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P10215 (UL31_HHV11) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Virion egress protein UL31
Alternative name(s):
Primary envelopment factor UL31
Gene names
Name:UL31
OrganismHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) [Reference proteome]
Taxonomic identifier10299 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a major role in virion nuclear egress, the first step of virion release from infected cell. Viral capsids are initially assembled within the nucleus, UL31/UL34 complex induces capsids budding and envelopment into the perinuclear space. Then UL31/UL34 complex promotes fusion of perinuclear virion envelope with the outer nuclear membrane, releasing viral capsid into the cytoplasm where it will engages budding sites in the Golgi or trans-Golgi network. Ref.4 Ref.5

Subunit structure

Forms a complex with UL34, which interacts with glycoprotein D. This interaction recruits glycoprotein D and glycoprotein M to the inner nuclear membrane. Ref.2 Ref.6 Ref.7 Ref.10

Subcellular location

Host nucleus inner membrane. Note: Remains attached to the nucleus inner membrane through interaction with UL34. Localizes also at the transient membrane of perinuclear virions. Ref.3 Ref.8

Post-translational modification

Phosphorylated on N-terminus serine residues by viral kinase US3. This phosphorylation regulates the localization within the inner nuclear membrane. Ref.9

Sequence similarities

Belongs to the herpesviridae UL31 family.

Ontologies

Keywords
   Cellular componentHost membrane
Host nucleus
Membrane
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componenthost cell nuclear inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 306306Virion egress protein UL31
PRO_0000116006

Sequences

Sequence LengthMass (Da)Tools
P10215 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: D4FE0FD98D934C46

FASTA30633,953
        10         20         30         40         50         60 
MYDTDPHRRG SRPGPYHGKE RRRSRSSAAG GTLGVVRRAS RKSLPPHARK QELCLHERQR 

        70         80         90        100        110        120 
YRGLFAALAQ TPSEEIAIVR SLSVPLVKTT PVSLPFCLDQ TVADNCLTLS GMGYYLGIGG 

       130        140        150        160        170        180 
CCPACNAGDG RFAATSREAL ILAFVQQINT IFEHRAFLAS LVVLADRHNA PLQDLLAGIL 

       190        200        210        220        230        240 
GQPELFFVHT ILRGGGACDP RLLFYPDPTY GGHMLYVIFP GTSAHLHYRL IDRMLTACPG 

       250        260        270        280        290        300 
YRFVAHVWQS TFVLVVRRNA EKPTDAEIPT VSAADIYCKM RDISFDGGLM LEYQRLYATF 


DEFPPP 

« Hide

References

[1]"The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1."
McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P.
J. Gen. Virol. 69:1531-1574(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"U(L)31 and U(L)34 proteins of herpes simplex virus type 1 form a complex that accumulates at the nuclear rim and is required for envelopment of nucleocapsids."
Reynolds A.E., Ryckman B.J., Baines J.D., Zhou Y., Liang L., Roller R.J.
J. Virol. 75:8803-8817(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UL34.
[3]"Ultrastructural localization of the herpes simplex virus type 1 UL31, UL34, and US3 proteins suggests specific roles in primary envelopment and egress of nucleocapsids."
Reynolds A.E., Wills E.G., Roller R.J., Ryckman B.J., Baines J.D.
J. Virol. 76:8939-8952(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[4]"Conformational changes in the nuclear lamina induced by herpes simplex virus type 1 require genes U(L)31 and U(L)34."
Reynolds A.E., Liang L., Baines J.D.
J. Virol. 78:5564-5575(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Herpes simplex virus 1 U(L)31 and U(L)34 gene products promote the late maturation of viral replication compartments to the nuclear periphery."
Simpson-Holley M., Baines J., Roller R., Knipe D.M.
J. Virol. 78:5591-5600(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Identification of an essential domain in the herpes simplex virus 1 UL34 protein that is necessary and sufficient to interact with UL31 protein."
Liang L., Baines J.D.
J. Virol. 79:3797-3806(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UL34.
[7]"Common and specific properties of herpesvirus UL34/UL31 protein family members revealed by protein complementation assay."
Schnee M., Ruzsics Z., Bubeck A., Koszinowski U.H.
J. Virol. 80:11658-11666(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UL34.
[8]"Herpes simplex virus 1-encoded protein kinase UL13 phosphorylates viral Us3 protein kinase and regulates nuclear localization of viral envelopment factors UL34 and UL31."
Kato A., Yamamoto M., Ohno T., Tanaka M., Sata T., Nishiyama Y., Kawaguchi Y.
J. Virol. 80:1476-1486(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Phosphorylation of the UL31 protein of herpes simplex virus 1 by the US3-encoded kinase regulates localization of the nuclear envelopment complex and egress of nucleocapsids."
Mou F., Wills E., Baines J.D.
J. Virol. 83:5181-5191(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[10]"The U(L)31 and U(L)34 gene products of herpes simplex virus 1 are required for optimal localization of viral glycoproteins D and M to the inner nuclear membranes of infected cells."
Wills E., Mou F., Baines J.D.
J. Virol. 83:4800-4809(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GLYCOPROTEIN D.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14112 Genomic DNA. Translation: CAA32324.1.
PIRWMBEH1. D30085.
RefSeqNP_044633.1. NC_001806.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

MINTMINT-224098.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2703350.

Phylogenomic databases

ProtClustDBPHA3328.

Family and domain databases

InterProIPR021152. Herpes_UL31.
[Graphical view]
PfamPF02718. Herpes_UL31. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUL31_HHV11
AccessionPrimary (citable) accession number: P10215
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 3, 2013
This is version 47 of the entry and version 1 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