MARH5_DANRE
ID MARH5_DANRE Reviewed; 289 AA.
AC Q6NYK8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
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, march5l; ORFNames=zgc:56713;
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].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) 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. {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 -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q9NX47}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NX47}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
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DR EMBL; BC066555; AAH66555.1; -; mRNA.
DR RefSeq; NP_956033.2; NM_199739.3.
DR AlphaFoldDB; Q6NYK8; -.
DR STRING; 7955.ENSDARP00000037207; -.
DR PaxDb; Q6NYK8; -.
DR Ensembl; ENSDART00000039187; ENSDARP00000037207; ENSDARG00000028559.
DR GeneID; 326067; -.
DR KEGG; dre:326067; -.
DR CTD; 326067; -.
DR ZFIN; ZDB-GENE-030131-4792; march5l.
DR eggNOG; KOG3053; Eukaryota.
DR GeneTree; ENSGT00390000009948; -.
DR HOGENOM; CLU_046472_1_0_1; -.
DR InParanoid; Q6NYK8; -.
DR OMA; HPCQCRG; -.
DR OrthoDB; 1210654at2759; -.
DR PhylomeDB; Q6NYK8; -.
DR TreeFam; TF316219; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6NYK8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 10.
DR Bgee; ENSDARG00000028559; Expressed in intestine and 26 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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 Endoplasmic reticulum; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..289
FT /note="E3 ubiquitin-protein ligase MARCHF5"
FT /id="PRO_0000271772"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 4..73
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
SQ SEQUENCE 289 AA; 32106 MW; CAD76606054A8336 CRC64;
MACVDEPPEK HCWVCFATEK EDRAAEWVSP CRCKGCTKWI HQSCLQRWLD EKQKGNSGGA
VSCPQCGTEY RIVFPKMGPV VYFLQQVDRA LSRASPFAAA GVVVGTVYWS AVTYGAVTVM
QVVGHKKGLD VMERADPLFL LMGLPTIPVM LVLGKMIRWE DYVVRLWQRH SAKLQIFSGL
VPGMGRALPR VPVEGSYGGD HLSVSRTLCG ALIFPSIANL VGRLLFRRVT SNLQRTILGG
IAFVVMKGVL KVYFKQQQYL IQANRHILNY PEPEGQADGA TEDEDSSNE
