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P03322

- GAG_RSVP

UniProt

P03322 - GAG_RSVP

Protein

Gag-Pro polyprotein

Gene

gag-pro

Organism
Rous sarcoma virus (strain Prague C) (RSV-PrC)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    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.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei155 – 1562Cleavage; by viral protease p15By similarity
    Sitei166 – 1672Cleavage; by viral protease p15By similarity
    Sitei177 – 1782Cleavage; by viral protease p15By similarity
    Sitei239 – 2402Cleavage; by viral protease p15By similarity
    Sitei479 – 4802Cleavage; by viral protease p15By similarity
    Sitei488 – 4892Cleavage; by viral protease p15By similarity
    Sitei577 – 5782Cleavage; by viral protease p15By similarity
    Active sitei614 – 6141For protease activity; shared with dimeric partnerPROSITE-ProRule annotation

    Regions

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

    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

    GO - Cellular componenti

    1. viral capsid Source: UniProtKB-KW

    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.1 Publication

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03322.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini609 – 69082Peptidase A2PROSITE-ProRule annotationAdd
    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.By similarity

    Sequence similaritiesi

    Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 peptidase A2 domain.PROSITE-ProRule annotation

    Zinc finger

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

    Experimental Info

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

    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: October 1, 2014
    This is version 117 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