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UniProtKB/Swiss-Prot entry P32537


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name POLG_HE701
Primary accession number P32537
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    November 25, 2008 (Entry version 86)
Name and origin of the protein
Protein name Genome polyprotein
Synonyms None
Contains Protein VP0
     (VP4-VP2)
Protein VP4
     (Virion protein 4)
     (P1A)
Protein VP2
     (Virion protein 2)
     (P1B)
Protein VP3
     (Virion protein 3)
     (P1C)
Protein VP1
     (Virion protein 1)
     (P1D)
Picornain 2A
     (Protein 2A)
     (P2A)
     (EC 3.4.22.29)
Protein 2B
     (P2B)
Protein 2C
     (P2C)
     (EC 3.6.1.15)
Protein 3A
     (P3A)
Protein 3B
     (P3B)
     (VPg)
Picornain 3C
     (EC 3.4.22.28)
     (Protease 3C)
     (P3C)
RNA-directed RNA polymerase 3D-POL
     (P3D-POL)
     (EC 2.7.7.48)
Gene name None
From
Human enterovirus 70 (strain J670/71) (EV 70) [TaxID: 31915] 
Taxonomy Viruses; ssRNA positive-strand viruses, no DNA stage; Picornavirales; Picornaviridae; Enterovirus.
Virus host Homo sapiens (Human) [TaxID: 9606]
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2172447 [NCBI, ExPASy, EBI, Israel, Japan]
Ryan M.D., Jenkins O., Hughes P.J., Brown A., Knowles N.J., Booth D., Minor P.D., Almond J.W.;
"The complete nucleotide sequence of enterovirus type 70: relationships with other members of the picornaviridae.";
J. Gen. Virol. 71:2291-2299(1990).
[2]
INTERACTION WITH HOST CD55.
PubMed=8764022 [NCBI, ExPASy, EBI, Israel, Japan]
Karnauchow T.M., Tolson D.L., Harrison B.A., Altman E., Lublin D.M., Dimock K.;
"The HeLa cell receptor for enterovirus 70 is decay-accelerating factor (CD55).";
J. Virol. 70:5143-5152(1996).
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 (By similarity). Capsid proteins interact with host CD55 to provide virion attachment to target cell.
  • FUNCTION: VP0 precursor is a component of immature procapsids (By similarity).
  • FUNCTION: 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).
  • FUNCTION: Protein 2B affects membrane integrity and cause an increase in membrane permeability (By similarity).
  • FUNCTION: Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).
  • FUNCTION: Protein 3A, via its hydrophobic domain, serves as membrane anchor. It also inhibits endoplasmic reticulum-to-Golgi transport (By similarity).
  • FUNCTION: 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).
  • FUNCTION: 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).
  • CATALYTIC ACTIVITY: Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
  • CATALYTIC ACTIVITY: 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.
  • CATALYTIC ACTIVITY: NTP + H2O = NDP + phosphate.
  • SUBUNIT: Capsid proteins interact with host CD55.
  • SUBCELLULAR LOCATION: Protein VP2: Virion. Cytoplasm (Potential).
  • SUBCELLULAR LOCATION: Protein VP3: Virion. Cytoplasm (Potential).
  • SUBCELLULAR LOCATION: Protein VP1: Virion. Cytoplasm (Potential).
  • SUBCELLULAR LOCATION: Protein 2B: 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).
  • SUBCELLULAR LOCATION: Protein 2C: 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).
  • SUBCELLULAR LOCATION: Protein 3A: 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).
  • SUBCELLULAR LOCATION: Protein 3B: Virion (Potential).
  • SUBCELLULAR LOCATION: Picornain 3C: Cytoplasm (Potential).
  • SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: 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).
  • PTM: 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).
  • PTM: VPg is covalently linked to the genomic RNA (By similarity).
  • PTM: Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle (By similarity).
  • SIMILARITY: Belongs to the picornaviruses polyprotein family.
  • SIMILARITY: Contains 2 peptidase C3 domains [view classification].
  • SIMILARITY: Contains 1 RdRp catalytic domain.
  • SIMILARITY: Contains 1 SF3 helicase domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D00820; BAA18891.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A36253; GNNYE7.
RefSeq NP_040760.1; -.
3D structure databases
HSSP P03300; 1RDR. [HSSP ENTRY / PDB]
SMR P32537; 1749-2193, 1750-2194.
ModBase P32537.
Protein family/group databases
MEROPS C03.011; -.
Ontologies
GO
GO:0031410; Cellular component: cytoplasmic vesicle (inferred from electronic annotation from UniProtKB-KW).
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0019028; Cellular component: viral capsid (inferred from electronic annotation from InterPro).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004197; Molecular function: cysteine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0003723; Molecular function: RNA binding (inferred from electronic annotation from InterPro).
GO:0003724; Molecular function: RNA helicase activity (inferred from electronic annotation from InterPro).
GO:0003968; Molecular function: RNA-directed RNA polymerase activity (inferred from electronic annotation from InterPro).
GO:0005198; Molecular function: structural molecule activity (inferred from electronic annotation from InterPro).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
GO:0018144; Biological process: RNA-protein covalent cross-linking (inferred from electronic annotation from InterPro).
GO:0006410; Biological process: transcription, RNA-dependent (inferred from electronic annotation from InterPro).
GO:0019079; Biological process: viral genome replication (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR003593; AAA+_ATPase_core.
IPR000605; Helicase_SF3_ssDNA/RNA_vir.
IPR014759; Helicase_SF3_ssRNA_vir.
IPR014838; P3A.
IPR000199; Pept_C3_picorn.
IPR000081; Peptidase_C3.
IPR003138; Pico_P1A.
IPR002527; Pico_P2B.
IPR001676; Picornavirus_capsid.
IPR001205; RNA_pol_P3D.
IPR007094; RNA_pol_PSvir.
Graphical view of domain structure.
Pfam PF08727; P3A; 1.
PF00548; Peptidase_C3; 1.
PF02226; Pico_P1A; 1.
PF00947; Pico_P2A; 1.
PF01552; Pico_P2B; 1.
PF00680; RdRP_1; 1.
PF00073; Rhv; 3.
PF00910; RNA_helicase; 1.
Pfam graphical view of domain structure.
ProDom PD001125; Pept_C3_picorn; 1.
PD001306; Peptidase_C3_2; 1.
PD001274; Pico_P2B; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00382; AAA; 1.
SMART graphical view of domain structure.
PROSITE PS50507; RDRP_SSRNA_POS; 1.
PS51218; SF3_HELICASE_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P32537.
ProtoNet P32537.
Genome annotation databases
GeneID 1461118; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Capsid protein; Complete proteome; Covalent protein-RNA linkage; Cytoplasm; Cytoplasmic vesicle; Helicase; Host-virus interaction; Hydrolase; Lipoprotein; Membrane; Myristate; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease; RNA replication; RNA-binding; RNA-directed RNA polymerase; Thiol protease; Transferase; Virion.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
INIT_MET   1      1        Removed; by host (By similarity). 
CHAIN   2    319  318     Protein VP0 (Potential). PRO_0000311037
CHAIN   2     69  68     Protein VP4 (Potential). PRO_0000039470
CHAIN   70    319  250     Protein VP2 (Potential). PRO_0000039471
CHAIN   320    561  242     Protein VP3 (Potential). PRO_0000039472
CHAIN   562    871  310     Protein VP1 (Potential). PRO_0000039473
CHAIN   872   1014  143     Picornain 2A (Potential). PRO_0000039474
CHAIN   1015   1113  99     Protein 2B (Potential). PRO_0000039475
CHAIN   1114   1443  330     Protein 2C (Potential). PRO_0000039476
CHAIN   1444   1532  89     Protein 3A (Potential). PRO_0000039477
CHAIN   1533   1554  22     Protein 3B (Potential). PRO_0000039478
CHAIN   1555   1737  183     Picornain 3C (Potential). PRO_0000039479
CHAIN   1738   2194  457     RNA-directed RNA polymerase 3D-POL (Potential). PRO_0000039480
TOPO_DOM   2   1509  1508     Cytoplasmic (Potential). 
TOPO_DOM   1510   1525  16     In membrane (Potential). 
TOPO_DOM   1526   2194  669     Cytoplasmic (Potential). 
DOMAIN   1218   1374  157     SF3 helicase. 
DOMAIN   1960   2075  116     RdRp catalytic. 
NP_BIND   1242   1249  8     ATP (Potential). 
ACT_SITE   885    885        For picornain 2A activity (By similarity). 
ACT_SITE   903    903        For picornain 2A activity (By similarity). 
ACT_SITE   974    974        For picornain 2A activity (By similarity). 
ACT_SITE   1594   1594        For picornain 3C activity (Potential). 
ACT_SITE   1625   1625        For picornain 3C activity (Potential). 
ACT_SITE   1701   1701        For picornain 3C activity (By similarity). 
SITE   69     70  2     Cleavage (Potential). 
SITE   319    320  2     Cleavage; by picornain 3C (Potential). 
SITE   561    562  2     Cleavage; by picornain 3C (Potential). 
SITE   871    872  2     Cleavage; by picornain 2A (Potential). 
SITE   1014   1015  2     Cleavage; by picornain 3C (Potential). 
SITE   1113   1114  2     Cleavage; by picornain 3C (Potential). 
SITE   1443   1444  2     Cleavage; by picornain 3C (Potential). 
SITE   1532   1533  2     Cleavage; by picornain 3C (Potential). 
SITE   1554   1555  2     Cleavage; by picornain 3C (Potential). 
SITE   1737   1738  2     Cleavage; by picornain 3C (Potential). 
MOD_RES   1535   1535        O-(5'-phospho-RNA)-tyrosine (By similarity). 
LIPID   2      2        N-myristoyl glycine; by host (By similarity). 
Sequence information
Length: 2194 AA [This is the length of the unprocessed precursor] Molecular weight: 244595 Da [This is the MW of the unprocessed precursor] CRC64: 15DBAE96EE06673C [This is a checksum on the sequence]
        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 

P32537 in FASTA format

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View entry in raw text format (no links)
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