MARH4_DANRE
ID MARH4_DANRE Reviewed; 421 AA.
AC Q0P496;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=E3 ubiquitin-protein ligase MARCHF4;
DE EC=2.3.2.27;
DE AltName: Full=Membrane-associated RING finger protein 4;
DE AltName: Full=Membrane-associated RING-CH protein IV;
DE Short=MARCH-IV;
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF4 {ECO:0000305};
DE Flags: Precursor;
GN Name=marchf4; Synonyms=march4; ORFNames=zgc:153256;
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=Testis;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase. E3 ubiquitin ligases accept
CC ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a
CC thioester and then directly transfer the ubiquitin to targeted
CC substrates. {ECO:0000250}.
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: Golgi apparatus membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
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; BC122209; AAI22210.1; -; mRNA.
DR RefSeq; NP_001038876.1; NM_001045411.1.
DR AlphaFoldDB; Q0P496; -.
DR STRING; 7955.ENSDARP00000081369; -.
DR PaxDb; Q0P496; -.
DR GeneID; 100000640; -.
DR KEGG; dre:100000640; -.
DR CTD; 100000640; -.
DR ZFIN; ZDB-GENE-060825-323; march4l.
DR eggNOG; KOG1609; Eukaryota.
DR InParanoid; Q0P496; -.
DR OrthoDB; 748231at2759; -.
DR PhylomeDB; Q0P496; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q0P496; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR046356; MARCHF4/9/11.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46053; PTHR46053; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 2: Evidence at transcript level;
KW Golgi apparatus; Membrane; Metal-binding; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..421
FT /note="E3 ubiquitin-protein ligase MARCHF4"
FT /id="PRO_0000274510"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 135..195
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT REGION 60..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
SQ SEQUENCE 421 AA; 46352 MW; BB78802ED1ECC78D CRC64;
MLLAIGVIVW CWGLLSRRPM LRRQGKQKGR CCVLFSDLEV FLLRPPTPSA SPPAFTPMNE
LNAEGNATSS ATESHSLANG HYQPVTGEEA LDTRGPDDWT HSVVDPPRTL DCCSSSEDCS
KEKLDERLSL NSCTDSGVRT PLCRICFQGP EQGELLSPCR CSGSVRCTHE PCLIKWISER
GSWSCELCYY KYQVIAISTK NPLQWQAISL TVIEKVQIAA AVLGSLFLIA SISWLVWSSL
SPSAKWQRQD LLFQICYAMY GFMDLVCIAL IVHEGPSVFR IFNRWQAVNQ QWKVLNYDKV
KDNEDHQKTG ATFRTLSLPL THRMGQSGPE GEPSTSTSSL MAAAAAAAAG TVTPTTNSVP
PAAGATTEPQ DSSEPSNGQP SLPDHHCAYN ILHLLSHLRQ QEPRGQTSNS NRELVMRVTT
V
