VGLI_HCMVM
ID VGLI_HCMVM Reviewed; 488 AA.
AC Q6SW94; D2K3K5;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 23-FEB-2022, entry version 57.
DE RecName: Full=UL37 immediate early glycoprotein;
DE Flags: Precursor;
GN Name=UL37;
OS Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=295027;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT "Genetic content of wild-type human cytomegalovirus.";
RL J. Gen. Virol. 85:1301-1312(2004).
CC -!- FUNCTION: Isoform vMIA sequesters proapoptotic BAX at the outer
CC mitochondrial membrane and prevents cytochrome c release and subsequent
CC initiation of the proapoptotic cascade. Also provoques a calcium efflux
CC from host endoplasmic reticulum and F-actin cytoskeleton disruption.
CC Participates in the increase of host mitochondrial biogenesis, thus
CC promoting viral replication by efficient use of newly made mitochondria
CC (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Isoform gpUL37 may play a role in escape from the host
CC antiviral response. {ECO:0000250}.
CC -!- SUBUNIT: Isoform vMIA interacts with host BAX. Isoform vMIA interacts
CC with host RSAD2/viperin; this interaction results in RSAD2/viperin
CC relocalization from the endoplasmic reticulum to the mitochondria,
CC actin cytoskeleton disruption and enhancement of infection (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform gpUL37]: Host membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Host endoplasmic reticulum
CC membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC Host Golgi apparatus membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Host mitochondrion membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Note=The C-terminal
CC fragment localizes to the endoplasmic reticulum while the N-terminal
CC fragment is stable and traffics to mitochondria. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform vMIA]: Host mitochondrion membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Host
CC endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Note=Transported from the endoplasmic reticulum
CC (ER) through the mitochondrial associated membrane (MAMs) to the
CC mitochondrial outer membrane. Associates with internal lipid rafts
CC (LRs) in the MAM (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform pUL37m]: Host mitochondrion membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Host
CC endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Note=Not cleaved or N-glycosylated.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=gpUL37;
CC IsoId=Q6SW94-1; Sequence=Displayed;
CC Name=vMIA;
CC IsoId=Q6SW94-2; Sequence=VSP_044022, VSP_044023;
CC Name=pUL37m;
CC IsoId=Q6SW94-3; Sequence=VSP_044024;
CC -!- SIMILARITY: Belongs to the immediate early glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; AY446894; AAR31602.1; -; Genomic_DNA.
DR RefSeq; YP_081496.1; NC_006273.2.
DR BMRB; Q6SW94; -.
DR PRIDE; Q6SW94; -.
DR GeneID; 3077462; -.
DR KEGG; vg:3077462; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Proteomes; UP000000938; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044191; C:host cell mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
DR InterPro; IPR010880; Herpes_UL37_HHV-5-rel.
DR Pfam; PF07413; Herpes_UL37_2; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Glycoprotein; Host endoplasmic reticulum;
KW Host Golgi apparatus; Host membrane; Host mitochondrion;
KW Host-virus interaction; Membrane;
KW Modulation of host cell apoptosis by virus; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..488
FT /note="UL37 immediate early glycoprotein"
FT /id="PRO_0000418298"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 83..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 193..194
FT /note="Cleavage site"
FT /evidence="ECO:0000250"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT VAR_SEQ 163
FT /note="H -> Q (in isoform vMIA)"
FT /evidence="ECO:0000305"
FT /id="VSP_044022"
FT VAR_SEQ 164..487
FT /note="Missing (in isoform vMIA)"
FT /evidence="ECO:0000305"
FT /id="VSP_044023"
FT VAR_SEQ 178..262
FT /note="Missing (in isoform pUL37m)"
FT /evidence="ECO:0000305"
FT /id="VSP_044024"
SQ SEQUENCE 488 AA; 56088 MW; 7F9956DE7D43CCF2 CRC64;
MSPVYVNLLG SVGLLAFWYF SYRWIQRKRL EDPLPPWLRK KKACALTRRS RHRLRRQHGV
IDGENSETER SVDLVAALLA EAGEESVTED TEREDTEEER EDEEEENEAR TPEVNPMDAE
GLSGLAREAC EALKKALRRH RFLWQRRRRA RLLQHNGPQQ SHHAAVFCRV HGLRGFQVSV
WLLLTLFWST GYGVSVRCTY HGTDINVTSN ATSMNCRLNC TCNHTQIYNG PCAGAESKLP
LNVTFRQSRR QWHSVMLTFG FQYHLEGWFP LRILNESRDI NVTEVYGEVA CFTNDTNITM
GQLTLNLTGR SYVLRALART SPFESSVNWE ETNVTDNATS SENNTVTVMS VLTVYAESDY
IFLQDMCPRF LKRSVKLAKN NRRNTTFTGT NVTSLPEWTL QQCQGWKYWT TLSIMWKNRR
SALLRAKSRA LGHWALLSIC TVAAGSIALL SLFCILLIGL RRDLLEDFRY ICRDEGSSST
KNDVHWIV
