P03300 (POLG_POL1M) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Genome polyprotein Cleaved into the following 12 chains: Protein VP0 Alternative name(s): VP4-VP2 Protein VP4 Alternative name(s): P1A Virion protein 4 Protein VP2 Alternative name(s): P1B Virion protein 2 Protein VP3 Alternative name(s): P1C Virion protein 3 Protein VP1 Alternative name(s): P1D Virion protein 1 Picornain 2A Short name=P2A Short name=Protein 2A EC=3.4.22.29 Protein 2B Short name=P2B Protein 2C Short name=P2C EC=3.6.1.15 Protein 3A Short name=P3A Protein 3B Short name=P3B Alternative name(s): VPg Picornain 3C EC=3.4.22.28 Alternative name(s): Protease 3C Short name=P3C RNA-directed RNA polymerase 3D-POL Short name=P3D-POL EC=2.7.7.48
Organism	Poliovirus type 1 (strain Mahoney) [Reference proteome]
Taxonomic identifier	12081 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Enterovirus › Enterovirus C › Human poliovirus 1
Virus host	Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	2209 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8 Ref.11 Ref.14 VP0 precursor is a component of immature procapsids By similarity. Ref.8 Ref.11 Ref.14 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. Ref.8 Ref.11 Ref.14 Protein 2B affects membrane integrity and cause an increase in membrane permeability By similarity. Ref.8 Ref.11 Ref.14 Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities. Ref.8 Ref.11 Ref.14 Protein 3A, via its hydrophobic domain, serves as membrane anchor. It also inhibits endoplasmic reticulum-to-Golgi transport By similarity. Ref.8 Ref.11 Ref.14 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. Ref.8 Ref.11 Ref.14 RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity. Ref.8 Ref.11 Ref.14
Catalytic activity	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.
Subunit structure	P2C N-terminus interacts with human RTN3. This interaction is important for viral replication By similarity. Interacts with human PVR. Ref.12
Subcellular location	Protein VP2: Virion. Host cytoplasm Potential. Protein VP3: Virion. Host cytoplasm Potential. Protein VP1: Virion. Host cytoplasm Potential. 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. Protein 3B: Virion Potential. Picornain 3C: Host cytoplasm Potential. 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.
Post-translational modification	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. Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle By similarity.
Sequence similarities	Belongs to the picornaviruses polyprotein family. Contains 2 peptidase C3 domains. Contains 1 RdRp catalytic domain. Contains 1 SF3 helicase domain.

Ontologies

Keywords
Biological process	Activation of host autophagy by virus Clathrin- and caveolin-independent endocytosis of virus by host Host-virus interaction Inhibition of host IFN-mediated response initiation by virus Inhibition of host RIG-I by virus Inhibition of host innate immune response by virus Ion transport Pore-mediated penetration of viral genome into host cell Transport Viral RNA replication Viral attachment to host cell Viral immunoevasion Viral penetration into host cytoplasm Virus endocytosis by host Virus entry into host cell
Cellular component	Host cytoplasm Host cytoplasmic vesicle Host membrane Membrane Virion
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Capsid protein Helicase Hydrolase Ion channel Nucleotidyltransferase Protease RNA-directed RNA polymerase Thiol protease Transferase Viral ion channel
PTM	Covalent protein-RNA linkage Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	RNA-protein covalent cross-linking Inferred from electronic annotation. Source: UniProtKB-KW induction by virus of host autophagy Inferred from electronic annotation. Source: UniProtKB-KW ion transport Inferred from electronic annotation. Source: UniProtKB-KW pore-mediated entry of viral genome into host cell Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host RIG-I activity Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host type I interferon production Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro viral attachment to host cell Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell via endocytosis Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell cytoplasmic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-KW viral capsid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA helicase activity Inferred from electronic annotation. Source: InterPro RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro 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

Initiator methionine

1

1

Removed; by host By similarity

Chain

2 – 341

340

Protein VP0 Potential

PRO_0000311078

Chain

2 – 69

68

Protein VP4 Potential

PRO_0000040080

Chain

70 – 341

272

Protein VP2 Potential

PRO_0000040081

Chain

342 – 579

238

Protein VP3 Potential

PRO_0000040082

Chain

580 – 881

302

Protein VP1 Potential

PRO_0000040083

Chain

882 – 1030

149

Picornain 2A Potential

PRO_0000040084

Chain

1031 – 1127

97

Protein 2B Potential

PRO_0000040085

Chain

1128 – 1456

329

Protein 2C Potential

PRO_0000040086

Chain

1457 – 1543

87

Protein 3A Potential

PRO_0000040087

Chain

1544 – 1565

22

Protein 3B Potential

PRO_0000040088

Chain

1566 – 1747

182

Picornain 3C Potential

PRO_0000040089

Chain

1748 – 2209

462

RNA-directed RNA polymerase 3D-POL Potential

PRO_0000040090

Regions

Topological domain

2 – 1520

1519

Cytoplasmic Potential

Intramembrane

1521 – 1536

16

Potential

Topological domain

1537 – 2209

673

Cytoplasmic Potential

Domain

1232 – 1388

157

SF3 helicase

Domain

1975 – 2090

116

RdRp catalytic

Nucleotide binding

1256 – 1263

8

ATP Potential

Sites

Active site

901

1

For picornain 2A activity By similarity

Active site

919

1

For picornain 2A activity By similarity

Active site

990

1

For picornain 2A activity By similarity

Active site

1605

1

For picornain 3C activity Potential

Active site

1636

1

For picornain 3C activity Potential

Active site

1712

1

For picornain 3C activity Potential

Site

25

1

Involved in the interaction with human RTN3 By similarity

Site

69 – 70

2

Cleavage Potential

Site

341 – 342

2

Cleavage; by picornain 3C Potential

Site

881 – 882

2

Cleavage; by picornain 2A Potential

Site

1030 – 1031

2

Cleavage; by picornain 3C Potential

Site

1127 – 1128

2

Cleavage; by picornain 3C Potential

Site

1456 – 1457

2

Cleavage; by picornain 3C Potential

Site

1543 – 1544

2

Cleavage; by picornain 3C Potential

Site

1565 – 1566

2

Cleavage; by picornain 3C Potential

Site

1748 – 1749

2

Cleavage; by picornain 3C Potential

Amino acid modifications

Modified residue

1546

1

O-(5'-phospho-RNA)-tyrosine

Lipidation

2

1

N-myristoyl glycine; by host Ref.6 Ref.17

Experimental info

Mutagenesis

3

1

A → D: 50% loss of myristoylation. Severe reduction in specific infectivity. Ref.6

Mutagenesis

3

1

A → G, L or V: No effect on myristoylation and virus growth. Ref.6

Mutagenesis

3

1

A → H: No effect on myristoylation. Severe reduction in specific infectivity. Ref.6

Sequence conflict

242 – 264

23

RFCPV…FVFPH → SSARWITSLEMARCWGMPLC SA in CAA24446. Ref.2

Sequence conflict

287

1

I → L in CAA24446. Ref.2

Sequence conflict

309

1

A → V in CAA24446. Ref.2

Sequence conflict

420 – 422

3

DDP → AAS in CAA24446. Ref.2

Sequence conflict

464

1

F → S in CAA24446. Ref.2

Sequence conflict

515

1

T → S in CAA24446. Ref.2

Sequence conflict

855 – 856

2

AV → QL in CAA24446. Ref.2

Sequence conflict

972

1

A → V in CAA24446. Ref.2

Sequence conflict

985

1

A → E in CAA24446. Ref.2

Sequence conflict

1140 – 1141

2

NA → QR in CAA24446. Ref.2

Sequence conflict

1619

1

V → A in CAA24446. Ref.2

Sequence conflict

1626 – 1627

2

AL → VF in CAA24446. Ref.2

Sequence conflict

1635

1

L → F in CAA24446. Ref.2

Sequence conflict

1682

1

G → R in CAA24446. Ref.2

Sequence conflict

1722 – 1730

9

VIGMHVGGN → SSGCMLVD in CAA24446. Ref.2

Sequence conflict

1743

1

Y → L in CAA24446. Ref.2

Sequence conflict

1752

1

Q → P in CAA24446. Ref.2

Sequence conflict

1759 – 1760

2

EV → DA in CAA24446. Ref.2

Sequence conflict

1840

1

T → I in CAA24446. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2209

Helix Strand Turn

Details...

Helix

1478 – 1484

7

Helix

1487 – 1496

10

Beta strand

1546 – 1550

5

Beta strand

1556 – 1558

3

Helix

1560 – 1564

5

Helix

1567 – 1579

13

Beta strand

1580 – 1585

6

Beta strand

1588 – 1597

10

Beta strand

1599 – 1603

5

Helix

1604 – 1606

3

Beta strand

1610 – 1614

5

Beta strand

1617 – 1628

12

Beta strand

1634 – 1645

12

Helix

1652 – 1654

3

Beta strand

1662 – 1669

8

Beta strand

1671 – 1674

4

Beta strand

1677 – 1692

16

Beta strand

1695 – 1705

11

Beta strand

1715 – 1718

4

Beta strand

1721 – 1729

9

Beta strand

1734 – 1738

5

Helix

1741 – 1744

4

Beta strand

1750 – 1756

7

Turn

1757 – 1761

5

Turn

1763 – 1766

4

Helix

1770 – 1772

3

Turn

1777 – 1781

5

Helix

1802 – 1807

6

Helix

1820 – 1834

15

Turn

1835 – 1837

3

Helix

1845 – 1850

6

Beta strand

1860 – 1862

3

Turn

1866 – 1872

7

Helix

1875 – 1878

4

Turn

1881 – 1884

4

Helix

1887 – 1895

9

Beta strand

1902 – 1906

5

Helix

1913 – 1917

5

Beta strand

1923 – 1926

4

Helix

1929 – 1948

20

Turn

1952 – 1955

4

Helix

1962 – 1965

4

Turn

1966 – 1968

3

Helix

1969 – 1972

4

Beta strand

1975 – 1978

4

Beta strand

1981 – 1984

4

Helix

1985 – 1988

4

Helix

1991 – 2003

13

Turn

2004 – 2006

3

Helix

2007 – 2010

4

Helix

2011 – 2017

7

Beta strand

2018 – 2023

6

Beta strand

2026 – 2032

7

Beta strand

2036 – 2038

3

Helix

2041 – 2060

20

Beta strand

2061 – 2063

3

Helix

2066 – 2068

3

Beta strand

2070 – 2074

5

Beta strand

2077 – 2084

8

Helix

2088 – 2097

10

Beta strand

2102 – 2104

3

Turn

2105 – 2107

3

Turn

2116 – 2118

3

Beta strand

2120 – 2123

4

Beta strand

2124 – 2128

5

Beta strand

2130 – 2132

3

Beta strand

2135 – 2139

5

Helix

2142 – 2149

8

Beta strand

2151 – 2153

3

Helix

2155 – 2157

3

Helix

2158 – 2169

12

Helix

2170 – 2172

3

Helix

2174 – 2184

11

Helix

2188 – 2191

4

Helix

2198 – 2208

11

Sequences

	Sequence		Length	Mass (Da)
	P03300 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DF1754F87F2E97D6	FASTA	2,209	246,540
	10 20 30 40 50 60 MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFSQDP SKFTEPIKDV 70 80 90 100 110 120 LIKTAPMLNS PNIEACGYSD RVLQLTLGNS TITTQEAANS VVAYGRWPEY LRDSEANPVD 130 140 150 160 170 180 QPTEPDVAAC RFYTLDTVSW TKESRGWWWK LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ 190 200 210 220 230 240 CNASKFHQGA LGVFAVPEMC LAGDSNTTTM HTSYQNANPG EKGGTFTGTF TPDNNQTSPA 250 260 270 280 290 300 RRFCPVDYLL GNGTLLGNAF VFPHQIINLR TNNCATLVLP YVNSLSIDSM VKHNNWGIAI 310 320 330 340 350 360 LPLAPLNFAS ESSPEIPITL TIAPMCCEFN GLRNITLPRL QGLPVMNTPG SNQYLTADNF 370 380 390 400 410 420 QSPCALPEFD VTPPIDIPGE VKNMMELAEI DTMIPFDLSA TKKNTMEMYR VRLSDKPHTD 430 440 450 460 470 480 DPILCLSLSP ASDPRLSHTM LGEILNYYTH WAGSLKFTFL FCGFMMATGK LLVSYAPPGA 490 500 510 520 530 540 DPPKKRKEAM LGTHVIWDIG LQSSCTMVVP WISNTTYRQT IDDSFTEGGY ISVFYQTRIV 550 560 570 580 590 600 VPLSTPREMD ILGFVSACND FSVRLLRDTT HIEQKALAQG LGQMLESMID NTVRETVGAA 610 620 630 640 650 660 TSRDALPNTE ASGPTHSKEI PALTAVETGA TNPLVPSDTV QTRHVVQHRS RSESSIESFF 670 680 690 700 710 720 ARGACVTIMT VDNPASTTNK DKLFAVWKIT YKDTVQLRRK LEFFTYSRFD MELTFVVTAN 730 740 750 760 770 780 FTETNNGHAL NQVYQIMYVP PGAPVPEKWD DYTWQTSSNP SIFYTYGTAP ARISVPYVGI 790 800 810 820 830 840 SNAYSHFYDG FSKVPLKDQS AALGDSLYGA ASLNDFGILA VRVVNDHNPT KVTSKIRVYL 850 860 870 880 890 900 KPKHIRVWCP RPPRAVAYYG PGVDYKDGTL TPLSTKDLTT YGFGHQNKAV YTAGYKICNY 910 920 930 940 950 960 HLATQDDLQN AVNVMWSRDL LVTESRAQGT DSIARCNCNA GVYYCESRRK YYPVSFVGPT 970 980 990 1000 1010 1020 FQYMEANNYY PARYQSHMLI GHGFASPGDC GGILRCHHGV IGIITAGGEG LVAFSDIRDL 1030 1040 1050 1060 1070 1080 YAYEEEAMEQ GITNYIESLG AAFGSGFTQQ ISDKITELTN MVTSTITEKL LKNLIKIISS 1090 1100 1110 1120 1130 1140 LVIITRNYED TTTVLATLAL LGCDASPWQW LRKKACDVLE IPYVIKQGDS WLKKFTEACN 1150 1160 1170 1180 1190 1200 AAKGLEWVSN KISKFIDWLK EKIIPQARDK LEFVTKLRQL EMLENQISTI HQSCPSQEHQ 1210 1220 1230 1240 1250 1260 EILFNNVRWL SIQSKRFAPL YAVEAKRIQK LEHTINNYIQ FKSKHRIEPV CLLVHGSPGT 1270 1280 1290 1300 1310 1320 GKSVATNLIA RAIAERENTS TYSLPPDPSH FDGYKQQGVV IMDDLNQNPD GADMKLFCQM 1330 1340 1350 1360 1370 1380 VSTVEFIPPM ASLEEKGILF TSNYVLASTN SSRISPPTVA HSDALARRFA FDMDIQVMNE 1390 1400 1410 1420 1430 1440 YSRDGKLNMA MATEMCKNCH QPANFKRCCP LVCGKAIQLM DKSSRVRYSI DQITTMIINE 1450 1460 1470 1480 1490 1500 RNRRSNIGNC MEALFQGPLQ YKDLKIDIKT SPPPECINDL LQAVDSQEVR DYCEKKGWIV 1510 1520 1530 1540 1550 1560 NITSQVQTER NINRAMTILQ AVTTFAAVAG VVYVMYKLFA GHQGAYTGLP NKKPNVPTIR 1570 1580 1590 1600 1610 1620 TAKVQGPGFD YAVAMAKRNI VTATTSKGEF TMLGVHDNVA ILPTHASPGE SIVIDGKEVE 1630 1640 1650 1660 1670 1680 ILDAKALEDQ AGTNLEITII TLKRNEKFRD IRPHIPTQIT ETNDGVLIVN TSKYPNMYVP 1690 1700 1710 1720 1730 1740 VGAVTEQGYL NLGGRQTART LMYNFPTRAG QCGGVITCTG KVIGMHVGGN GSHGFAAALK 1750 1760 1770 1780 1790 1800 RSYFTQSQGE IQWMRPSKEV GYPIINAPSK TKLEPSAFHY VFEGVKEPAV LTKNDPRLKT 1810 1820 1830 1840 1850 1860 DFEEAIFSKY VGNKITEVDE YMKEAVDHYA GQLMSLDINT EQMCLEDAMY GTDGLEALDL 1870 1880 1890 1900 1910 1920 STSAGYPYVA MGKKKRDILN KQTRDTKEMQ KLLDTYGINL PLVTYVKDEL RSKTKVEQGK 1930 1940 1950 1960 1970 1980 SRLIEASSLN DSVAMRMAFG NLYAAFHKNP GVITGSAVGC DPDLFWSKIP VLMEEKLFAF 1990 2000 2010 2020 2030 2040 DYTGYDASLS PAWFEALKMV LEKIGFGDRV DYIDYLNHSH HLYKNKTYCV KGGMPSGCSG 2050 2060 2070 2080 2090 2100 TSIFNSMINN LIIRTLLLKT YKGIDLDHLK MIAYGDDVIA SYPHEVDASL LAQSGKDYGL 2110 2120 2130 2140 2150 2160 TMTPADKSAT FETVTWENVT FLKRFFRADE KYPFLIHPVM PMKEIHESIR WTKDPRNTQD 2170 2180 2190 2200 HVRSLCLLAW HNGEEEYNKF LAKIRSVPIG RALLLPEYST LYRRWLDSF

References

[1]	"Primary structure, gene organization and polypeptide expression of poliovirus RNA." Kitamura N., Semler B.L., Rothberg P.G., Larsen G.R., Adler C.J., Dorner A.J., Emini E.A., Hanecak R., Lee J.J., van der Werf S., Anderson C.W., Wimmer E. Nature 291:547-553(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Molecular cloning of poliovirus cDNA and determination of the complete nucleotide sequence of the viral genome." Racaniello V.R., Baltimore D. Proc. Natl. Acad. Sci. U.S.A. 78:4887-4891(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]	"Identification of the initiation site of poliovirus polyprotein synthesis." Dorner A.J., Dorner L.F., Larsen G.R., Wimmer E., Anderson C.W. J. Virol. 42:1017-1028(1982) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-69.
[4]	"The genome-linked protein of picornaviruses. VII. Genetic mapping of poliovirus VPg by protein and RNA sequence studies." Kitamura N., Adler C.J., Rothberg P.G., Martinko J., Nathenson S.G., Wimmer E. Cell 21:295-302(1980) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1539-1574, COVALENT RNA-LINKAGE OF VPG.
[5]	"Protein is linked to the 5' end of poliovirus RNA by a phosphodiester linkage to tyrosine." Ambros V., Baltimore D. J. Biol. Chem. 253:5263-5266(1978) [PubMed] [Europe PMC] [Abstract] Cited for: COVALENT RNA-LINKAGE OF VPG.
[6]	"Myristoylation is important at multiple stages in poliovirus assembly." Moscufo N., Simons J., Chow M. J. Virol. 65:2372-2380(1991) [PubMed] [Europe PMC] [Abstract] Cited for: MYRISTOYLATION AT GLY-2, MUTAGENESIS OF ALA-3.
[7]	"Poliovirus protein 2C has ATPase and GTPase activities." Rodriguez P.L., Carrasco L. J. Biol. Chem. 268:8105-8110(1993) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF PROTEIN 2C.
[8]	"Poliovirus 2A proteinase cleaves directly the eIF-4G subunit of eIF-4F complex." Ventoso I., MacMillan S.E., Hershey J.W., Carrasco L. FEBS Lett. 435:79-83(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF PICORNAIN 2A.
[9]	"Biochemical and genetic studies of the VPg uridylylation reaction catalyzed by the RNA polymerase of poliovirus." Paul A.V., Peters J., Mugavero J., Yin J., van Boom J.H., Wimmer E. J. Virol. 77:891-904(2003) [PubMed] [Europe PMC] [Abstract] Cited for: COVALENT RNA-LINKAGE OF VPG, URIDYLYLATION AT TYR-1546.
[10]	"Intramolecular and intermolecular uridylylation by poliovirus RNA-dependent RNA polymerase." Richards O.C., Spagnolo J.F., Lyle J.M., Vleck S.E., Kuchta R.D., Kirkegaard K. J. Virol. 80:7405-7415(2006) [PubMed] [Europe PMC] [Abstract] Cited for: COVALENT RNA-LINKAGE OF VPG, URIDYLYLATION AT TYR-1546.
[11]	"The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes." Bubeck D., Filman D.J., Cheng N., Steven A.C., Hogle J.M., Belnap D.M. J. Virol. 79:7745-7755(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF VP1 AND VP4.
[12]	"Reticulon 3 binds the 2C protein of enterovirus 71 and is required for viral replication." Tang W.-F., Yang S.-Y., Wu B.-W., Jheng J.-R., Chen Y.-L., Shih C.-H., Lin K.-H., Lai H.-C., Tang P., Horng J.-T. J. Biol. Chem. 282:5888-5898(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN RTN3.
[13]	"Membrane topography of the hydrophobic anchor sequence of poliovirus 3A and 3AB proteins and the functional effect of 3A/3AB membrane association upon RNA replication." Fujita K., Krishnakumar S.S., Franco D., Paul A.V., London E., Wimmer E. Biochemistry 46:5185-5199(2007) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
[14]	"New (fluorescent) light on poliovirus entry." Bergelson J.M. Trends Microbiol. 16:44-47(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF CAPSID PROTEINS.
[15]	"Three-dimensional structure of poliovirus at 2.9-A resolution." Hogle J.M., Chow M., Filman D.J. Science 229:1358-1365(1985) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-881.
[16]	"Structures of poliovirus complexes with anti-viral drugs: implications for viral stability and drug design." Grant R.A., Hiremath C.N., Filman D.J., Syed R., Andries K., Hogle J.M. Curr. Biol. 4:784-797(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-881.
[17]	"Interaction of the poliovirus receptor with poliovirus." He Y., Bowman V.D., Mueller S., Bator C.M., Bella J., Peng X., Baker T.S., Wimmer E., Kuhn R.J., Rossmann M.G. Proc. Natl. Acad. Sci. U.S.A. 97:79-84(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (2.0 ANGSTROMS) OF 1-881, MYRISTOYLATION AT GLY-2.
+	Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure associated with cellular receptor

Virus Particle ExploreR db

Icosahedral capsid structure associated with cellular receptor

Virus Particle ExploreR db

Icosahedral capsid structure in complex with R80633, an inhibitor of viral replication

Virus Particle ExploreR db

Icosahedral capsid structure in complex with R77975, an inhibitor of viral replication

Virus Particle ExploreR db

Icosahedral empty capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure complexed with R78206

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure of 135S cell entry intermediate

Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V01149 Genomic RNA. Translation: CAA24461.1.
V01148 Genomic RNA. Translation: CAA24446.1.

PIR

GNNY2P. A03898.
GNNY1P. A93258.

RefSeq

NP_041277.1. NC_002058.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AL2	X-ray	2.90	1	580-880	[»]
			2	70-340	[»]
			3	342-578	[»]
			4	2-69	[»]
1AR6	X-ray	2.90	1	580-880	[»]
			2	70-340	[»]
			3	342-578	[»]
			4	2-69	[»]
1AR7	X-ray	2.90	1	580-880	[»]
			2	70-340	[»]
			3	342-578	[»]
			4	2-69	[»]
1AR8	X-ray	2.90	1	580-880	[»]
			2	70-340	[»]
			3	342-578	[»]
			4	2-69	[»]
1AR9	X-ray	2.90	1	580-880	[»]
			2	70-340	[»]
			3	342-578	[»]
			4	2-69	[»]
1ASJ	X-ray	2.90	1	580-880	[»]
			2	70-340	[»]
			3	342-578	[»]
			4	2-69	[»]
1DGI	electron microscopy	22.00	2	74-341	[»]
			3	342-576	[»]
1FPT	X-ray	3.00	P	665-682	[»]
1HXS	X-ray	2.20	1	580-880	[»]
			2	70-340	[»]
			3	342-577	[»]
			4	2-68	[»]
1L1N	X-ray	2.10	A/B	1566-1747	[»]
1NG7	NMR	-	A/B	1457-1514	[»]
1NN8	electron microscopy	15.00	1	580-881	[»]
			2	70-341	[»]
			3	342-576	[»]
			4	2-69	[»]
1PO1	X-ray	2.90	1	580-880	[»]
			2	70-340	[»]
			3	342-578	[»]
			4	2-69	[»]
1PO2	X-ray	2.90	1	580-880	[»]
			2	70-340	[»]
			3	342-578	[»]
			4	2-69	[»]
1POV	X-ray	2.80	0	2-340	[»]
			1	580-880	[»]
			3	342-578	[»]
1RA6	X-ray	2.00	A	1749-2208	[»]
1RA7	X-ray	2.35	A	1749-2208	[»]
1RAJ	X-ray	2.50	A	1817-2208	[»]
1RDR	X-ray	2.40	A	1749-2208	[»]
1TQL	X-ray	2.30	A	1750-2208	[»]
1VBD	X-ray	2.90	1	580-881	[»]
			2	70-341	[»]
			3	342-579	[»]
			4	2-69	[»]
1XYR	electron microscopy	11.00	1	650-880	[»]
			2	97-332	[»]
			3	391-571	[»]
			5	342-353	[»]
			6	355-389	[»]
			7	82-95	[»]
			8	621-631	[»]
2BBL	NMR	-	A	1544-1565	[»]
2BBP	NMR	-	A	1544-1565	[»]
2IJD	X-ray	3.40	1/2	1566-2208	[»]
2IJF	X-ray	3.00	A	1749-2208	[»]
2ILY	X-ray	2.60	A	1749-2208	[»]
2ILZ	X-ray	2.50	A	1749-2208	[»]
2IM0	X-ray	2.25	A	1749-2208	[»]
2IM1	X-ray	2.50	A	1749-2208	[»]
2IM2	X-ray	2.35	A	1749-2208	[»]
2IM3	X-ray	2.60	A	1749-2208	[»]
2PLV	X-ray	2.88	1	580-880	[»]
			2	70-340	[»]
			3	342-578	[»]
			4	2-68	[»]
3EPC	electron microscopy	8.00	1	599-881	[»]
			2	74-341	[»]
			3	342-576	[»]
			4	2-69	[»]
3IYB	electron microscopy	-	1	647-881	[»]
			4	97-341	[»]
3IYC	electron microscopy	-	1	647-881	[»]
			4	97-341	[»]
3OL7	X-ray	2.70	A/E/I/M	1749-2209	[»]
4DCD	X-ray	1.69	A	1566-1748	[»]

ProteinModelPortal

P03300.

SMR

P03300. Positions 2-579, 599-1030, 1457-1515, 1566-2209.

ModBase

Search...

Protein family/group databases

MEROPS

C03.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

4.10.80.10. 2 hits.

InterPro

IPR003593. AAA+_ATPase.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]

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.
[Graphical view]

ProDom

PD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00382. AAA. 1 hit.
[Graphical view]

SUPFAM

SSF89043. P3A. 1 hit.
SSF50494. Pept_Ser_Cys. 2 hits.

PROSITE

PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P03300.

ChEMBL

CHEMBL5127.

EvolutionaryTrace

P03300.

PMAP-CutDB

P03299.

Entry information

Entry name

POLG_POL1M

Accession

Primary (citable) accession number: P03300
Secondary accession number(s): P03299 , Q84879, Q84880, Q89679

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 155 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program