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P16778

- VGLI_HCMVA

UniProt

P16778 - VGLI_HCMVA

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Protein

UL37 immediate early glycoprotein

Gene

UL37

Organism
Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.
Isoform gpUL37 may play a role in escape from the host antiviral response.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei193 – 1942Cleavage site

GO - Biological processi

  1. modulation by virus of host apoptotic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Modulation of host cell apoptosis by virus

Names & Taxonomyi

Protein namesi
Recommended name:
UL37 immediate early glycoprotein
Gene namesi
Name:UL37
OrganismiHuman cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Taxonomic identifieri10360 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeBetaherpesvirinaeCytomegalovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000008991: Genome, UP000008992: Genome

Subcellular locationi

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.
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei433 – 45927HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell endoplasmic reticulum Source: UniProtKB-KW
  2. host cell Golgi apparatus Source: UniProtKB-KW
  3. host cell membrane Source: UniProtKB-KW
  4. host cell mitochondrion Source: UniProtKB-KW
  5. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host endoplasmic reticulum, Host Golgi apparatus, Host membrane, Host mitochondrion, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 487465UL37 immediate early glycoproteinPRO_0000037455Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi206 – 2061N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi210 – 2101N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi219 – 2191N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi223 – 2231N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi242 – 2421N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi246 – 2461N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi275 – 2751N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi281 – 2811N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi294 – 2941N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi297 – 2971N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi306 – 3061N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi333 – 3331N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi337 – 3371N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi343 – 3431N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi379 – 3791N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi384 – 3841N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi391 – 3911N-linked (GlcNAc...); by hostSequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

DIPiDIP-60096N.

Structurei

Secondary structure

1
487
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi138 – 1458Combined sources
Beta strandi146 – 1483Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LR1NMR-B130-150[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi97 – 10812Poly-GluAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR010880. Herpes_UL37_HHV-5-rel.
[Graphical view]
PfamiPF07413. Herpes_UL37_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform gpUL37 (identifier: P16778-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSPVYVNLLG SVGLLAFWYF SYRWIQRKRL EDPLPPWLRK KKACALTRRS
60 70 80 90 100
RHRLRRQHGV IDGENSETER SVDLVAALLA EAGEESVTED TEREDTEEER
110 120 130 140 150
EDEEEENEAR TPEVNPIDAE GLSGLAREAC EALKKALRRH RFLWQRRQRA
160 170 180 190 200
RMLQHNGPQQ SHHAAVFCRV HGLRGFQVSV WLLLTLLWST GHGVSVRCTY
210 220 230 240 250
HGTDVNRTSN TTSMNCHLNC TRNHTQIYNG PCLGTEARLP LNVTFNQSRR
260 270 280 290 300
KWHSVMLKFG FQYHLEGWFP LRVLNESREI NVTEVHGEVA CFRNDTNVTV
310 320 330 340 350
GQLTLNFTGH SYVLRAIAHT SPFESYVRWE ETNVTDNATS SENTTTVMST
360 370 380 390 400
LTKYAESDYI FLQDMCPRFL KRTVKLTRNK TKHNVTVTGN NMTTLPVWTP
410 420 430 440 450
ECKGWTYWTT LSVMWRNRRS ALLRAKSRAL GHWALLSICT VAAGSIALLS
460 470 480
LFCILLIGLR RDLLEDFRYI CRDEGSSSTK NDVHRIV
Length:487
Mass (Da):56,125
Last modified:May 30, 2000 - v2
Checksum:iFA39A37C51FFB4A3
GO
Isoform vMIA (identifier: P16778-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     163-163: H → Q
     164-487: Missing.

Show »
Length:163
Mass (Da):19,115
Checksum:iB657342BB57AEC21
GO
Isoform pUL37m (identifier: P16778-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:402
Mass (Da):46,435
Checksum:iBDFD81E69DC4753E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei163 – 1631H → Q in isoform vMIA. CuratedVSP_044014
Alternative sequencei164 – 487324Missing in isoform vMIA. CuratedVSP_044015Add
BLAST
Alternative sequencei178 – 26285Missing in isoform pUL37m. CuratedVSP_044016Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17403 Genomic DNA. Translation: CAA35396.1.
BK000394 Genomic DNA. Translation: DAA00142.1.
PIRiS09801. QQBEU5.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17403 Genomic DNA. Translation: CAA35396.1 .
BK000394 Genomic DNA. Translation: DAA00142.1 .
PIRi S09801. QQBEU5.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LR1 NMR - B 130-150 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60096N.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR010880. Herpes_UL37_HHV-5-rel.
[Graphical view ]
Pfami PF07413. Herpes_UL37_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "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.
  5. Cited for: FUNCTION, INTERACTION WITH HOST BAX.
  6. "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.
  7. "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.
  8. "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.
  9. "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.
  10. "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.

Entry informationi

Entry nameiVGLI_HCMVA
AccessioniPrimary (citable) accession number: P16778
Secondary accession number(s): P87887, Q7M6P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: May 30, 2000
Last modified: November 26, 2014
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3