P20919 (REV_EIAVY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein Rev

Alternative name(s):
3'-ORF protein

Gene names

Name:

rev

Organism

Equine infectious anemia virus (strain Wyoming) (EIAV)

Taxonomic identifier

11672 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Lentivirus › Equine lentivirus group › Equine infectious anemia virus

Virus host

Equus asinus (Donkey) [TaxID: 9793]
Equus caballus (Horse) [TaxID: 9796]

Protein attributes

Sequence length	165 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre-mRNAs carry two recognition sequences that function as Rev responsive element (RRE), that are not present in fully spliced viral mRNAs (early transcripts). This function is essential since most viral proteins are translated from unspliced or partially spliced pre-mRNAs which cannot exit the nucleus by the pathway used by fully processed cellular mRNAs By similarity.
Subunit structure	Homomultimer; when bound to the RRE. Multimeric assembly is essential for activity By similarity.
Subcellular location	Host nucleus › host nucleolus. Host cytoplasm. Note: The presence of both nuclear import and nuclear export signals leads to continuous shuttling between the nucleus and cytoplasm Probable. Ref.5
Domain	The bipartite RNA-binding motif binds to the RREs present in incompletely spliced viral pre-mRNAs. It consists of a central region, and a C-terminal region that also contains the NLS which mediates nuclear localization. These overlapping functions prevent Rev bound to RRE from undesirable return to the nucleus. When Rev binds the RRE, the NLS becomes masked while the NES remains accessible.
Sequence caution	The sequence AAA43027.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transport mRNA transport
Cellular component	Host cytoplasm Host nucleus
Domain	Coiled coil
Ligand	RNA-binding
Gene Ontology (GO)
Biological_process	mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell host cell nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell viral capsid Inferred from electronic annotation. Source: InterPro
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 165	165	Protein Rev		PRO_0000085478
Regions
	Region	57 – 130	74	RNA-binding (RRE)
	Region	144 – 165	22	RNA-binding (RRE)
	Coiled coil	1 – 26	26	Potential
	Motif	32 – 55	24	Nuclear export signal Probable
	Motif	159 – 163	5	Nuclear localization signal
Experimental info
	Mutagenesis	159	1	K → A: Complete loss of nuclear import; when associated with A-160. Ref.5
	Mutagenesis	160	1	R → A: Complete loss of nuclear import; when associated with A-159 or A-161. Ref.5
	Mutagenesis	161	1	R → A: Complete loss of nuclear import; when associated with A-160 or A-162. Ref.5
	Mutagenesis	162	1	R → A: Complete loss of nuclear import; when associated with A-161 or A-163. Ref.5
	Mutagenesis	163	1	K → A: Complete loss of nuclear import; when associated with A-162. Ref.5
	Sequence conflict	30	1	K → I Ref.2
	Sequence conflict	59	1	C → Y in AAA43027. Ref.2
	Sequence conflict	88	1	T → A in AAA43027. Ref.2
	Sequence conflict	114	1	R → Q in AAA43027. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P20919 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 04FDEB0830888F36	FASTA	165	19,810
	10 20 30 40 50 60 MAESKEARDQ EMNLKEESKE EKRRNDWWKK DPQGPLESDQ WCRVLRQSLP EEKIPSQTCI 70 80 90 100 110 120 ARRHLGPGPT QHTPSRRDRW IRGQILQTEV LQERLEWRIR GVQQAAKELG EVNRGIWREL 130 140 150 160 YFREDQRGDF SAWGGYQRAQ ERLWGEQSSP RVLRPGDSKR RRKHL

References

[1]	"Identification of sequences encoding the equine infectious anemia virus tat gene." Noiman S., Gazit A., Tori O., Sherman L., Miki T., Tronick S.R., Yaniv A. Virology 176:280-288(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Cloning and characterization of cDNAs encoding equine infectious anemia virus tat and putative Rev proteins." Stephens R.M., Derse D., Rice N.R. J. Virol. 64:3716-3725(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]	"Identification of the activation domain of equine infectious anemia virus rev." Fridell R.A., Partin K.M., Carpenter S., Cullen B.R. J. Virol. 67:7317-7323(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEAR EXPORT SIGNAL.
[4]	"Nuclear transport of human immunodeficiency virus type 1, visna virus, and equine infectious anemia virus Rev proteins: identification of a family of transferable nuclear export signals." Meyer B.E., Meinkoth J.L., Malim M.H. J. Virol. 70:2350-2359(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEAR EXPORT SIGNAL.
[5]	"Characterization of functional domains of equine infectious anemia virus Rev suggests a bipartite RNA-binding domain." Lee J.-H., Murphy S.C., Belshan M., Sparks W.O., Wannemuehler Y., Liu S., Hope T.J., Dobbs D., Carpenter S. J. Virol. 80:3844-3852(2006) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, RNA-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-159; ARG-160; ARG-161; ARG-162 AND LYS-163.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M36592 Genomic RNA. Translation: AAB02404.1. M54797 Genomic RNA. Translation: AAA43027.1. Different initiation.
PIR	ASLJ22. B46357.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR021311. EIAV_Rev. IPR001361. Gp90_EIAV. [Graphical view]
Pfam	PF00971. EIAV_GP90. 1 hit. PF11129. EIAV_Rev. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

REV_EIAVY

Accession

Primary (citable) accession number: P20919

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	April 3, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program