MARH5_CHICK
ID MARH5_CHICK Reviewed; 281 AA.
AC Q5ZJ41;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
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; ORFNames=RCJMB04_20o22;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720593; CAG32252.1; -; mRNA.
DR RefSeq; NP_001012924.1; NM_001012906.1.
DR AlphaFoldDB; Q5ZJ41; -.
DR SMR; Q5ZJ41; -.
DR STRING; 9031.ENSGALP00000011138; -.
DR PaxDb; Q5ZJ41; -.
DR PRIDE; Q5ZJ41; -.
DR GeneID; 423815; -.
DR KEGG; gga:423815; -.
DR CTD; 561952; -.
DR VEuPathDB; HostDB:geneid_423815; -.
DR eggNOG; KOG3053; Eukaryota.
DR HOGENOM; CLU_046472_1_1_1; -.
DR InParanoid; Q5ZJ41; -.
DR OrthoDB; 1210654at2759; -.
DR PhylomeDB; Q5ZJ41; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5ZJ41; -.
DR Proteomes; UP000000539; Unplaced.
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..281
FT /note="E3 ubiquitin-protein ligase MARCHF5"
FT /id="PRO_0000271771"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 9..78
FT /note="RING-CH-type"
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 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
SQ SEQUENCE 281 AA; 31422 MW; 4A02FF4488FCD013 CRC64;
MSEQTGLALP QTMDRSCWVC FATDEDDRTA EWVRPCRCRG STKWVHQTCL QRWVDEKQRG
NSTARVACPQ CNAEYLIVFP KLGPVVYVLD LADRLISKAC PFAAAGIMVG SIYWTAVTYG
AVTVMQVVGH KEGLDVMERA DPLFLLIGLP TIPVMLILGK MIRWEDYVLR LWRKYSNKLQ
ILNSIFPGIG CPVPRIPAEA NPLADHVSAT RILCGALVFP TIATIVGKLM FSSVNSNLQR
TILGGIAFVA IKGAFKVYFK QQQYLRQAHR KILNYPEQEG A
