B2MW50 (Z_PARVP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Zinc-binding protein

Gene names

Name:

Z

Organism

Parana virus (isolate Rat/Paraguay/12056/1965) (PARV) [Complete proteome]

Taxonomic identifier

45222 [NCBI]

Taxonomic lineage

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

Virus host

Oryzomys angouya (Paraguayan rice rat) (Oryzomys buccinatus) [TaxID: 530180]

Protein attributes

Sequence length	95 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. 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 By similarity.
Subunit structure	Interacts with protein N; this interaction probably directs the encapsidated genome to budding sites. Interacts (via RING domain) with polymerase L; this interaction inhibits viral transcription and replication. Interacts with the glycoprotein complex; this interaction plays a role in virion budding.
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 By similarity.
Domain	The RING finger domain is essential for the inhibitory activity of protein Z in transcription and RNA replication By similarity. 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 PSAP motif that may be sufficient to mediate budding By similarity.
Sequence similarities	Belongs to the arenaviridae Z protein family. Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Host-virus interaction Inhibition of host IFN-mediated response initiation by virus Inhibition of host RIG-I by virus Inhibition of host innate immune response by virus Viral budding Viral budding via the host ESCRT complexes Viral immunoevasion 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
Gene Ontology (GO)
Biological_process	suppression by virus of host RIG-I activity Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host type I interferon production Inferred from electronic annotation. Source: UniProtKB-KW viral release from host cell 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	1	1	Removed; by host By similarity
	Chain	2 – 95	94	RING finger protein Z		PRO_0000361038
Regions
	Zinc finger	38 – 74	37	RING-type; atypical
	Motif	88 – 91	4	PTAP/PSAP motif
Amino acid modifications
	Lipidation	2	1	N-myristoyl glycine; by host By similarity

Sequences

	Sequence		Length	Mass (Da)
	B2MW50 [UniParc]. Last modified June 10, 2008. Version 1. Checksum: 44D99FB07D4B75CD	FASTA	95	10,650
	10 20 30 40 50 60 MGLRYSKAVK DKYGDREIEG RATMTLNLPQ GLYGRFNCKR CWFATKGLIA CSDHYLCLNC 70 80 90 LTIMLSDGNF CEVCGKTLPK KIVFEESPSA PPYDG

References

[1]	"Phylogeny of the genus Arenavirus." Charrel R.N., de Lamballerie X., Emonet S. Curr. Opin. Microbiol. 11:362-368(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	EU627613 Genomic RNA. Translation: ACC94301.1.
RefSeq	YP_001936027.1. NC_010761.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6334529.
Family and domain databases
InterPro	IPR003224. Znf_P11. [Graphical view]
Pfam	PF03854. zf-P11. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Z_PARVP

Accession

Primary (citable) accession number: B2MW50

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	June 10, 2008
Last modified:	April 3, 2013
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program