ID   MUL1A_DANRE             Reviewed;         341 AA.
AC   Q5M7X9;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Mitochondrial ubiquitin ligase activator of nfkb 1-A;
DE            EC=2.3.2.27;
DE   AltName: Full=E3 ubiquitin-protein ligase mul1-A;
DE   AltName: Full=RING-type E3 ubiquitin transferase nfkb 1-A {ECO:0000305};
GN   Name=mul1a; Synonyms=mul1; ORFNames=zgc:92166;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-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; BC088385; AAH88385.1; -; mRNA.
DR   RefSeq; NP_001018134.1; NM_001018124.1.
DR   AlphaFoldDB; Q5M7X9; -.
DR   SMR; Q5M7X9; -.
DR   STRING; 7955.ENSDARP00000018598; -.
DR   PaxDb; Q5M7X9; -.
DR   Ensembl; ENSDART00000018818; ENSDARP00000018598; ENSDARG00000021398.
DR   GeneID; 553180; -.
DR   KEGG; dre:553180; -.
DR   CTD; 553180; -.
DR   ZFIN; ZDB-GENE-050102-5; mul1a.
DR   eggNOG; KOG1571; Eukaryota.
DR   GeneTree; ENSGT00390000012141; -.
DR   HOGENOM; CLU_050604_1_0_1; -.
DR   InParanoid; Q5M7X9; -.
DR   OMA; WTDSERV; -.
DR   OrthoDB; 926101at2759; -.
DR   PhylomeDB; Q5M7X9; -.
DR   TreeFam; TF325195; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q5M7X9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 2.
DR   Bgee; ENSDARG00000021398; Expressed in muscle tissue 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:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
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   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..341
FT                   /note="Mitochondrial ubiquitin ligase activator of nfkb 1-
FT                   A"
FT                   /id="PRO_0000277663"
FT   TOPO_DOM        1..5
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..233
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..341
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         292..329
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   341 AA;  38585 MW;  4B07666981CF2D70 CRC64;
     MEDFPVLEMV CLGSSVALSG LFYYIYRKKR KTVDKLKEAP VMALDAKLID LLNATPGKCL
     QYVVVEGTVQ PVGEPLRSQF QESSVGVIQK LVLREHKLVW NSLGRIWTDS ERVLLQRVNA
     VPFNLLGLNK SFVRVLCPLE ATGPKMEIVH EKFHQATYGF TDLIGQYLSG EKPKGQLETE
     EMLKVGASLT VVGELILDTD RLLKIRPPTD GSEYFLSSAD FETLLMEQEG QAEVWRVFAC
     ICALAGVAVL IWTGRRYYRQ LKLRWEQENL RREFEGMGTG EREEDNGVEN ACVICLSNPR
     GCVLLDCGHV CCCFRCYQAL PQPFCPICRQ HIKRVVPLYQ A