Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

RING finger protein Z

Gene

Z

Organism
Sabia mammarenavirus (isolate Human/Brasil/SPH114202/1990) (SABV) (Sabi mammarenavirus)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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. 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.UniRule annotation

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri43 – 79RING-type; atypicalUniRule annotationAdd BLAST37

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processHost-virus interaction, Viral budding, Viral budding via the host ESCRT complexes, Viral release from host cell
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
RING finger protein ZUniRule annotation
Short name:
Protein ZUniRule annotation
Alternative name(s):
Zinc-binding proteinUniRule annotation
Gene namesi
Name:ZUniRule annotation
OrganismiSabia mammarenavirus (isolate Human/Brasil/SPH114202/1990) (SABV) (Sabi mammarenavirus)
Taxonomic identifieri45709 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesArenaviridaeMammarenavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000009267 Componenti: Genome

Subcellular locationi

  • Virion UniRule annotation
  • host perinuclear region UniRule annotation
  • Host cell membrane UniRule annotation; Lipid-anchor UniRule annotation; Cytoplasmic side UniRule annotation
  • Note: Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells.UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host cytoplasm, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostUniRule annotation
ChainiPRO_00003610402 – 100RING finger protein ZUniRule annotationAdd BLAST99

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostUniRule annotation1

Keywords - PTMi

Lipoprotein, Myristate

Interactioni

Subunit structurei

Interacts with protein NP; 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. 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.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
DDX58O957862EBI-3647496,EBI-995350From Homo sapiens.

Protein-protein interaction databases

IntActiQ6UY62, 1 interactor

Structurei

3D structure databases

SMRiQ6UY62
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi93 – 96PTAP/PSAP motifUniRule annotation4

Domaini

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.UniRule annotation

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri43 – 79RING-type; atypicalUniRule annotationAdd BLAST37

Keywords - Domaini

Zinc-finger

Phylogenomic databases

OrthoDBiVOG090001O4

Family and domain databases

Gene3Di3.30.160.310, 1 hit
HAMAPiMF_04087 ARENA_Z, 1 hit
InterProiView protein in InterPro
IPR024183 RING_finger_Z_arenaviridae
IPR038485 Z_RING-type_Znf_sf
IPR003224 Z_RING_Znf
PfamiView protein in Pfam
PF03854 zf-P11, 1 hit
PIRSFiPIRSF004030 Z_ArenaV, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q6UY62-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNSKSKSKL SANQYEQQTV NSTKQVAILK RQAEPSLYGR HNCRCCWFAN
60 70 80 90 100
TNLIKCSDHY ICLKCLNIML GKSSFCDICG EELPTSIVVP IEPSAPPPED
Length:100
Mass (Da):11,123
Last modified:July 5, 2004 - v1
Checksum:i544CCC8FDDD891AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358026 Genomic RNA Translation: AAQ55262.1
AY216506 Genomic RNA Translation: ABY59837.1
RefSeqiYP_089659.1, NC_006313.1

Genome annotation databases

GeneIDi3077249
KEGGivg:3077249

Similar proteinsi

Entry informationi

Entry nameiZ_SABVB
AccessioniPrimary (citable) accession number: Q6UY62
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: July 5, 2004
Last modified: April 25, 2018
This is version 58 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health