MARH8_BOVIN
ID MARH8_BOVIN Reviewed; 289 AA.
AC Q0VD59;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=E3 ubiquitin-protein ligase MARCHF8;
DE EC=2.3.2.27;
DE AltName: Full=Membrane-associated RING finger protein 8;
DE AltName: Full=Membrane-associated RING-CH protein VIII;
DE Short=MARCH-VIII;
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF8 {ECO:0000305};
GN Name=MARCHF8; Synonyms=MARCH8;
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=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of
CC CD86 and MHC class II proteins, such as HLA-DR alpha and beta, and
CC promotes their subsequent endocytosis and sorting to lysosomes via
CC multivesicular bodies. May also promote ubiquitination and endocytosis
CC of TFRC and FAS. {ECO:0000250|UniProtKB:Q5T0T0}.
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: Interacts with CD86. {ECO:0000250|UniProtKB:Q5T0T0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q5T0T0}; Multi-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q5T0T0}; Multi-
CC pass membrane protein {ECO:0000255}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q5T0T0}; 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; BC119819; AAI19820.1; -; mRNA.
DR RefSeq; NP_001069700.1; NM_001076232.1.
DR AlphaFoldDB; Q0VD59; -.
DR SMR; Q0VD59; -.
DR STRING; 9913.ENSBTAP00000039686; -.
DR PaxDb; Q0VD59; -.
DR Ensembl; ENSBTAT00000039901; ENSBTAP00000039686; ENSBTAG00000019537.
DR Ensembl; ENSBTAT00000068001; ENSBTAP00000059358; ENSBTAG00000019537.
DR GeneID; 540667; -.
DR KEGG; bta:540667; -.
DR CTD; 220972; -.
DR VEuPathDB; HostDB:ENSBTAG00000019537; -.
DR VGNC; VGNC:55990; MARCHF8.
DR eggNOG; KOG1609; Eukaryota.
DR GeneTree; ENSGT00940000158282; -.
DR HOGENOM; CLU_070599_0_1_1; -.
DR InParanoid; Q0VD59; -.
DR OMA; SCCRMKL; -.
DR OrthoDB; 1222747at2759; -.
DR TreeFam; TF319557; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000019537; Expressed in floor plate of diencephalon and 104 other tissues.
DR ExpressionAtlas; Q0VD59; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0042287; F:MHC protein binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0002495; P:antigen processing and presentation of peptide antigen via MHC class II; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
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 Adaptive immunity; Cytoplasmic vesicle; Endosome; Immunity; Lysosome;
KW Membrane; Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..289
FT /note="E3 ubiquitin-protein ligase MARCHF8"
FT /id="PRO_0000274369"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 70..131
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 124
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; 32780 MW; E7E1E0E11FD2560B CRC64;
MNMPLHQISA IPSQDATSAR VYRSKTKEKE REEQNEKTLG HSMSHSSNIS KAGGSSVASA
PVSSFPRTSV TPSNQDICRI CHCEGDDESP LITPCRCTGS LHFVHQTCLQ QWIKSSDTRC
CELCKYEFIM ETKLKPLRKW EKLQMTSSER RKIMCSVTFH VIAITCVVWS LYVLIDRTAE
EIRQGQATGI LEWPFWTKLV VVAIGFTGGL LFMYVQCKVY VQLWRRLKAY NRVIYVQNCP
ETSKRNIFEK PALPEPNFES KDGRGVCHSD TNSSCCTEPE DTGAEIIHV
