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P16778 (VGLI_HCMVA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UL37 immediate early glycoprotein
Gene names
Name:UL37
OrganismHuman cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) [Complete proteome]
Taxonomic identifier10360 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeBetaherpesvirinaeCytomegalovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length487 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.6 Ref.7 Ref.11

Isoform gpUL37 may play a role in escape from the host antiviral response. Ref.6 Ref.7 Ref.11

Subunit structure

Isofom 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. Ref.6 Ref.10

Subcellular location

Isoform gpUL37: Host membrane; Single-pass membrane protein. Host endoplasmic reticulum membrane; Single-pass membrane protein. Host Golgi apparatus membrane; Single-pass membrane protein. Host mitochondrion membrane; Single-pass membrane protein. Note: The C-terminal fragment localizes to the endoplasmic reticulum while the N-terminal fragment is stable and traffics to mitochondria. Ref.5 Ref.8 Ref.9

Isoform vMIA: Host mitochondrion membrane; Single-pass membrane protein. Host endoplasmic reticulum membrane; Single-pass membrane protein. 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. Ref.5 Ref.8 Ref.9

Isoform pUL37m: Host mitochondrion membrane; Single-pass membrane protein. Host endoplasmic reticulum membrane; Single-pass membrane protein. Note: Not cleaved or N-glycosylated. Ref.5 Ref.8 Ref.9

Sequence similarities

Belongs to the immediate early glycoprotein family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform gpUL37 (identifier: P16778-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform vMIA (identifier: P16778-2)

The sequence of this isoform differs from the canonical sequence as follows:
     163-163: H → Q
     164-487: Missing.
Isoform pUL37m (identifier: P16778-3)

The sequence of this isoform differs from the canonical sequence as follows:
     178-262: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 487465UL37 immediate early glycoprotein
PRO_0000037455

Regions

Transmembrane433 – 45927Helical; Potential
Compositional bias97 – 10812Poly-Glu

Sites

Site193 – 1942Cleavage site

Amino acid modifications

Glycosylation2061N-linked (GlcNAc...); by host Potential
Glycosylation2101N-linked (GlcNAc...); by host Potential
Glycosylation2191N-linked (GlcNAc...); by host Potential
Glycosylation2231N-linked (GlcNAc...); by host Potential
Glycosylation2421N-linked (GlcNAc...); by host Potential
Glycosylation2461N-linked (GlcNAc...); by host Potential
Glycosylation2751N-linked (GlcNAc...); by host Potential
Glycosylation2811N-linked (GlcNAc...); by host Potential
Glycosylation2941N-linked (GlcNAc...); by host Potential
Glycosylation2971N-linked (GlcNAc...); by host Potential
Glycosylation3061N-linked (GlcNAc...); by host Potential
Glycosylation3331N-linked (GlcNAc...); by host Potential
Glycosylation3371N-linked (GlcNAc...); by host Potential
Glycosylation3431N-linked (GlcNAc...); by host Potential
Glycosylation3791N-linked (GlcNAc...); by host Potential
Glycosylation3841N-linked (GlcNAc...); by host Potential
Glycosylation3911N-linked (GlcNAc...); by host Potential

Natural variations

Alternative sequence1631H → Q in isoform vMIA.
VSP_044014
Alternative sequence164 – 487324Missing in isoform vMIA.
VSP_044015
Alternative sequence178 – 26285Missing in isoform pUL37m.
VSP_044016

Secondary structure

.... 487
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform gpUL37 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: FA39A37C51FFB4A3

FASTA48756,125
        10         20         30         40         50         60 
MSPVYVNLLG SVGLLAFWYF SYRWIQRKRL EDPLPPWLRK KKACALTRRS RHRLRRQHGV 

        70         80         90        100        110        120 
IDGENSETER SVDLVAALLA EAGEESVTED TEREDTEEER EDEEEENEAR TPEVNPIDAE 

       130        140        150        160        170        180 
GLSGLAREAC EALKKALRRH RFLWQRRQRA RMLQHNGPQQ SHHAAVFCRV HGLRGFQVSV 

       190        200        210        220        230        240 
WLLLTLLWST GHGVSVRCTY HGTDVNRTSN TTSMNCHLNC TRNHTQIYNG PCLGTEARLP 

       250        260        270        280        290        300 
LNVTFNQSRR KWHSVMLKFG FQYHLEGWFP LRVLNESREI NVTEVHGEVA CFRNDTNVTV 

       310        320        330        340        350        360 
GQLTLNFTGH SYVLRAIAHT SPFESYVRWE ETNVTDNATS SENTTTVMST LTKYAESDYI 

       370        380        390        400        410        420 
FLQDMCPRFL KRTVKLTRNK TKHNVTVTGN NMTTLPVWTP ECKGWTYWTT LSVMWRNRRS 

       430        440        450        460        470        480 
ALLRAKSRAL GHWALLSICT VAAGSIALLS LFCILLIGLR RDLLEDFRYI CRDEGSSSTK 


NDVHRIV 

« Hide

Isoform vMIA [UniParc].

Checksum: B657342BB57AEC21
Show »

FASTA16319,115
Isoform pUL37m [UniParc].

Checksum: BDFD81E69DC4753E
Show »

FASTA40246,435

References

« Hide 'large scale' references
[1]"An immediate early gene of human cytomegalovirus encodes a potential membrane glycoprotein."
Kouzarides T., Bankier A.T., Satchwell S.C., Preddy E., Barrell B.G.
Virology 165:151-164(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of the protein-coding content of the sequence of human cytomegalovirus strain AD169."
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.
Curr. Top. Microbiol. Immunol. 154:125-169(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ISOFORM PUL37M, ISOFORM VMIA.
[3]"The human cytomegalovirus genome revisited: comparison with the chimpanzee cytomegalovirus genome."
Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J., McGeoch D.J., Hayward G.S.
J. Gen. Virol. 84:17-28(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
[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]"The human cytomegalovirus UL37 immediate-early regulatory protein is an integral membrane N-glycoprotein which traffics through the endoplasmic reticulum and Golgi apparatus."
Al-Barazi H.O., Colberg-Poley A.M.
J. Virol. 70:7198-7208(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"An anti-apoptotic viral protein that recruits Bax to mitochondria."
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.
J. Biol. Chem. 279:22605-22614(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HOST BAX.
[7]"Cytomegalovirus cell death suppressor vMIA blocks Bax- but not Bak-mediated apoptosis by binding and sequestering Bax at mitochondria."
Arnoult D., Bartle L.M., Skaletskaya A., Poncet D., Zamzami N., Park P.U., Sharpe J., Youle R.J., Goldmacher V.S.
Proc. Natl. Acad. Sci. U.S.A. 101:7988-7993(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Internal cleavage of the human cytomegalovirus UL37 immediate-early glycoprotein and divergent trafficking of its proteolytic fragments."
Mavinakere M.S., Colberg-Poley A.M.
J. Gen. Virol. 85:1989-1994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE SITE, SUBCELLULAR LOCATION.
[9]"Trafficking of UL37 proteins into mitochondrion-associated membranes during permissive human cytomegalovirus infection."
Bozidis P., Williamson C.D., Wong D.S., Colberg-Poley A.M.
J. Virol. 84:7898-7903(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Human cytomegalovirus directly induces the antiviral protein viperin to enhance infectivity."
Seo J.Y., Yaneva R., Hinson E.R., Cresswell P.
Science 332:1093-1097(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HOST RSAD2.
[11]"Human cytomegalovirus infection increases mitochondrial biogenesis."
Kaarbo M., Ager-Wick E., Osenbroch P.O., Kilander A., Skinnes R., Muller F., Eide L.
Mitochondrion 11:935-945(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17403 Genomic DNA. Translation: CAA35396.1.
BK000394 Genomic DNA. Translation: DAA00142.1.
PIRQQBEU5. S09801.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LR1NMR-B130-150[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60096N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR010880. Herpes_UL37_HHV-5-rel.
[Graphical view]
PfamPF07413. Herpes_UL37_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVGLI_HCMVA
AccessionPrimary (citable) accession number: P16778
Secondary accession number(s): P87887, Q7M6P6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: May 30, 2000
Last modified: February 19, 2014
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references