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UL37 immediate early glycoprotein

 VGLI_HCMVA              Reviewed;         487 AA.
P16778; P87887; Q7M6P6;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
25-OCT-2017, entry version 70.
RecName: Full=UL37 immediate early glycoprotein;
Flags: Precursor;
Name=UL37;
Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Betaherpesvirinae; Cytomegalovirus.
NCBI_TaxID=10360;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2838954; DOI=10.1016/0042-6822(88)90668-X;
Kouzarides T., Bankier A.T., Satchwell S.C., Preddy E., Barrell B.G.;
"An immediate early gene of human cytomegalovirus encodes a potential
membrane glycoprotein.";
Virology 165:151-164(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ISOFORM PUL37M, AND
ISOFORM VMIA.
PubMed=2161319;
Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
"Analysis of the protein-coding content of the sequence of human
cytomegalovirus strain AD169.";
Curr. Top. Microbiol. Immunol. 154:125-169(1990).
[3]
GENOME REANNOTATION.
PubMed=12533697; DOI=10.1099/vir.0.18606-0;
Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J.,
Alcendor D.J., McGeoch D.J., Hayward G.S.;
"The human cytomegalovirus genome revisited: comparison with the
chimpanzee cytomegalovirus genome.";
J. Gen. Virol. 84:17-28(2003).
[4]
ERRATUM.
Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J.,
Alcendor D.J., McGeoch D.J., Hayward G.S.;
J. Gen. Virol. 84:1053-1053(2003).
[5]
SUBCELLULAR LOCATION.
PubMed=8794367;
Al-Barazi H.O., Colberg-Poley A.M.;
"The human cytomegalovirus UL37 immediate-early regulatory protein is
an integral membrane N-glycoprotein which traffics through the
endoplasmic reticulum and Golgi apparatus.";
J. Virol. 70:7198-7208(1996).
[6]
FUNCTION, AND INTERACTION WITH HOST BAX.
PubMed=15004026; DOI=10.1074/jbc.M308408200;
Poncet D., Larochette N., Pauleau A.L., Boya P., Jalil A.A.,
Cartron P.F., Vallette F., Schnebelen C., Bartle L.M., Skaletskaya A.,
Boutolleau D., Martinou J.C., Goldmacher V.S., Kroemer G., Zamzami N.;
"An anti-apoptotic viral protein that recruits Bax to mitochondria.";
J. Biol. Chem. 279:22605-22614(2004).
[7]
FUNCTION.
PubMed=15148411; DOI=10.1073/pnas.0401897101;
Arnoult D., Bartle L.M., Skaletskaya A., Poncet D., Zamzami N.,
Park P.U., Sharpe J., Youle R.J., Goldmacher V.S.;
"Cytomegalovirus cell death suppressor vMIA blocks Bax- but not Bak-
mediated apoptosis by binding and sequestering Bax at mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 101:7988-7993(2004).
[8]
CLEAVAGE SITE, AND SUBCELLULAR LOCATION.
PubMed=15218184; DOI=10.1099/vir.0.80094-0;
Mavinakere M.S., Colberg-Poley A.M.;
"Internal cleavage of the human cytomegalovirus UL37 immediate-early
glycoprotein and divergent trafficking of its proteolytic fragments.";
J. Gen. Virol. 85:1989-1994(2004).
[9]
SUBCELLULAR LOCATION.
PubMed=20504938; DOI=10.1128/JVI.00885-10;
Bozidis P., Williamson C.D., Wong D.S., Colberg-Poley A.M.;
"Trafficking of UL37 proteins into mitochondrion-associated membranes
during permissive human cytomegalovirus infection.";
J. Virol. 84:7898-7903(2010).
[10]
INTERACTION WITH HOST RSAD2.
PubMed=21527675; DOI=10.1126/science.1202007;
Seo J.Y., Yaneva R., Hinson E.R., Cresswell P.;
"Human cytomegalovirus directly induces the antiviral protein viperin
to enhance infectivity.";
Science 332:1093-1097(2011).
[11]
FUNCTION.
PubMed=21907833; DOI=10.1016/j.mito.2011.08.008;
Kaarbo M., Ager-Wick E., Osenbroch P.O., Kilander A., Skinnes R.,
Muller F., Eide L.;
"Human cytomegalovirus infection increases mitochondrial biogenesis.";
Mitochondrion 11:935-945(2011).
-!- FUNCTION: Isoform vMIA sequesters proapoptotic BAX at the outer
mitochondrial membrane and prevents cytochrome c release and
subsequent initiation of the proapoptotic cascade. Also provoques
a calcium efflux from host endoplasmic reticulum and F-actin
cytoskeleton disruption. Participates in the increase of host
mitochondrial biogenesis, thus promoting viral replication by
efficient use of newly made mitochondria.
-!- FUNCTION: Isoform gpUL37 may play a role in escape from the host
antiviral response.
-!- SUBUNIT: Isoform vMIA interacts with host BAX. Isoform vMIA
interacts with host RSAD2/viperin; this interaction results in
RSAD2/viperin relocalization from the endoplasmic reticulum to the
mitochondria, actin cytoskeleton disruption and enhancement of
infection. {ECO:0000269|PubMed:15004026,
ECO:0000269|PubMed:21527675}.
-!- INTERACTION:
Q07812:BAX (xeno); NbExp=2; IntAct=EBI-16026491, EBI-516580;
-!- SUBCELLULAR LOCATION: Isoform gpUL37: Host endoplasmic reticulum
membrane {ECO:0000269|PubMed:8794367}; Single-pass membrane
protein {ECO:0000255}. Host Golgi apparatus membrane
{ECO:0000269|PubMed:8794367}; Single-pass membrane protein
{ECO:0000255}. Host mitochondrion membrane
{ECO:0000269|PubMed:20504938}; Single-pass membrane protein
{ECO:0000255}. Note=The C-terminal fragment localizes to the
endoplasmic reticulum while the N-terminal fragment is stable and
traffics to mitochondria.
-!- SUBCELLULAR LOCATION: Isoform vMIA: Host mitochondrion membrane
{ECO:0000269|PubMed:15218184}; Single-pass membrane protein
{ECO:0000255}. Host endoplasmic reticulum membrane
{ECO:0000269|PubMed:15218184}; Single-pass membrane protein
{ECO:0000255}. Note=Transported from the endoplasmic reticulum
(ER) through the mitochondrial associated membrane (MAMs) to the
mitochondrial outer membrane. Associates with internal lipid rafts
(LRs) in the MAM. {ECO:0000269|PubMed:15218184}.
-!- SUBCELLULAR LOCATION: Isoform pUL37m: Host mitochondrion membrane
{ECO:0000269|PubMed:15218184}; Single-pass membrane protein
{ECO:0000255}. Host endoplasmic reticulum membrane
{ECO:0000269|PubMed:15218184}; Single-pass membrane protein
{ECO:0000255}. Note=Not cleaved or N-glycosylated.
{ECO:0000269|PubMed:15218184}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=gpUL37;
IsoId=P16778-1; Sequence=Displayed;
Name=vMIA;
IsoId=P16778-2; Sequence=VSP_044014, VSP_044015;
Name=pUL37m;
IsoId=P16778-3; Sequence=VSP_044016;
-!- SIMILARITY: Belongs to the immediate early glycoprotein family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X17403; CAA35396.1; -; Genomic_DNA.
EMBL; BK000394; DAA00142.1; -; Genomic_DNA.
PIR; S09801; QQBEU5.
PDB; 2LR1; NMR; -; B=130-150.
PDBsum; 2LR1; -.
SMR; P16778; -.
DIP; DIP-60096N; -.
IntAct; P16778; 1.
PRIDE; P16778; -.
OrthoDB; VOG090000BL; -.
Proteomes; UP000008991; Genome.
Proteomes; UP000008992; Genome.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0044191; C:host cell mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
InterPro; IPR010880; Herpes_UL37_HHV-5-rel.
Pfam; PF07413; Herpes_UL37_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Glycoprotein;
Host endoplasmic reticulum; Host Golgi apparatus; Host membrane;
Host mitochondrion; Host-virus interaction; Membrane;
Modulation of host cell apoptosis by virus; Reference proteome;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 487 UL37 immediate early glycoprotein.
/FTId=PRO_0000037455.
TRANSMEM 433 459 Helical. {ECO:0000255}.
COMPBIAS 97 108 Poly-Glu.
SITE 193 194 Cleavage site.
CARBOHYD 206 206 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 210 210 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 223 223 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 242 242 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 294 294 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 297 297 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 306 306 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 337 337 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 343 343 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 379 379 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 384 384 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 391 391 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
VAR_SEQ 163 163 H -> Q (in isoform vMIA). {ECO:0000305}.
/FTId=VSP_044014.
VAR_SEQ 164 487 Missing (in isoform vMIA). {ECO:0000305}.
/FTId=VSP_044015.
VAR_SEQ 178 262 Missing (in isoform pUL37m).
{ECO:0000305}.
/FTId=VSP_044016.
HELIX 138 145 {ECO:0000244|PDB:2LR1}.
STRAND 146 148 {ECO:0000244|PDB:2LR1}.
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


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