RING finger protein Z - Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV)

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P18541 (Z_LYCVA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 81. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
RING finger protein Z
Short name=Protein Z

Alternative name(s):
Zinc-binding protein

Gene names

Name:

Organism

Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV) [Reference proteome]

Taxonomic identifier

11624 [NCBI]

Taxonomic lineage

Viruses › ssRNA negative-strand viruses › Arenaviridae › Arenavirus › Old world arenaviruses ›

Virus host

Homo sapiens (Human) [TaxID: 9606]
Mesocricetus auratus (Golden hamster) [TaxID: 10036]
Mus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length	90 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L By similarity. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. Ref.7
Subunit structure	Interacts with protein NP; this interaction probably directs the encapsidated genome to budding sites By similarity. Interacts (via RING domain) with polymerase L; this interaction inhibits viral transcription and replication By similarity. Interacts with the glycoprotein complex; this interaction plays a role in virion budding. Interacts with host eIF4E; this interaction results in eIF4E reduced affinity for its substrate, the 5'-m7 G cap structure. Interacts (via late-budding domain) with host TSG101; this interaction is essential for budding and release of viral particles. Interacts with host RPLP0; this interaction may serve to load ribosome-like particles inside the virion. Interacts with host PML; this interaction induces PML bodies redistribution in the cytoplasm upon viral infection. Ref.4 Ref.5 Ref.9
Subcellular location	Virion. Host cytoplasm › host perinuclear region. Host cell membrane; Lipid-anchor; Cytoplasmic side. Note: Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells.
Domain	The RING finger domain is essential for the inhibitory activity of protein Z in transcription and RNA replication. Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. Ring-finger protein Z contains one L domain: a PPXY motif which probably binds to the WW domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases By similarity.
Sequence similarities	Belongs to the arenaviridae Z protein family. Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Host-virus interaction Viral budding Viral budding via the host ESCRT complexes Virus exit from host cell
Cellular component	Host cell membrane Host cytoplasm Host membrane Membrane Virion
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Lipoprotein Myristate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	viral release from host cell Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	host cell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-KW virion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed; by host

Chain

2 – 90

RING finger protein Z

PRO_0000079202

Regions

Zinc finger

32 – 68

RING-type; atypical

Motif

85 – 88

PPXY motif

Amino acid modifications

Lipidation

N-myristoyl glycine; by host Ref.8

Experimental info

Mutagenesis

G → A: Complete loss of myristoylation. Complete loss of virion budding. Ref.8

Mutagenesis

C → F: Complete loss of inhibitory activity on viral RNA synthesis; when associated with G-35. Ref.6

Mutagenesis

C → G: Complete loss of inhibitory activity on viral RNA synthesis; when associated with F-32. Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P18541 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D25AF9EC2287E4EA
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FASTA

10,184

        10         20         30         40         50         60 
MGQGKSREEK GTNSTNRAEI LPDTTYLGPL SCKSCWQKFD SLVRCHDHYL CRHCLNLLLS 

        70         80         90 
VSDRCPLCKY PLPTRLKIST APSSPPPYEE

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References

[1]	"The completed sequence of lymphocytic choriomeningitis virus reveals a unique RNA structure and a gene for a zinc finger protein." Salvato M.S., Shimomaye E.M. Virology 173:1-10(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Mutagenesis-induced, large fitness variations with an invariant arenavirus consensus genomic nucleotide sequence." Grande-Perez A., Gomez-Mariano G., Lowenstein P.R., Domingo E. J. Virol. 79:10451-10459(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate Armstrong 53b.
[3]	"Recovery of an arenavirus entirely from RNA polymerase I/II-driven cDNA." Flatz L., Bergthaler A., de la Torre J.C., Pinschewer D.D. Proc. Natl. Acad. Sci. U.S.A. 103:4663-4668(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate Armstrong-derived variant Cl13.
[4]	"Two RING finger proteins, the oncoprotein PML and the arenavirus Z protein, colocalize with the nuclear fraction of the ribosomal P proteins." Borden K.L., Campbell-Dwyer E.J., Carlile G.W., Djavani M., Salvato M.S. J. Virol. 72:3819-3826(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HOST RPLP0 AND HOST PML.
[5]	"The lymphocytic choriomeningitis virus RING protein Z associates with eukaryotic initiation factor 4E and selectively represses translation in a RING-dependent manner." Campbell-Dwyer E.J., Lai H., MacDonald R.C., Salvato M.S., Borden K.L. J. Virol. 74:3293-3300(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HOST EIF4E.
[6]	"RING finger Z protein of lymphocytic choriomeningitis virus (LCMV) inhibits transcription and RNA replication of an LCMV S-segment minigenome." Cornu T.I., de la Torre J.C. J. Virol. 75:9415-9426(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-32 AND CYS-35.
[7]	"Characterization of the arenavirus RING finger Z protein regions required for Z-mediated inhibition of viral RNA synthesis." Cornu T.I., de la Torre J.C. J. Virol. 76:6678-6688(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Myristoylation of the RING finger Z protein is essential for arenavirus budding." Perez M., Greenwald D.L., de la Torre J.C. J. Virol. 78:11443-11448(2004) [PubMed] [Europe PMC] [Abstract] Cited for: MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2.
[9]	"Arenavirus Z-glycoprotein association requires Z myristoylation but not functional RING or late domains." Capul A.A., Perez M., Burke E., Kunz S., Buchmeier M.J., de la Torre J.C. J. Virol. 81:9451-9460(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GLYCOPROTEIN COMPLEX GPC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M27693 Genomic RNA. Translation: AAA46268.1. AY847351 Genomic RNA. Translation: AAX49343.1. DQ361066 Genomic RNA. Translation: ABC96003.1.
PIR	ZNXPLC. A32592.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-59720N.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR024183. RING_finger_Z_arenaviridae. IPR003224. Znf_P11. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF03854. zf-P11. 1 hit. [Graphical view]
PIRSF	PIRSF004030. Z_ArenaV. 1 hit.
PROSITE	PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Z_LYCVA

Accession

Primary (citable) accession number: P18541
Secondary accession number(s): Q49K85

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 81 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents