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E3 ubiquitin-protein ligase MARCH8 (EC 2.3.2.27) (Cellular modulator of immune recognition) (c-MIR) (Membrane-associated RING finger protein 8) (Membrane-associated RING-CH protein VIII) (MARCH-VIII) (RING-type E3 ubiquitin transferase MARCH8)

 MARH8_MOUSE             Reviewed;         286 AA.
Q9DBD2;
06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
10-MAY-2017, entry version 129.
RecName: Full=E3 ubiquitin-protein ligase MARCH8;
EC=2.3.2.27;
AltName: Full=Cellular modulator of immune recognition;
Short=c-MIR;
AltName: Full=Membrane-associated RING finger protein 8;
AltName: Full=Membrane-associated RING-CH protein VIII;
Short=MARCH-VIII;
AltName: Full=RING-type E3 ubiquitin transferase MARCH8 {ECO:0000305};
Name=March8; Synonyms=Mir;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION.
PubMed=16785530; DOI=10.4049/jimmunol.177.1.341;
Ohmura-Hoshino M., Matsuki Y., Aoki M., Goto E., Mito M., Uematsu M.,
Kakiuchi T., Hotta H., Ishido S.;
"Inhibition of MHC class II expression and immune responses by c-
MIR.";
J. Immunol. 177:341-354(2006).
-!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
of CD86 and MHC class II proteins, such as HLA-DR alpha and beta,
and promotes their subsequent endocytosis and sorting to lysosomes
via multivesicular bodies. May also promote ubiquitination and
endocytosis of TFRC and FAS (By similarity). {ECO:0000250,
ECO:0000269|PubMed:16785530}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with CD86. {ECO:0000250|UniProtKB:Q5T0T0}.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
{ECO:0000250|UniProtKB:Q5T0T0}; Multi-pass membrane protein
{ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q5T0T0};
Multi-pass membrane protein {ECO:0000255}. Early endosome membrane
{ECO:0000250|UniProtKB:Q5T0T0}; Multi-pass membrane protein
{ECO:0000255}.
-!- DOMAIN: The RING-CH-type zinc finger domain is required for E3
ligase activity.
-----------------------------------------------------------------------
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EMBL; AK005032; BAB23759.1; -; mRNA.
EMBL; AK154976; BAE32966.1; -; mRNA.
EMBL; BC050908; AAH50908.1; -; mRNA.
EMBL; BC053090; AAH53090.1; -; mRNA.
CCDS; CCDS20451.1; -.
RefSeq; NP_001289312.1; NM_001302383.1.
RefSeq; NP_001289313.1; NM_001302384.1.
RefSeq; NP_001289314.1; NM_001302385.1.
RefSeq; NP_082196.1; NM_027920.5.
UniGene; Mm.27064; -.
ProteinModelPortal; Q9DBD2; -.
SMR; Q9DBD2; -.
STRING; 10090.ENSMUSP00000078024; -.
iPTMnet; Q9DBD2; -.
PhosphoSitePlus; Q9DBD2; -.
MaxQB; Q9DBD2; -.
PaxDb; Q9DBD2; -.
PRIDE; Q9DBD2; -.
Ensembl; ENSMUST00000079012; ENSMUSP00000078024; ENSMUSG00000025702.
Ensembl; ENSMUST00000101032; ENSMUSP00000098594; ENSMUSG00000025702.
GeneID; 71779; -.
KEGG; mmu:71779; -.
UCSC; uc009djz.2; mouse.
CTD; 220972; -.
MGI; MGI:1919029; March8.
eggNOG; KOG1609; Eukaryota.
eggNOG; COG5183; LUCA.
GeneTree; ENSGT00730000110355; -.
HOGENOM; HOG000113483; -.
HOVERGEN; HBG081957; -.
InParanoid; Q9DBD2; -.
KO; K10656; -.
OrthoDB; EOG091G0WJX; -.
PhylomeDB; Q9DBD2; -.
TreeFam; TF319557; -.
UniPathway; UPA00143; -.
ChiTaRS; March8; mouse.
PRO; PR:Q9DBD2; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000025702; -.
CleanEx; MM_MARCH8; -.
ExpressionAtlas; Q9DBD2; baseline and differential.
Genevisible; Q9DBD2; MM.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0042289; F:MHC class II protein binding; IPI:BHF-UCL.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0002495; P:antigen processing and presentation of peptide antigen via MHC class II; IDA:UniProtKB.
GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IDA:BHF-UCL.
GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR033275; MARCH-like.
InterPro; IPR011016; Znf_RING-CH.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR23012; PTHR23012; 1.
Pfam; PF12906; RINGv; 1.
SMART; SM00744; RINGv; 1.
PROSITE; PS51292; ZF_RING_CH; 1.
2: Evidence at transcript level;
Adaptive immunity; Complete proteome; Cytoplasmic vesicle; Endosome;
Immunity; Lysosome; Membrane; Metal-binding; Phosphoprotein;
Reference proteome; Transferase; Transmembrane; Transmembrane helix;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 286 E3 ubiquitin-protein ligase MARCH8.
/FTId=PRO_0000274371.
TRANSMEM 153 173 Helical. {ECO:0000255}.
TRANSMEM 193 213 Helical. {ECO:0000255}.
ZN_FING 68 129 RING-CH-type. {ECO:0000255|PROSITE-
ProRule:PRU00623}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000250|UniProtKB:Q5T0T0}.
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


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