P06209 (POLG_POL32) Reviewed, UniProtKB/Swiss-Prot
Last modified May 1, 2013. Version 125. History...
Names and origin
|Protein names||Recommended name:|
Cleaved into the following 12 chains:
|Organism||Poliovirus type 3 (strain 23127) [Complete proteome]|
|Taxonomic identifier||12087 [NCBI]|
|Taxonomic lineage||Viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Enterovirus › Enterovirus C ›|
|Virus host||Homo sapiens (Human) [TaxID: 9606]|
|Sequence length||2206 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Inferred from homology|
General annotation (Comments)
Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The interaction of five VP1 proteins in the fivefold axes results in a prominent protusion extending to about 25 Angstroms from the capsid shell. The resulting structure appears as a steep plateau encircled by a valley or cleft. This depression also termed canyon is the receptor binding site. The capsid interacts with human PVR at this site to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis in Hela cells and through caveolin-mediated endocytosis in brain microvascular endothelial cells. VP4 and VP1 subsequently undergo conformational changes leading to the formation of a pore in the endosomal membrane, thereby delivering the viral genome into the cytoplasm By similarity.
VP0 precursor is a component of immature procapsids By similarity.
Protein 2A is a cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA transcription By similarity.
Protein 2B affects membrane integrity and cause an increase in membrane permeability By similarity.
Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity.
Protein 3A, via its hydrophobic domain, serves as membrane anchor. It also inhibits endoplasmic reticulum-to-Golgi transport By similarity.
Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease By similarity.
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
NTP + H2O = NDP + phosphate.
Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.
Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.
Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.
RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.
Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle By similarity.
VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle By similarity.
Belongs to the picornaviruses polyprotein family.
Contains 2 peptidase C3 domains.
Contains 1 RdRp catalytic domain.
Contains 1 SF3 helicase domain.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Initiator methionine||1||1||Removed; by host By similarity|
|Chain||2 – 340||339||Protein VP0 Potential||PRO_0000311082|
|Chain||2 – 69||68||Protein VP4 Potential||PRO_0000040124|
|Chain||70 – 340||271||Protein VP2 Potential||PRO_0000040125|
|Chain||341 – 578||238||Protein VP3 Potential||PRO_0000040126|
|Chain||579 – 878||300||Protein VP1 Potential||PRO_0000040127|
|Chain||879 – 1027||149||Picornain 2A Potential||PRO_0000040128|
|Chain||1028 – 1124||97||Protein 2B Potential||PRO_0000040129|
|Chain||1125 – 1453||329||Protein 2C Potential||PRO_0000040130|
|Chain||1454 – 1540||87||Protein 3A Potential||PRO_0000040131|
|Chain||1541 – 1562||22||Protein 3B Potential||PRO_0000040132|
|Chain||1563 – 1745||183||Picornain 3C Potential||PRO_0000040133|
|Chain||1746 – 2206||461||RNA-directed RNA polymerase 3D-POL Potential||PRO_0000040134|
|Topological domain||2 – 1517||1516||Cytoplasmic Potential|
|Intramembrane||1518 – 1533||16||Potential|
|Topological domain||1534 – 2206||673||Cytoplasmic Potential|
|Domain||1229 – 1385||157||SF3 helicase|
|Domain||1972 – 2087||116||RdRp catalytic|
|Nucleotide binding||1253 – 1260||8||ATP Potential|
|Active site||898||1||For picornain 2A activity By similarity|
|Active site||916||1||For picornain 2A activity By similarity|
|Active site||987||1||For picornain 2A activity By similarity|
|Active site||1602||1||For picornain 3C activity Potential|
|Active site||1633||1||For picornain 3C activity Potential|
|Active site||1709||1||For picornain 3C activity By similarity|
|Site||69 – 70||2||Cleavage Potential|
|Site||340 – 341||2||Cleavage; by picornain 3C Potential|
|Site||878 – 879||2||Cleavage; by picornain 2A Potential|
|Site||1027 – 1028||2||Cleavage; by picornain 3C Potential|
|Site||1124 – 1125||2||Cleavage; by picornain 3C Potential|
|Site||1453 – 1454||2||Cleavage; by picornain 3C Potential|
|Site||1540 – 1541||2||Cleavage; by picornain 3C Potential|
|Site||1562 – 1563||2||Cleavage; by picornain 3C Potential|
|Site||1745 – 1746||2||Cleavage; by picornain 3C Potential|
Amino acid modifications
|Modified residue||1543||1||O-(5'-phospho-RNA)-tyrosine By similarity|
|Lipidation||2||1||N-myristoyl glycine; by host By similarity|
|||"The nucleotide sequence of a type 3 poliovirus isolated during a recent outbreak of poliomyelitis in Finland."|
Hughes P.J., Evans D.M.A., Minor P.D., Schild G.C., Almond J.W., Stanway G.
J. Gen. Virol. 67:2093-2102(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|X04468 Genomic RNA. Translation: CAA28155.1.|
|PIR||GNNY27. A27245. |
3D structure databases
|SMR||P06209. Positions 2-575, 600-1027, 1454-1512, 1563-2206. |
Protein family/group databases
Protocols and materials databases
Family and domain databases
|Gene3D||18.104.22.168. 2 hits. |
|InterPro||IPR003593. AAA+_ATPase. |
|Pfam||PF08727. P3A. 1 hit. |
PF00548. Peptidase_C3. 1 hit.
PF02226. Pico_P1A. 1 hit.
PF00947. Pico_P2A. 1 hit.
PF01552. Pico_P2B. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
|ProDom||PD001306. Peptidase_C3. 1 hit. |
PD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
|SMART||SM00382. AAA. 1 hit. |
|SUPFAM||SSF89043. P3A. 1 hit. |
SSF50494. Pept_Ser_Cys. 2 hits.
|PROSITE||PS50507. RDRP_SSRNA_POS. 1 hit. |
PS51218. SF3_HELICASE_2. 1 hit.
|Accession||Primary (citable) accession number: P06209|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|