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E3 ubiquitin-protein ligase MIR1 (EC 2.3.2.27) (MK3) (Modulator of immune recognition 1 homolog) (ORF K3) (RING-type E3 ubiquitin transferase MIR1)

 MIR1_MHV68              Reviewed;         201 AA.
O41933;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
27-SEP-2017, entry version 99.
RecName: Full=E3 ubiquitin-protein ligase MIR1;
EC=2.3.2.27;
AltName: Full=MK3;
AltName: Full=Modulator of immune recognition 1 homolog;
AltName: Full=ORF K3;
AltName: Full=RING-type E3 ubiquitin transferase MIR1 {ECO:0000305};
Name=K3;
Murid herpesvirus 4 (MuHV-4) (Murine gammaherpesvirus 68).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Gammaherpesvirinae; Rhadinovirus.
NCBI_TaxID=33708;
NCBI_TaxID=10129; Apodemus sylvaticus (European woodmouse).
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Isolate g2.4, and Isolate WUMS;
PubMed=9223479;
Virgin H.W. IV, Latreille P., Wamsley P., Hallsworth K., Weck K.E.,
Dal Canto A.J., Speck S.H.;
"Complete sequence and genomic analysis of murine gammaherpesvirus
68.";
J. Virol. 71:5894-5904(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Isolate g2.4;
PubMed=2351958; DOI=10.1099/0022-1317-71-6-1355;
Efstathiou S., Ho Y.M., Minson A.C.;
"Cloning and molecular characterization of the murine herpesvirus 68
genome.";
J. Gen. Virol. 71:1355-1364(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MHV76;
PubMed=11333912; DOI=10.1128/JVI.75.11.5315-5327.2001;
Macrae A.I., Dutia B.M., Milligan S., Brownstein D.G., Allen D.J.,
Mistrikova J., Davison A.J., Nash A.A., Stewart J.P.;
"Analysis of a novel strain of murine gammaherpesvirus reveals a
genomic locus important for acute pathogenesis.";
J. Virol. 75:5315-5327(2001).
[4]
FUNCTION.
PubMed=10890918; DOI=10.1073/pnas.150240097;
Stevenson P.G., Efstathiou S., Doherty P.C., Lehner P.J.;
"Inhibition of MHC class I-restricted antigen presentation by gamma 2-
herpesviruses.";
Proc. Natl. Acad. Sci. U.S.A. 97:8455-8460(2000).
[5]
FUNCTION, DOMAIN RING-CH-TYPE ZINC-FINGER, AND SUBCELLULAR LOCATION.
PubMed=11672544; DOI=10.1016/S1074-7613(01)00213-8;
Boname J.M., Stevenson P.G.;
"MHC class I ubiquitination by a viral PHD/LAP finger protein.";
Immunity 15:627-636(2001).
[6]
DOMAIN RING-CH-TYPE ZINC-FINGER.
PubMed=12695663; DOI=10.4161/cc.2.2.335;
Aravind L., Iyer L.M., Koonin E.V.;
"Scores of RINGS but no PHDs in ubiquitin signaling.";
Cell Cycle 2:123-126(2003).
[7]
FUNCTION, DOMAIN DIRT, AND MUTAGENESIS OF TRP-9.
PubMed=17502423; DOI=10.1083/jcb.200611063;
Wang X., Herr R.A., Chua W.J., Lybarger L., Wiertz E.J., Hansen T.H.;
"Ubiquitination of serine, threonine, or lysine residues on the
cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3.";
J. Cell Biol. 177:613-624(2007).
[8]
FUNCTION.
PubMed=19531064; DOI=10.1111/j.1600-0854.2009.00946.x;
Herr R.A., Harris J., Fang S., Wang X., Hansen T.H.;
"Role of the RING-CH domain of viral ligase mK3 in ubiquitination of
non-lysine and lysine MHC I residues.";
Traffic 10:1301-1317(2009).
[9]
FUNCTION, AND INTERACTION WITH HOST UBE2J2.
PubMed=19951915; DOI=10.1083/jcb.200908036;
Wang X., Herr R.A., Rabelink M., Hoeben R.C., Wiertz E.J.,
Hansen T.H.;
"Ube2j2 ubiquitinates hydroxylated amino acids on ER-associated
degradation substrates.";
J. Cell Biol. 187:655-668(2009).
-!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
of host surface class I (MHC-I) H-2D(b)/H2-D1 and H-2K(b)/H2-K1
molecules before they exit the endoplasmic reticulum, leading to
their degradation by the endoplasmic reticulum-associated
degradation (ERAD) system, thus blocking the immune detection of
virus-infected cells. Mediates ubiquitination of lysine, as well
as serine and threonine residues present in the cytoplasmic tail
of surface class I molecules. Promotes ubiquitination of
hydroxylated serine or threonine residues via ester bonds instead
of the classical isopeptide linkage. {ECO:0000269|PubMed:10890918,
ECO:0000269|PubMed:11672544, ECO:0000269|PubMed:17502423,
ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915}.
-!- 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 host UBE2J2.
{ECO:0000269|PubMed:19951915}.
-!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
{ECO:0000269|PubMed:11672544}; Multi-pass membrane protein
{ECO:0000269|PubMed:11672544}.
-!- DOMAIN: The DIRT (domain in between the RING-CH-type and the first
transmembrane) region is essential to determine substrate residues
that can be ubiquitinated.
-!- DOMAIN: The RING-CH-type zinc finger (also named RINGV-type zinc-
finger) mediates the E3 ubiquitin ligase activity.
-!- MISCELLANEOUS: Murine herpesvirus 76 (MHV76) is identical to
murine herpesvirus 68 except for a large deletion at the genome
left end of the unique region.
-----------------------------------------------------------------------
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EMBL; U97553; AAB66429.1; -; Genomic_DNA.
EMBL; AF105037; AAF19280.1; -; Genomic_DNA.
EMBL; AF324455; AAK16705.1; -; Genomic_DNA.
RefSeq; NP_044852.1; NC_001826.2.
ProteinModelPortal; O41933; -.
SMR; O41933; -.
GeneID; 1497186; -.
KEGG; vg:1497186; -.
UniPathway; UPA00143; -.
Proteomes; UP000099649; Genome.
Proteomes; UP000175018; Genome.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:0039504; P:suppression by virus of host adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0046776; P:suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW.
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.
1: Evidence at protein level;
Complete proteome; Early protein; Host endoplasmic reticulum;
Host membrane; Host-virus interaction;
Inhibition of host adaptive immune response by virus;
Inhibition of host MHC class I molecule presentation by virus;
Membrane; Metal-binding; Reference proteome; Transferase;
Transmembrane; Transmembrane helix; Ubl conjugation pathway;
Viral immunoevasion; Zinc; Zinc-finger.
CHAIN 1 201 E3 ubiquitin-protein ligase MIR1.
/FTId=PRO_0000221391.
TOPO_DOM 1 81 Cytoplasmic. {ECO:0000255}.
TRANSMEM 82 102 Helical. {ECO:0000255}.
TOPO_DOM 103 113 Extracellular. {ECO:0000255}.
TRANSMEM 114 134 Helical. {ECO:0000255}.
TOPO_DOM 135 201 Cytoplasmic. {ECO:0000255}.
ZN_FING 1 58 RING-CH-type. {ECO:0000255|PROSITE-
ProRule:PRU00623}.
REGION 52 79 DIRT.
MUTAGEN 9 9 W->R: Abolishes E3 ligase activity.
{ECO:0000269|PubMed:17502423}.
SEQUENCE 201 AA; 22214 MW; 0953B5BDACDF8367 CRC64;
MDSTGEFCWI CHQPEGPLKR FCGCKGSCAV SHQDCLRGWL ETSRRQTCAL CGTPYSMKWK
TKPLREWTWG EEEVLAAMEA CLPLVLIPLA VLMIVMGTWL LVNHNGFLSP RMQVVLVVIV
LLAMIVFSAS ASYVMVEGPG CLDTCTAKNS TVTVNSIDEA IATQQPTKTD LGLARETLST
RFRRGKCRSC CRLGCVRLCC V


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