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P32537 (POLG_HE701) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 12 chains:

  1. Protein VP0
    Alternative name(s):
    VP4-VP2
  2. Protein VP4
    Alternative name(s):
    P1A
    Virion protein 4
  3. Protein VP2
    Alternative name(s):
    P1B
    Virion protein 2
  4. Protein VP3
    Alternative name(s):
    P1C
    Virion protein 3
  5. Protein VP1
    Alternative name(s):
    P1D
    Virion protein 1
  6. Protease 2A
    Short name=P2A
    EC=3.4.22.29
    Alternative name(s):
    Protein 2A
  7. Protein 2B
    Short name=P2B
  8. Protein 2C
    Short name=P2C
    EC=3.6.1.15
  9. Protein 3A
    Short name=P3A
  10. Protein 3B
    Short name=P3B
    Alternative name(s):
    VPg
  11. Protease 3C
    Short name=P3C
    EC=3.4.22.28
    Alternative name(s):
    Picornain 3C
  12. RNA-directed RNA polymerase 3D-POL
    Short name=P3D-POL
    EC=2.7.7.48
OrganismHuman enterovirus 70 (strain J670/71) (EV 70) [Complete proteome]
Taxonomic identifier31915 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus D
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length2194 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein VP1: Forms, together with VP2 and VP3, an icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Protein VP1 mainly forms the vertices of the capsid. VP1 interacts with host cell receptor to provide virion attachment to target cell. After binding to its receptor, the capsid undergoes conformational changes. VP1 N-terminus (that contains an amphipathic alpha-helix) is externalized, VP4 is released and together, they shape a virion-cell connecting channel and a pore in the host membrane through which RNase-protected transfer of the viral genome takes place. After genome has been released, the channel shrinks By similarity.

Protein VP2: Forms, together with VP1 and VP3, an icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome By similarity.

Protein VP3: Forms, together with VP1 and VP2, an icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome By similarity.

Protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. VP4 is released, VP1 N-terminus is externalized, and together, they shape a virion-cell connecting channel and a pore in the host membrane through which RNase-protected transfer of the viral genome takes place. After genome has been released, the channel shrinks By similarity.

Protein VP0: Protein VP0: VP0 precursor is a component of immature procapsids, which gives rise to VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step By similarity.

Protease 2A: 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 off 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.

Protease 3C: 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 cooperatively to the protease By similarity.

RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity.

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

Capsid proteins interact with host CD55.

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.

Protease 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 By similarity.

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 processActivation of host autophagy by virus
Host gene expression shutoff by virus
Host translation shutoff by virus
Host-virus interaction
Inhibition of host innate immune response by virus
Inhibition of host RIG-I by virus
Inhibition of host RLR pathway by virus
Ion transport
Pore-mediated penetration of viral genome into host cell
Transport
Viral attachment to host cell
Viral immunoevasion
Viral penetration into host cytoplasm
Viral RNA replication
Virus entry into host cell
   Cellular componentCapsid protein
Host cytoplasm
Host cytoplasmic vesicle
Host membrane
Membrane
Virion
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
Ion channel
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase
Thiol protease
Transferase
Viral ion channel
   PTMCovalent protein-RNA linkage
Lipoprotein
Myristate
Phosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processRNA-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 transmembrane transport

Inferred from electronic annotation. Source: GOC

pore formation by virus in membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

pore-mediated entry of viral genome into host cell

Inferred from electronic annotation. Source: UniProtKB-KW

protein oligomerization

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 translation

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: InterPro

transcription, RNA-templated

Inferred from electronic annotation. Source: GOC

viral genome replication

Inferred from electronic annotation. Source: InterPro

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP 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

ion channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 319318Protein VP0 Potential
PRO_0000311037
Chain2 – 6968Protein VP4 Potential
PRO_0000039470
Chain70 – 319250Protein VP2 Potential
PRO_0000039471
Chain320 – 561242Protein VP3 Potential
PRO_0000039472
Chain562 – 871310Protein VP1 Potential
PRO_0000039473
Chain872 – 1014143Protease 2A Potential
PRO_0000039474
Chain1015 – 111399Protein 2B Potential
PRO_0000039475
Chain1114 – 1443330Protein 2C Potential
PRO_0000039476
Chain1444 – 153289Protein 3A Potential
PRO_0000039477
Chain1533 – 155422Protein 3B Potential
PRO_0000039478
Chain1555 – 1737183Protease 3C Potential
PRO_0000039479
Chain1738 – 2194457RNA-directed RNA polymerase 3D-POL Potential
PRO_0000039480

Regions

Topological domain2 – 15091508Cytoplasmic Potential
Intramembrane1510 – 152516 Potential
Topological domain1526 – 2194669Cytoplasmic Potential
Domain1218 – 1374157SF3 helicase
Domain1960 – 2075116RdRp catalytic
Nucleotide binding1242 – 12498ATP Potential

Sites

Active site8851For protease 2A activity By similarity
Active site9031For protease 2A activity By similarity
Active site9741For protease 2A activity By similarity
Active site15941For protease 3C activity Potential
Active site16251For protease 3C activity Potential
Active site17011For protease 3C activity By similarity
Site69 – 702Cleavage Potential
Site319 – 3202Cleavage; by protease 3C Potential
Site561 – 5622Cleavage; by protease 3C Potential
Site871 – 8722Cleavage; by protease 2A Potential
Site1014 – 10152Cleavage; by protease 3C Potential
Site1113 – 11142Cleavage; by protease 3C Potential
Site1443 – 14442Cleavage; by protease 3C Potential
Site1532 – 15332Cleavage; by protease 3C Potential
Site1554 – 15552Cleavage; by protease 3C Potential
Site1737 – 17382Cleavage; by protease 3C Potential

Amino acid modifications

Modified residue15351O-(5'-phospho-RNA)-tyrosine By similarity
Lipidation21N-myristoyl glycine; by host By similarity

Sequences

Sequence LengthMass (Da)Tools
P32537 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 15DBAE96EE06673C

FASTA2,194244,595
        10         20         30         40         50         60 
MGAQVSRQQT GTHENANVAT GGSSITYNQI NFYKDSYAAS ASKQDFSQDP SKFTEPVAEA 

        70         80         90        100        110        120 
LKAGAPVLKS PSAEACGYSD RVLQLKLGNS SIVTQEAANI CCAYGEWPTY LPDNEAVAID 

       130        140        150        160        170        180 
KPTQPETSTD RFYTLKSKKW ESNSTGWWWK LPDALNQIGM FGQNVQYHYL YRSGFLCHVQ 

       190        200        210        220        230        240 
CNATKFHQGT LLIVAIPEHQ IGKKGTGTSA SFAEVMKGAE GGVFEQPYLL DDGTSLACAL 

       250        260        270        280        290        300 
VYPHQWINLR TNNSATIVLP WMNSAPMDFA LRHNNWTLAV IPVCPLAGGT GNTNTYVPIT 

       310        320        330        340        350        360 
ISIAPMCAEY NGLRNAITQG VPTCLLPGSN QFLTTDDHSS APAFPDFSPT PEMHIPGQVH 

       370        380        390        400        410        420 
SMLEIVQIES MMEINNVNDA SGVERLRVQI SAQSDMDQLL FNIPLDIQLE GPLRNTLLGN 

       430        440        450        460        470        480 
ISRYYTHWSG SLEMTFMFCG SFMTTGKLII CYTPPGGSSP TDRMQAMLAT HVVWDFGLQS 

       490        500        510        520        530        540 
SITIIIPWIS GSHYRMFNTD AKAINANVGY VTCFMQTNLV APVGAADQCY IVGMVAAKKD 

       550        560        570        580        590        600 
FNLRLMRDSP DIGQSAILPE QAATTQIGEI VKTVANTVES EIKAELGVIP SLNAVETGAT 

       610        620        630        640        650        660 
SNTEPEEAIQ TRTVINMHGT AECLVENFLG RSALVCMRSF EYKNHSTSTS SIQKNFFIWT 

       670        680        690        700        710        720 
LNTRELVQIR RKMELFTYLR FDTEITIVPT LRLFSSSNVS FSGLPNLTLQ AMYVPTGARK 

       730        740        750        760        770        780 
PSSQDSFEWQ SACNPSVFFK INDPPARLTI PFMSINSAYA NFYDGFAGFE KKATVLYGIN 

       790        800        810        820        830        840 
PANTMGNLCL RVVNSYQPVQ YTLTVRVYMK PKHIKAWAPR APRTMPYTNI LNNNYAGRSA 

       850        860        870        880        890        900 
APNAPTAIVS HRSTIKTMPN DINLTTAGPG YGGAFVGSYK IINYHLATDE EKERSVYVDW 

       910        920        930        940        950        960 
QSDVLVTTVA AHGKHQIARC RCNTGVYYCK HKNRSYPVCF EGPGIQWINE SDYYPARYQT 

       970        980        990       1000       1010       1020 
NTLLAMGPCQ PGDCGGLLVC SHGVIGLVTA GGEGIVAFTD IRNLLWLEDD AMEQGITDYI 

      1030       1040       1050       1060       1070       1080 
QNLGSAFGTG FTETISEKAK EIQNMLVGED SLLEKLLKAL IKIVSAMVIV IRNSEDLVTV 

      1090       1100       1110       1120       1130       1140 
TATLALLGCN DSPWAFLKQK VCSYLGIPYT IRQSDSWLKK FTEACNALRG LDWLAQKIDK 

      1150       1160       1170       1180       1190       1200 
FINWLKTKIL PEAREKHEFV QKLKQLPVIE SQINTIEHSC PNSEXQQALF NNVQYYSHYC 

      1210       1220       1230       1240       1250       1260 
KKYAPLYALE AKRVSALERK INNYIQFKSK SRIEPVCLII HGSPGTGKSV ASNLIARAIT 

      1270       1280       1290       1300       1310       1320 
EKLGGDSYSL PPDPKYFDGY KQQTVVLMDD LMQNPDGNDI AMFCQMVSTV DFIPPMASLE 

      1330       1340       1350       1360       1370       1380 
EKGTLYTSPF LIATTNAGSI HAPTVSDSKA LARRFKFDME IESMESYKDG VRLDMFKAVE 

      1390       1400       1410       1420       1430       1440 
LCNPEKCRPT NYKKCCPLIC GKAIQFRDKR TNVRYSVDML VTEMIKEYRI RNSTQDKLEA 

      1450       1460       1470       1480       1490       1500 
LFQGPPTFKE IKISVTPETP APDAINDLLR SIDSQEVRDY CQKKGWIVMH PPTELVVDKH 

      1510       1520       1530       1540       1550       1560 
ISRAFIALQA ITTFVSIAGV VYVIYKLFAG IQGPYTGLPN QKPKVPTLRT AKVQGPSLDF 

      1570       1580       1590       1600       1610       1620 
AQAIMRKNTV IARTSKGEFT MLGIYDRIAV VPTHASVEEE IYINDVPVKV KDAYALRDIN 

      1630       1640       1650       1660       1670       1680 
DVNLEITVVE LDRNEKFRDI RGFLPKYEDD YNDAILSVNT SKFPNMYIPV GQTLNYGFLN 

      1690       1700       1710       1720       1730       1740 
LGGTPTHRIL MYNFPTRAGQ CGGVVTTTGK VIGIHVGGNG AQGFAAMLLQ NYFTEKQGEI 

      1750       1760       1770       1780       1790       1800 
VSIEKTGVFI NAPAKTKLEP SVFHEVFEGV KEPAVLHSKD KRLKVDFEEA IFSKYVGNKT 

      1810       1820       1830       1840       1850       1860 
MLMDEYMEEA VDHYVGCLEP LDISTEPIKL EEAMYGMDGL EALDLTTSAG YPYLLQGKKK 

      1870       1880       1890       1900       1910       1920 
RDIFNRQTRD TTEMTKMLDK YGVDLPFVTF VKDELRSREK VEKGKSRLIE ASSLNDSVAM 

      1930       1940       1950       1960       1970       1980 
RVAFGNLYAT FHKNPGVATG SAVGCDPDLF WSKIPVXLDG KIFAFDYTGY DASLSPVWFA 

      1990       2000       2010       2020       2030       2040 
CLKKTLVKLG YTHQTAFVDY LCHSVHLYKD RKYIVNGGMP SGSSGTSIFN TMINNIIIRT 

      2050       2060       2070       2080       2090       2100 
LLLKVYKGID LDQFKMIAYG DDVIASYPHE IDPGLLAKAG KEYGLIMTPA DKSSGFTETT 

      2110       2120       2130       2140       2150       2160 
WENVTFLKRY FRADEQYPFL IHPVMPMKEI HESIRWTKDP RNTQDHVRSL CLLAWHNGEE 

      2170       2180       2190 
TYNEFCRKIR TVPVGRALAL PVYSSLRRKW LDSF 

« Hide

References

[1]"The complete nucleotide sequence of enterovirus type 70: relationships with other members of the picornaviridae."
Ryan M.D., Jenkins O., Hughes P.J., Brown A., Knowles N.J., Booth D., Minor P.D., Almond J.W.
J. Gen. Virol. 71:2291-2299(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"The HeLa cell receptor for enterovirus 70 is decay-accelerating factor (CD55)."
Karnauchow T.M., Tolson D.L., Harrison B.A., Altman E., Lublin D.M., Dimock K.
J. Virol. 70:5143-5152(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HOST CD55.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00820 Genomic RNA. Translation: BAA18891.1.
PIRGNNYE7. A36253.
RefSeqNP_040760.1. NC_001430.1.

3D structure databases

ProteinModelPortalP32537.
SMRP32537. Positions 2-68, 74-317, 867-1014.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC03.011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1461118.

Family and domain databases

Gene3D4.10.80.10. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
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]
PfamPF08727. 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]
ProDomPD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOLG_HE701
AccessionPrimary (citable) accession number: P32537
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 130 of the entry and version 4 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