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P03322

- GAG_RSVP

UniProt

P03322 - GAG_RSVP

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Protein

Gag-Pro polyprotein

Gene
gag-pro
Organism
Rous sarcoma virus (strain Prague C) (RSV-PrC)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei155 – 1562Cleavage; by viral protease p15 By similarity
Sitei166 – 1672Cleavage; by viral protease p15 By similarity
Sitei177 – 1782Cleavage; by viral protease p15 By similarity
Sitei239 – 2402Cleavage; by viral protease p15 By similarity
Sitei479 – 4802Cleavage; by viral protease p15 By similarity
Sitei488 – 4892Cleavage; by viral protease p15 By similarity
Sitei577 – 5782Cleavage; by viral protease p15 By similarity
Active sitei614 – 6141For protease activity; shared with dimeric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri507 – 52418CCHC-type 1Add
BLAST
Zinc fingeri533 – 55018CCHC-type 2Add
BLAST

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB-KW
  2. nucleic acid binding Source: InterPro
  3. structural constituent of virion Source: UniProtKB-KW
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. viral process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiA02.015.

Names & Taxonomyi

Protein namesi
Recommended name:
Gag-Pro polyprotein
Cleaved into the following 8 chains:
Gene namesi
Name:gag-pro
OrganismiRous sarcoma virus (strain Prague C) (RSV-PrC)
Taxonomic identifieri11888 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeAlpharetrovirus
Virus hostiGallus gallus (Chicken) [TaxID: 9031]
ProteomesiUP000007183: Genome

Subcellular locationi

Chain Matrix protein p19 : Virion Reviewed prediction
Chain Capsid protein p27 : Virion Reviewed prediction

GO - Cellular componenti

  1. viral capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Viral matrix protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 155155Matrix protein p19PRO_0000026113Add
BLAST
Chaini156 – 16611p2APRO_0000026114Add
BLAST
Chaini167 – 17711p2BPRO_0000026115Add
BLAST
Chaini178 – 23962p10PRO_0000026116Add
BLAST
Chaini240 – 479240Capsid protein p27PRO_0000026117Add
BLAST
Chaini480 – 4889p3PRO_0000026118
Chaini489 – 57789Nucleocapsid protein p12PRO_0000026119Add
BLAST
Chaini578 – 701124Protease p15PRO_0000026120Add
BLAST

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins.

Interactioni

Subunit structurei

The protease is active as a homodimer.

Protein-protein interaction databases

MINTiMINT-6616346.

Structurei

Secondary structure

1
701
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1615
Turni17 – 193
Helixi25 – 317
Helixi33 – 353
Helixi42 – 465
Turni48 – 514
Helixi52 – 609
Turni61 – 633
Beta strandi67 – 715
Helixi72 – 8615
Helixi222 – 2309
Beta strandi234 – 2363
Beta strandi241 – 2433
Beta strandi245 – 2506
Helixi255 – 26814
Helixi273 – 28210
Helixi289 – 29911
Helixi302 – 32524
Beta strandi334 – 3374
Helixi342 – 3454
Turni350 – 3545
Helixi356 – 3627
Helixi365 – 38521
Helixi392 – 3943
Helixi403 – 41513
Beta strandi417 – 4193
Helixi421 – 4233
Helixi424 – 43512
Helixi438 – 4447
Helixi454 – 4629
Beta strandi579 – 5813
Beta strandi584 – 5863
Beta strandi589 – 5968
Beta strandi605 – 6139
Beta strandi621 – 6233
Turni624 – 6263
Beta strandi633 – 6353
Beta strandi650 – 6556
Beta strandi657 – 6626
Beta strandi672 – 6743
Beta strandi677 – 6804
Beta strandi682 – 6865
Helixi688 – 6936
Beta strandi697 – 6993

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP03322.
SMRiP03322. Positions 2-87, 214-469, 503-552, 578-701.

Miscellaneous databases

EvolutionaryTraceiP03322.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini609 – 69082Peptidase A2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi172 – 1754PPXY motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi171 – 1744Poly-Pro

Domaini

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.1 Publication

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri507 – 52418CCHC-type 1Add
BLAST
Zinc fingeri533 – 55018CCHC-type 2Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Family and domain databases

Gene3Di1.10.1200.30. 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.
InterProiIPR001969. 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]
PfamiPF00607. Gag_p24. 1 hit.
PF02813. Retro_M. 1 hit.
PF00077. RVP. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
ProDomiPD002871. Gag_M. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by ribosomal frameshifting. Align

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) [UniParc]FASTAAdd to Basket

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.

« Hide

MEAVIKVISS ACKTYCGKTS PSKKEIGAML SLLQKEGLLM SPSDLYSPGS    50
WDPITAALSQ RAMILGKSGE LKTWGLVLGA LKAAREEQVT SEQAKFWLGL 100
GGGRVSPPGP ECIEKPATER RIDKGEEVGE TTVQRDAKMA PEETATPKTV 150
GTSCYHCGTA IGCNCATASA PPPPYVGSGL YPSLAGVGEQ QGQGGDTPPG 200
AEQSRAEPGH AGQAPGPALT DWARVREELA STGPPVVAMP VVIKTEGPAW 250
TPLEPKLITR LADTVRTKGL RSPITMAEVE ALMSSPLLPH DVTNLMRVIL 300
GPAPYALWMD AWGVQLQTVI AAATRDPRHP ANGQGRGERT NLNRLKGLAD 350
GMVGNPQGQA ALLRPGELVA ITASALQAFR EVARLAEPAG PWADIMQGPS 400
ESFVDFANRL IKAVEGSDLP PSARAPVIID CFRQKSQPDI QQLIRTAPST 450
LTTPGEIIKY VLDRQKTAPL TDQGIAAAMS SAIQPLIMAV VNRERDGQTG 500
SGGRARGLCY TCGSPGHYQA QCPKKRKSGN SRERCQLCNG MGHNAKQCRK 550
RDGNQGQRPG KGLSSGPWPG PEPPAVSLAM TMEHKDRPLV RVILTNTGSH 600
PVKQRSVYIT ALLDSGADIT IISEEDWPTD WPVMEAANPQ IHGIGGGIPM 650
RKSRDMIELG VINRDGSLER PLLLFPAVAM VRGSILGRDC LQGLGLRLTN 700
L 701

Note: Produced by conventional translation.

Length:701
Mass (Da):74,527
Last modified:July 21, 1986 - v1
Checksum:i5FD365D9CFEF37F1
GO
Isoform Gag-Pro-Pol polyprotein (identifier: P03354-1) [UniParc]FASTAAdd to Basket

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.

Length:1,603
Mass (Da):173,881
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti505 – 5051A → S AA sequence 1 Publication
Sequence conflicti536 – 5361Q → E AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02342 Genomic RNA. Translation: AAB59932.1.
V01197 Genomic DNA. Translation: CAA24512.1.
PIRiA90834. FOFV1R.
RefSeqiNP_056887.1. NC_001407.1.

Genome annotation databases

GeneIDi1491923.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02342 Genomic RNA. Translation: AAB59932.1 .
V01197 Genomic DNA. Translation: CAA24512.1 .
PIRi A90834. FOFV1R.
RefSeqi NP_056887.1. NC_001407.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A6S NMR - A 2-87 [» ]
1BAI X-ray 2.40 A/B 578-701 [» ]
1EM9 X-ray 2.05 A/B 240-393 [» ]
1EOQ NMR - A 394-488 [» ]
1P7N X-ray 2.60 A 215-386 [» ]
2IHX NMR - A 503-563 [» ]
2RSP X-ray 2.00 A/B 578-701 [» ]
2X8Q electron microscopy 18.30 A 240-465 [» ]
3G0V X-ray 2.00 A 389-465 [» ]
3G1G X-ray 2.01 A/B 390-476 [» ]
3G1I X-ray 2.10 A/B 389-465 [» ]
3G21 X-ray 0.90 A 389-465 [» ]
3G26 X-ray 1.55 A 389-465 [» ]
3G28 X-ray 1.64 A 389-465 [» ]
3G29 X-ray 2.50 A/B 389-465 [» ]
ProteinModelPortali P03322.
SMRi P03322. Positions 2-87, 214-469, 503-552, 578-701.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-6616346.

Protein family/group databases

MEROPSi A02.015.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1491923.

Miscellaneous databases

EvolutionaryTracei P03322.

Family and domain databases

Gene3Di 1.10.1200.30. 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.
InterProi IPR001969. 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 ]
Pfami PF00607. Gag_p24. 1 hit.
PF02813. Retro_M. 1 hit.
PF00077. RVP. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view ]
ProDomi PD002871. Gag_M. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00343. ZnF_C2HC. 2 hits.
[Graphical view ]
SUPFAMi SSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEi PS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiGAG_RSVP
AccessioniPrimary (citable) accession number: P03322
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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