ID A0A2U9CHM7_SCOMX Unreviewed; 281 AA.
AC A0A2U9CHM7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=E3 ubiquitin-protein ligase MARCHF5 {ECO:0000256|ARBA:ARBA00040151};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Membrane-associated RING finger protein 5 {ECO:0000256|ARBA:ARBA00043185};
DE AltName: Full=Membrane-associated RING-CH protein V {ECO:0000256|ARBA:ARBA00043044};
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF5 {ECO:0000256|ARBA:ARBA00043231};
GN ORFNames=SMAX5B_008693 {ECO:0000313|EMBL:AWP14372.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP14372.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP14372.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC outer membrane {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004374}.
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DR EMBL; CP026257; AWP14372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CHM7; -.
DR STRING; 52904.ENSSMAP00000022759; -.
DR Proteomes; UP000246464; Chromosome 15.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16701; RING_CH-C4HC3_MARCH5; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46283; E3 UBIQUITIN-PROTEIN LIGASE MARCH5; 1.
DR PANTHER; PTHR46283:SF4; E3 UBIQUITIN-PROTEIN LIGASE MARCHF5; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..78
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
SQ SEQUENCE 281 AA; 31387 MW; 7DDBF148FA705D2D CRC64;
MADQGAVVMQ QNLDRSCWVC FATDEDDRTA EWVRPCHCRG STKWVHQACL QRWVDEKQRG
NSTARVACPQ CNAEYRIVFP KLGPVVYVLD LADRLISKAG PFAAAGIMVG SIYWTAVTYG
AVTVMQVVGH KEGLDVMERA DPLFLLIGLP TIPVMLILGK MIRWEDYVLR LWRKYSNKLQ
ILNSIFPGIG CPVPRIPAEA SPLADHVSAT RILCGALVFP TIATIVGKLM FSSVNSNLQR
TILGGIAFVA IKGAFKVYFK QQQYLRQAHR KILNFSEQEE A
//
