VGLI_HCMVA
ID VGLI_HCMVA Reviewed; 487 AA.
AC P16778; P87887; Q7M6P6;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 02-JUN-2021, entry version 81.
DE RecName: Full=UL37 immediate early glycoprotein;
DE Flags: Precursor;
GN Name=UL37;
OS Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2838954; DOI=10.1016/0042-6822(88)90668-x;
RA Kouzarides T., Bankier A.T., Satchwell S.C., Preddy E., Barrell B.G.;
RT "An immediate early gene of human cytomegalovirus encodes a potential
RT membrane glycoprotein.";
RL Virology 165:151-164(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ISOFORM PUL37M, AND ISOFORM
RP VMIA.
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [3]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [4]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=8794367; DOI=10.1128/jvi.70.10.7198-7208.1996;
RA Al-Barazi H.O., Colberg-Poley A.M.;
RT "The human cytomegalovirus UL37 immediate-early regulatory protein is an
RT integral membrane N-glycoprotein which traffics through the endoplasmic
RT reticulum and Golgi apparatus.";
RL J. Virol. 70:7198-7208(1996).
RN [6]
RP FUNCTION, AND INTERACTION WITH HOST BAX.
RX PubMed=15004026; DOI=10.1074/jbc.m308408200;
RA Poncet D., Larochette N., Pauleau A.L., Boya P., Jalil A.A., Cartron P.F.,
RA Vallette F., Schnebelen C., Bartle L.M., Skaletskaya A., Boutolleau D.,
RA Martinou J.C., Goldmacher V.S., Kroemer G., Zamzami N.;
RT "An anti-apoptotic viral protein that recruits Bax to mitochondria.";
RL J. Biol. Chem. 279:22605-22614(2004).
RN [7]
RP FUNCTION.
RX PubMed=15148411; DOI=10.1073/pnas.0401897101;
RA Arnoult D., Bartle L.M., Skaletskaya A., Poncet D., Zamzami N., Park P.U.,
RA Sharpe J., Youle R.J., Goldmacher V.S.;
RT "Cytomegalovirus cell death suppressor vMIA blocks Bax- but not Bak-
RT mediated apoptosis by binding and sequestering Bax at mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7988-7993(2004).
RN [8]
RP CLEAVAGE SITE, AND SUBCELLULAR LOCATION.
RX PubMed=15218184; DOI=10.1099/vir.0.80094-0;
RA Mavinakere M.S., Colberg-Poley A.M.;
RT "Internal cleavage of the human cytomegalovirus UL37 immediate-early
RT glycoprotein and divergent trafficking of its proteolytic fragments.";
RL J. Gen. Virol. 85:1989-1994(2004).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=20504938; DOI=10.1128/jvi.00885-10;
RA Bozidis P., Williamson C.D., Wong D.S., Colberg-Poley A.M.;
RT "Trafficking of UL37 proteins into mitochondrion-associated membranes
RT during permissive human cytomegalovirus infection.";
RL J. Virol. 84:7898-7903(2010).
RN [10]
RP INTERACTION WITH HOST RSAD2.
RX PubMed=21527675; DOI=10.1126/science.1202007;
RA Seo J.Y., Yaneva R., Hinson E.R., Cresswell P.;
RT "Human cytomegalovirus directly induces the antiviral protein viperin to
RT enhance infectivity.";
RL Science 332:1093-1097(2011).
RN [11]
RP FUNCTION.
RX PubMed=21907833; DOI=10.1016/j.mito.2011.08.008;
RA Kaarbo M., Ager-Wick E., Osenbroch P.O., Kilander A., Skinnes R.,
RA Muller F., Eide L.;
RT "Human cytomegalovirus infection increases mitochondrial biogenesis.";
RL Mitochondrion 11:935-945(2011).
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
CC mitochondria.
CC -!- FUNCTION: Isoform gpUL37 may play a role in escape from the host
CC antiviral response.
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.
CC {ECO:0000269|PubMed:15004026, ECO:0000269|PubMed:21527675}.
CC -!- INTERACTION:
CC P16778; Q07812: BAX; Xeno; NbExp=2; IntAct=EBI-16026491, EBI-516580;
CC -!- SUBCELLULAR LOCATION: [Isoform gpUL37]: Host endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:8794367}; Single-pass membrane protein
CC {ECO:0000255}. Host Golgi apparatus membrane
CC {ECO:0000269|PubMed:8794367}; Single-pass membrane protein
CC {ECO:0000255}. Host mitochondrion membrane
CC {ECO:0000269|PubMed:20504938}; Single-pass membrane protein
CC {ECO:0000255}. Note=The C-terminal fragment localizes to the
CC endoplasmic reticulum while the N-terminal fragment is stable and
CC traffics to mitochondria.
CC -!- SUBCELLULAR LOCATION: [Isoform vMIA]: Host mitochondrion membrane
CC {ECO:0000269|PubMed:15218184}; Single-pass membrane protein
CC {ECO:0000255}. Host endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15218184}; Single-pass membrane protein
CC {ECO:0000255}. Note=Transported from the endoplasmic reticulum (ER)
CC through the mitochondrial associated membrane (MAMs) to the
CC mitochondrial outer membrane. Associates with internal lipid rafts
CC (LRs) in the MAM. {ECO:0000269|PubMed:15218184}.
CC -!- SUBCELLULAR LOCATION: [Isoform pUL37m]: Host mitochondrion membrane
CC {ECO:0000269|PubMed:15218184}; Single-pass membrane protein
CC {ECO:0000255}. Host endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15218184}; Single-pass membrane protein
CC {ECO:0000255}. Note=Not cleaved or N-glycosylated.
CC {ECO:0000269|PubMed:15218184}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=gpUL37;
CC IsoId=P16778-1; Sequence=Displayed;
CC Name=vMIA;
CC IsoId=P16778-2; Sequence=VSP_044014, VSP_044015;
CC Name=pUL37m;
CC IsoId=P16778-3; Sequence=VSP_044016;
CC -!- SIMILARITY: Belongs to the immediate early glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; X17403; CAA35396.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00142.1; -; Genomic_DNA.
DR PIR; S09801; QQBEU5.
DR PDB; 2LR1; NMR; -; B=130-150.
DR PDBsum; 2LR1; -.
DR BMRB; P16778; -.
DR SMR; P16778; -.
DR DIP; DIP-60096N; -.
DR IntAct; P16778; 1.
DR BindingDB; P16778; -.
DR PRIDE; P16778; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Glycoprotein;
KW Host endoplasmic reticulum; Host Golgi apparatus; Host membrane;
KW Host mitochondrion; 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..487
FT /note="UL37 immediate early glycoprotein"
FT /id="PRO_0000037455"
FT TRANSMEM 433..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 83..121
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 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 246
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 379
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_044014"
FT VAR_SEQ 164..487
FT /note="Missing (in isoform vMIA)"
FT /evidence="ECO:0000305"
FT /id="VSP_044015"
FT VAR_SEQ 178..262
FT /note="Missing (in isoform pUL37m)"
FT /evidence="ECO:0000305"
FT /id="VSP_044016"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:2LR1"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2LR1"
SQ SEQUENCE 487 AA; 56125 MW; FA39A37C51FFB4A3 CRC64;
MSPVYVNLLG SVGLLAFWYF SYRWIQRKRL EDPLPPWLRK KKACALTRRS RHRLRRQHGV
IDGENSETER SVDLVAALLA EAGEESVTED TEREDTEEER EDEEEENEAR TPEVNPIDAE
GLSGLAREAC EALKKALRRH RFLWQRRQRA RMLQHNGPQQ SHHAAVFCRV HGLRGFQVSV
WLLLTLLWST GHGVSVRCTY HGTDVNRTSN TTSMNCHLNC TRNHTQIYNG PCLGTEARLP
LNVTFNQSRR KWHSVMLKFG FQYHLEGWFP LRVLNESREI NVTEVHGEVA CFRNDTNVTV
GQLTLNFTGH SYVLRAIAHT SPFESYVRWE ETNVTDNATS SENTTTVMST LTKYAESDYI
FLQDMCPRFL KRTVKLTRNK TKHNVTVTGN NMTTLPVWTP ECKGWTYWTT LSVMWRNRRS
ALLRAKSRAL GHWALLSICT VAAGSIALLS LFCILLIGLR RDLLEDFRYI CRDEGSSSTK
NDVHRIV
