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P03322 (GAG_RSVP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gag-Pro polyprotein
Gene names
Name:gag-pro
OrganismRous sarcoma virus (strain Prague C) (RSV-PrC) [Complete proteome]
Taxonomic identifier11888 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeAlpharetrovirus
Virus hostGallus gallus (Chicken) [TaxID: 9031]

Protein attributes

Sequence length701 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Capsid protein p27 forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex By similarity.

The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell By similarity.

Subunit structure

The protease is active as a homodimer.

Subcellular location

Matrix protein p19: Virion Potential.

Capsid protein p27: Virion Potential.

Nucleocapsid protein p12: Virion Potential.

Domain

Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. P2B 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. Ref.4

Post-translational modification

Specific enzymatic cleavages in vivo yield mature proteins.

Sequence similarities

Contains 2 CCHC-type zinc fingers.

Contains 1 peptidase A2 domain.

Alternative products

This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]

Note: Translation results in the formation of the Gag-Pro. Ribosomal frameshifting at the gag-pro/pol genes boundary produces the Gag-Pro-Pol polyprotein.
Isoform Gag-Pro polyprotein (identifier: P03322-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Produced by conventional translation.
Isoform Gag-Pro-Pol polyprotein (identifier: P03354-1)

The sequence of this isoform can be found in the external entry P03354.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by -1 ribosomal frameshifting.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 155155Matrix protein p19
PRO_0000026113
Chain156 – 16611p2A
PRO_0000026114
Chain167 – 17711p2B
PRO_0000026115
Chain178 – 23962p10
PRO_0000026116
Chain240 – 479240Capsid protein p27
PRO_0000026117
Chain480 – 4889p3
PRO_0000026118
Chain489 – 57789Nucleocapsid protein p12
PRO_0000026119
Chain578 – 701124Protease p15
PRO_0000026120

Regions

Domain609 – 69082Peptidase A2
Zinc finger507 – 52418CCHC-type 1
Zinc finger533 – 55018CCHC-type 2
Motif172 – 1754PPXY motif
Compositional bias171 – 1744Poly-Pro

Sites

Active site6141For protease activity; shared with dimeric partner By similarity
Site155 – 1562Cleavage; by viral protease p15 By similarity
Site166 – 1672Cleavage; by viral protease p15 By similarity
Site177 – 1782Cleavage; by viral protease p15 By similarity
Site239 – 2402Cleavage; by viral protease p15 By similarity
Site479 – 4802Cleavage; by viral protease p15 By similarity
Site488 – 4892Cleavage; by viral protease p15 By similarity
Site577 – 5782Cleavage; by viral protease p15 By similarity

Experimental info

Sequence conflict5051A → S AA sequence Ref.2
Sequence conflict5361Q → E AA sequence Ref.2

Secondary structure

................................................................................... 701
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Gag-Pro polyprotein [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 5FD365D9CFEF37F1

FASTA70174,527
        10         20         30         40         50         60 
MEAVIKVISS ACKTYCGKTS PSKKEIGAML SLLQKEGLLM SPSDLYSPGS WDPITAALSQ 

        70         80         90        100        110        120 
RAMILGKSGE LKTWGLVLGA LKAAREEQVT SEQAKFWLGL GGGRVSPPGP ECIEKPATER 

       130        140        150        160        170        180 
RIDKGEEVGE TTVQRDAKMA PEETATPKTV GTSCYHCGTA IGCNCATASA PPPPYVGSGL 

       190        200        210        220        230        240 
YPSLAGVGEQ QGQGGDTPPG AEQSRAEPGH AGQAPGPALT DWARVREELA STGPPVVAMP 

       250        260        270        280        290        300 
VVIKTEGPAW TPLEPKLITR LADTVRTKGL RSPITMAEVE ALMSSPLLPH DVTNLMRVIL 

       310        320        330        340        350        360 
GPAPYALWMD AWGVQLQTVI AAATRDPRHP ANGQGRGERT NLNRLKGLAD GMVGNPQGQA 

       370        380        390        400        410        420 
ALLRPGELVA ITASALQAFR EVARLAEPAG PWADIMQGPS ESFVDFANRL IKAVEGSDLP 

       430        440        450        460        470        480 
PSARAPVIID CFRQKSQPDI QQLIRTAPST LTTPGEIIKY VLDRQKTAPL TDQGIAAAMS 

       490        500        510        520        530        540 
SAIQPLIMAV VNRERDGQTG SGGRARGLCY TCGSPGHYQA QCPKKRKSGN SRERCQLCNG 

       550        560        570        580        590        600 
MGHNAKQCRK RDGNQGQRPG KGLSSGPWPG PEPPAVSLAM TMEHKDRPLV RVILTNTGSH 

       610        620        630        640        650        660 
PVKQRSVYIT ALLDSGADIT IISEEDWPTD WPVMEAANPQ IHGIGGGIPM RKSRDMIELG 

       670        680        690        700 
VINRDGSLER PLLLFPAVAM VRGSILGRDC LQGLGLRLTN L 

« Hide

Isoform Gag-Pro-Pol polyprotein [UniParc].

See P03354.

References

[1]"Nucleotide sequence of Rous sarcoma virus."
Schwartz D., Tizard R., Gilbert W.
Cell 32:853-869(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Primary structure of Rous sarcoma virus RNA-associated polypeptide."
Misono K.S., Sharief F.S., Leis J.
Fed. Proc. 39:1611-1611(1980)
Cited for: PROTEIN SEQUENCE OF 489-577.
[3]"Comparative studies on the substrate specificity of avian myeloblastosis virus proteinase and lentiviral proteinases."
Tozser J., Bagossi P., Weber I.T., Copeland T.D., Oroszlan S.
J. Biol. Chem. 271:6781-6788(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[4]"Crystal structure of a retroviral protease proves relationship to aspartic protease family."
Miller M., Jaskolski M., Rao J.K.M., Leis J., Wlodawer A.
Nature 337:576-579(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF PROTEASE DOMAIN.
[5]"Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus."
McDonnell J.M., Fushman D., Cahill S.M., Zhou W., Wolven A., Wilson C.B., Nelle T.D., Resh M.D., Wills J., Cowburn D.
J. Mol. Biol. 279:921-928(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-87.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02342 Genomic RNA. Translation: AAB59932.1.
V01197 Genomic DNA. Translation: CAA24512.1.
PIRFOFV1R. A90834.
RefSeqNP_056887.1. NC_001407.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A6SNMR-A2-87[»]
1BAIX-ray2.40A/B578-701[»]
1EM9X-ray2.05A/B240-393[»]
1EOQNMR-A394-488[»]
1P7NX-ray2.60A215-386[»]
2IHXNMR-A503-563[»]
2RSPX-ray2.00A/B578-701[»]
2X8Qelectron microscopy18.30A240-465[»]
3G0VX-ray2.00A389-465[»]
3G1GX-ray2.01A/B390-476[»]
3G1IX-ray2.10A/B389-465[»]
3G21X-ray0.90A389-465[»]
3G26X-ray1.55A389-465[»]
3G28X-ray1.64A389-465[»]
3G29X-ray2.50A/B389-465[»]
ProteinModelPortalP03322.
SMRP03322. Positions 2-87, 214-469, 503-552, 578-701.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-6616346.

Protein family/group databases

MEROPSA02.015.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1491923.

Family and domain databases

Gene3D1.10.1200.30. 1 hit.
1.10.150.90. 1 hit.
1.10.375.10. 1 hit.
2.40.70.10. 1 hit.
4.10.60.10. 1 hit.
InterProIPR001969. Aspartic_peptidase_AS.
IPR004028. Gag_M.
IPR000721. Gag_p24.
IPR012344. Matrix_N_HIV/RSV.
IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR001878. Znf_CCHC.
[Graphical view]
PfamPF00607. Gag_p24. 1 hit.
PF02813. Retro_M. 1 hit.
PF00077. RVP. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
ProDomPD002871. Gag_M. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMSSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP03322.

Entry information

Entry nameGAG_RSVP
AccessionPrimary (citable) accession number: P03322
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 116 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

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references