MARH8_MOUSE
ID MARH8_MOUSE Reviewed; 286 AA.
AC Q9DBD2;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=E3 ubiquitin-protein ligase MARCHF8;
DE EC=2.3.2.27;
DE AltName: Full=Cellular modulator of immune recognition;
DE Short=c-MIR;
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, Mir;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=16785530; DOI=10.4049/jimmunol.177.1.341;
RA Ohmura-Hoshino M., Matsuki Y., Aoki M., Goto E., Mito M., Uematsu M.,
RA Kakiuchi T., Hotta H., Ishido S.;
RT "Inhibition of MHC class II expression and immune responses by c-MIR.";
RL J. Immunol. 177:341-354(2006).
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 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:16785530}.
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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK005032; BAB23759.1; -; mRNA.
DR EMBL; AK154976; BAE32966.1; -; mRNA.
DR EMBL; BC050908; AAH50908.1; -; mRNA.
DR EMBL; BC053090; AAH53090.1; -; mRNA.
DR CCDS; CCDS20451.1; -.
DR RefSeq; NP_001289312.1; NM_001302383.1.
DR RefSeq; NP_001289313.1; NM_001302384.1.
DR RefSeq; NP_001289314.1; NM_001302385.1.
DR RefSeq; NP_082196.1; NM_027920.5.
DR AlphaFoldDB; Q9DBD2; -.
DR STRING; 10090.ENSMUSP00000098594; -.
DR iPTMnet; Q9DBD2; -.
DR PhosphoSitePlus; Q9DBD2; -.
DR MaxQB; Q9DBD2; -.
DR PaxDb; Q9DBD2; -.
DR PRIDE; Q9DBD2; -.
DR ProteomicsDB; 252733; -.
DR Antibodypedia; 3041; 167 antibodies from 32 providers.
DR DNASU; 71779; -.
DR Ensembl; ENSMUST00000079012; ENSMUSP00000078024; ENSMUSG00000025702.
DR Ensembl; ENSMUST00000101032; ENSMUSP00000098594; ENSMUSG00000025702.
DR GeneID; 71779; -.
DR KEGG; mmu:71779; -.
DR UCSC; uc009djz.2; mouse.
DR CTD; 220972; -.
DR MGI; MGI:1919029; Marchf8.
DR VEuPathDB; HostDB:ENSMUSG00000025702; -.
DR eggNOG; KOG1609; Eukaryota.
DR GeneTree; ENSGT00940000158282; -.
DR InParanoid; Q9DBD2; -.
DR OMA; SCCRMKL; -.
DR PhylomeDB; Q9DBD2; -.
DR TreeFam; TF319557; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 71779; 2 hits in 48 CRISPR screens.
DR ChiTaRS; March8; mouse.
DR PRO; PR:Q9DBD2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9DBD2; protein.
DR Bgee; ENSMUSG00000025702; Expressed in otolith organ and 224 other tissues.
DR ExpressionAtlas; Q9DBD2; baseline and differential.
DR Genevisible; Q9DBD2; MM.
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:0042289; F:MHC class II protein binding; IPI:BHF-UCL.
DR GO; GO:0042287; F:MHC protein binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA: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; IDA:UniProtKB.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
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; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..286
FT /note="E3 ubiquitin-protein ligase MARCHF8"
FT /id="PRO_0000274371"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 68..129
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT REGION 23..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T0T0"
SQ SEQUENCE 286 AA; 32243 MW; 3F4D68112A4C0400 CRC64;
MSMPLHQISA IPSQDAISAR VYRSKTKDKE QNEKTLGHSM SHPSNISKAG SSPPSTTAPV
SAFSRTSVTP SNQDICRICH CEGDDESPLI TPCHCTGSLH FVHQACLQQW IKSSDTRCCE
LCKYEFIMET KLKPLRKWEK LQMTASERRK IMCSVTFHVI AITCVVWSLY VLIDRTAEEI
KQGQVTGILE WPFWTKLVVV AIGFTGGLLF MYVQCKVYLQ LWKRLKAYNR VIYVQNCPET
SKKNIFEKSA LTEPTLENKE GHGMCHSTTN SSCTEPEDTG AEIINV
