2.3.2.27;
DE   AltName: Full=E3 ubiquitin-protein ligase mul1;
DE   AltName: Full=RING-type E3 ubiquitin transferase nfkb 1 {ECO:0000305};
GN   Name=mul1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that plays a role in the control
CC       of mitochondrial morphology. Promotes mitochondrial fragmentation and
CC       influences mitochondrial localization. Inhibits cell growth. E3
CC       ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating
CC       enzyme in the form of a thioester and then directly transfer the
CC       ubiquitin to targeted substrates. {ECO:0000250|UniProtKB:Q969V5}.
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:0000250|UniProtKB:Q969V5};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q969V5}.
CC   -!- SUBUNIT: Homooligomer. {ECO:0000250|UniProtKB:Q969V5}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:Q969V5}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DOMAIN: The zinc finger domain is required for E3 ligase activity.
CC       {ECO:0000250|UniProtKB:Q969V5}.
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DR   EMBL; BC068869; AAH68869.1; -; mRNA.
DR   RefSeq; NP_001084716.1; NM_001091247.1.
DR   AlphaFoldDB; Q6NTT6; -.
DR   SMR; Q6NTT6; -.
DR   PRIDE; Q6NTT6; -.
DR   DNASU; 414680; -.
DR   GeneID; 414680; -.
DR   KEGG; xla:414680; -.
DR   CTD; 414680; -.
DR   Xenbase; XB-GENE-5884896; mul1.L.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 414680; Expressed in intestine and 20 other tissues.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR   GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR   GO; GO:0051646; P:mitochondrion localization; ISS:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR022170; MUL1-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF12483; GIDE; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..353
FT                   /note="Mitochondrial ubiquitin ligase activator of nfkb 1"
FT                   /id="PRO_0000277664"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..239
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..353
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         303..341
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   353 AA;  40359 MW;  102A3C761CDD7EFA CRC64;
     MENGGRPSVG QVILLTTSSA ITALFYSIYR HKYRSVQTLK EAKKFCLTDD LPAVLSDLPG
     KCVPYAVIEG AVTSVKEVLN SQYVENCKGV IQRLSLKEHK MVWNRTTHLW NDHEKIIHQR
     SNTVPFDLAP ENPGESGVSV RVLRPLEAVD LGLETIYEKF HPAVQSFSNI LGHYMTGERP
     KGVQETEEML KIGATITGVG ELVLDNKTIK LQPPKDGMLF YLSSMDYEGL LEKQEVQMRW
     WRILSIVFGV ASCITLFFIL RRKYRHYKEK QHLKNLQREF EESRARQRVQ QEPQNKEEVQ
     NPCSICLSTE KSCVFLECGH VCSCISCYQA LPSPKKCPIC RNFIDRIVPL YNS