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- 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 (By similarity).
- 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.
- 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.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 2206 AA [This is the length of the unprocessed precursor] |
Molecular weight: 245733 Da [This is the MW of the unprocessed precursor] |
CRC64: F226AD85403C37BA [This is a checksum on the sequence] |
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10 20 30 40 50 60
MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYKDSASNA ASKQDYSQDP SKFTEPLKDV
70 80 90 100 110 120
LIKTAPALNS PNVEACGYSD RVLQLTLGNS TITTQEAANS VVAYGRWPEF IRDDEANPVD
130 140 150 160 170 180
QPTEPDVATS RFYTLDTVMW GKESRGWWWK LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ
190 200 210 220 230 240
CNASKFHQGS LGVFAIPEFC LAGDSDTQRY TSYANANPGE KGGKFYAQFN KDTAVTSPKR
250 260 270 280 290 300
EFCPVDYLLG CGVLIGNAFV FPHQIINLRT NNSATLVLPY VNALSIDSMV KHNNWGIAIL
310 320 330 340 350 360
PLSPLDFAQD SSVEIPITVT IAPMCSEFNG LRNVTAPKLQ GLPVLNTPGS NQYLTSDNHQ
370 380 390 400 410 420
SPCAIPEFDV TPPIDIPGEV KNVMELAEID TMIPLNLENT KRNTMDMYRV RLSDSANLSG
430 440 450 460 470 480
PILCLSLSPA ADPRLSHTML GEVLNYYTHW AGSLKFTFLF CGSMMATGKL LVAYAPPGAQ
490 500 510 520 530 540
PPTSRKEAML GTHVIWDLGL QSSCTMVVPW ISNVTYRQTT QDSFTEGGYI SMFYQTRIVV
550 560 570 580 590 600
PLSTPKAMDM LGFVSACNDF SVRLLRDTTH ISQAAMPQGV DDLITEVAQN ALALSLPKPQ
610 620 630 640 650 660
SNLPDTKASG PAHSKEVPTL TAVETGATNP LVPSDTVQTR HVIQQRSRSE STIESFFARG
670 680 690 700 710 720
ACVAIIEVDN EQPATNVQKL FATWRITYKD TVQLRRKLEF FTYSRFDMEF TFVVTANFTN
730 740 750 760 770 780
SNNGHALNQV YQIMYIPPGA PTPKSWDDYT WQTSSNPSIF YTYGAAPARI SVPYVGLANA
790 800 810 820 830 840
YSHFYDGFAK VPLKSDANDQ VGDSLYSAMA VDDFGVLAIR VVNDHNPTKV TSKVRVYMKP
850 860 870 880 890 900
KHVRVWCPRP PRAVPYYGPG VDYKDGLAPL SEKGLTTYGF GHQNKAVYTA GYKICNYHLA
910 920 930 940 950 960
TQEDLQNAVS VMWNRDLLVT ESKAQGIDSI ARCNCSTGVY YCESRSRYYP VSFVGPTFQY
970 980 990 1000 1010 1020
MEANDYYPAR YQSHMLIGHG FASPGDCGGI LRCQHGVIGI ITAGGEGLVA FSDIRDLYAY
1030 1040 1050 1060 1070 1080
EEEAMEQGIS SYVESLGAAF GSGFTQQIGD KIIELTGMVT STITEKLLKN LIKIVSSLVI
1090 1100 1110 1120 1130 1140
ITRNYDDTTT VLATLALLGC DVSPWQWLKK KACDILEIPY VMRQGDSWLK KFTEACNAAK
1150 1160 1170 1180 1190 1200
GLEWVSNKIS KFIDWLREKI IPQARDKLEF VTKLKQLEML ENQIATIHQS CPSQEHQEIL
1210 1220 1230 1240 1250 1260
FNNVRWLSIQ SKRFAPLYAL EAKRIQKLEH TINNYIQFKS KHRIEPVCLL VHGSPGTGKS
1270 1280 1290 1300 1310 1320
VATNLIARAI AEKENTSTYS LPPDPSHFDG YKQQGVVIMD DLNQNPDGAD MKLFCQMVST
1330 1340 1350 1360 1370 1380
VEFIPPMASL EEKGILFTSN YVLASTNSSR ITPPTVAHSD ALARRFAFDM DIQVMSEYSR
1390 1400 1410 1420 1430 1440
DGKLNMTMAT EMCKNCHQPA NFKRCCPLVC GKAIQLMDKS SRVRYSIDQI TTMIVNEKNR
1450 1460 1470 1480 1490 1500
RSNIGNCMEA LFQGPLQYKD LKIDIKTTPP PECINDLLQA VDSQEVRDYC EKKGWIVNIT
1510 1520 1530 1540 1550 1560
SQVQTERNIN RAMTILQAVT TFAAVAGVVY VMYKLFAGHQ GAYTGLPNKR PNVPTIRTAK
1570 1580 1590 1600 1610 1620
VQGPGFDYAV AMAKRNILTA TTSKGEFTML GVHDNVAILP THASPGETIV IDGKEIEVLD
1630 1640 1650 1660 1670 1680
AKALEDQAGT NLEITIVTLK RNEKFRDIRP HIPAQITETN DGVLIVNTSK YPNMYVPVGA
1690 1700 1710 1720 1730 1740
VTEQGYLNLG GRQTARTLMY NFPTRAGQCG GVITCTGKVI GMHVGGNGSH GFAAALKRSY
1750 1760 1770 1780 1790 1800
FTQSQGEIQW MRPSKEVGYP IINAPSKTKL EPSAFHYVFE GVKEPAVLTK NDPRFKTGFE
1810 1820 1830 1840 1850 1860
EAIFSKYVGN KITEVDEYMK EAVDHYAGQL MSLDINTEQM CLEDAMYGTD GLEALDLSTS
1870 1880 1890 1900 1910 1920
AGYPYVTMGK KKRDILNKQT RDTKEMQRLL DTYGINLPLV TYVKDELRSK TKVEQGKSRL
1930 1940 1950 1960 1970 1980
IEASSLNDSV AMRMAFGNLY AAFHKNPGVV TGSAVGCDPD LFWSKIPVLM EEKLFAFDYT
1990 2000 2010 2020 2030 2040
GYDASLSPAW FEALKMVLEK IGFGDRVDYI DYLNHSHHLY KNKTYCVKGG MPSGCSGTSI
2050 2060 2070 2080 2090 2100
FNSMINNLII RTLLLKTYKG IDLDHLKMIA YGDDVIASYP HEVDASLLAQ SGKDYGLTMT
2110 2120 2130 2140 2150 2160
PADKSATFET VTWENVTFLK RFFRADERYP FLIHPVMPMK EIHESIRWTK DPRNTQDHVR
2170 2180 2190 2200
SLCLLAWHNG EDEYNKFLAM IRSVPIGRAL LLPEYSTLYR RWLDSF
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P06209 in FASTA format |
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