MARH5_BOVIN
ID MARH5_BOVIN Reviewed; 278 AA.
AC Q3ZC24;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=E3 ubiquitin-protein ligase MARCHF5;
DE EC=2.3.2.27;
DE AltName: Full=Membrane-associated RING finger protein 5;
DE AltName: Full=Membrane-associated RING-CH protein V;
DE Short=MARCH-V;
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF5 {ECO:0000305};
GN Name=MARCHF5; Synonyms=MARCH5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mitochondrial E3 ubiquitin-protein ligase that plays a
CC crucial role in the control of mitochondrial morphology by acting as a
CC positive regulator of mitochondrial fission. May play a role in the
CC prevention of cell senescence acting as a regulator of mitochondrial
CC quality control. Promotes ubiquitination of FIS1, DNM1L and MFN1.
CC {ECO:0000250|UniProtKB:Q9NX47}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Monomer and homodimer. Interacts with MFN1, MFN2, DNM1L and
CC FIS1. {ECO:0000250|UniProtKB:Q9NX47}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q9NX47}; Multi-pass membrane protein
CC {ECO:0000250}.
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
CC -!- PTM: Autoubiquitinated leading to degradation (short half-life).
CC {ECO:0000250|UniProtKB:Q9NX47}.
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DR EMBL; BC102966; AAI02967.1; -; mRNA.
DR RefSeq; NP_001029887.1; NM_001034715.1.
DR AlphaFoldDB; Q3ZC24; -.
DR STRING; 9913.ENSBTAP00000027942; -.
DR PaxDb; Q3ZC24; -.
DR Ensembl; ENSBTAT00000027942; ENSBTAP00000027942; ENSBTAG00000020981.
DR GeneID; 540937; -.
DR KEGG; bta:540937; -.
DR CTD; 54708; -.
DR VEuPathDB; HostDB:ENSBTAG00000020981; -.
DR VGNC; VGNC:31240; MARCHF5.
DR eggNOG; KOG3053; Eukaryota.
DR GeneTree; ENSGT00390000009948; -.
DR HOGENOM; CLU_046472_1_1_1; -.
DR InParanoid; Q3ZC24; -.
DR OMA; KRYCWVC; -.
DR OrthoDB; 1210654at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000020981; Expressed in semitendinosus and 105 other tissues.
DR ExpressionAtlas; Q3ZC24; baseline.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0090140; P:regulation of mitochondrial fission; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS51292; ZF_RING_CH; 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; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..278
FT /note="E3 ubiquitin-protein ligase MARCHF5"
FT /id="PRO_0000271767"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 6..75
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
SQ SEQUENCE 278 AA; 31232 MW; CB00A408E228A9EE CRC64;
MPDQALQQML DRSCWVCFAT DEDDRTAEWV RPCRCRGSTK WVHQACLQRW VDEKQRGNST
ARVACPQCNA EYLIVFPKLG PVVYVLDLAD RLISKACPFA AAGIMVGSIY WTAVTYGAVT
VMQVVGHKEG LDVMERADPL FLLIGLPTIP VMLILGKMIR WEDYVLRLWR KYSNKLQILN
SIFPGIGCPV PRIPAEANPL ADHVSATRIL CGALVFPTIA TIVGKLMFSS VNSNLQRTIL
GGIAFVAIKG AFKVYFKQQQ YLRQAHRKIL NYPEQEEA
