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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 capsid interacts with human ICAM1 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.
- WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure; URL="http://viperdb.scripps.edu/info_page.php?VDB=1z7s";.
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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: 246051 Da [This is the MW of the unprocessed precursor] |
CRC64: 537F6A13AD37723B [This is a checksum on the sequence] |
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10 20 30 40 50 60
MGAQVSTQKT GAHENQNVAA NGSTINYTTI NYYKDSASNS ATRQDLSQDP SKFTEPVKDL
70 80 90 100 110 120
MLKTAPALNS PNVEACGYSD RVRQITLGNS TITTQEAANA IVAYGEWPTY INDSEANPVD
130 140 150 160 170 180
APTEPDVSSN RFYTLESVSW KTTSRGWWWK LPDCLKDMGM FGQNMYYHYL GRSGYTIHVQ
190 200 210 220 230 240
CNASKFHQGA LGVFLIPEFV MACNTESKTS YVSYINANPG ERGGEFTNTY NPSNTDVSEG
250 260 270 280 290 300
RQFAALDYLL GSGVLAGNAF VYPHQIINLR TNNSATIVVP YVNSLVIDCM AKHNNWGIVI
310 320 330 340 350 360
LPLAPLAFAA TSSPQVPITV TIAPMCTEFN GLRNITIPVH QGLPTMNTPG SNQFLTSDDF
370 380 390 400 410 420
QSPCALPNFD VTPPIHIPGE VKNMMELAEI DTLIPMNAVD GKVNTMEMYQ IPLNDNLSKA
430 440 450 460 470 480
PIFCLSLSPA SDKRLSHTML GEILNYYTHW TGSIRFTFLF CGSMMATGKL LLSYSPPGAK
490 500 510 520 530 540
PPTNRKDAML GTHIIWDLGL QSSCSMVAPW ISNTVYRRCA RDDFTEGGFI TCFYQTRIVV
550 560 570 580 590 600
PASTPTSMFM LGFVSACPDF SVRLLRDTSH ISQSKLIART QGIEDLIDTA IKNALRVSQP
610 620 630 640 650 660
LRPSQLKQPN GVNSQEVPAL TAVETGASGQ AIPSDVVETR HVINYKTRSE SCLESFFGRA
670 680 690 700 710 720
ACVTILSLTN SSKSGEEKKH FNIWNITYTD TVQLRRKLEF FTYSRFDLEM TFVFTENYPS
730 740 750 760 770 780
TASGEVRNQC DQIMYIPPGA PRPSSWDDYT WQSSSNPSIF YMYGNAPPRM SIPYVGIANA
790 800 810 820 830 840
YSHFYDGFAR VPLEGENTDA GDTFYGLVSI NDFGVLAVRA VNRSNPHTIH TSVRVYMKPK
850 860 870 880 890 900
HIRCWCPRPP RAVLYRGEGV DMISSAIQPL TKVDSITTFG FGHQNKAVYV AGYKICNYHL
910 920 930 940 950 960
ATPSDHLNAI SVLWDRDLMV VESRAQGTDT IARCSCRCGV YYCESRRKYY LVTFTGPTFR
970 980 990 1000 1010 1020
FMEANDYYPA RYQSHMLIGC GFAEPGDCGG ILRCTHGVIG IITAGGEGIV AFADIRDLWV
1030 1040 1050 1060 1070 1080
YEEEAMEQGI TSYIESLGTA FGAGFTHTIS EKVTELTTMV TSTITEKLLK NLVKIVSALV
1090 1100 1110 1120 1130 1140
IVVRNYEDTT TILATLALLG CDISPWQWLK KKACDLLEIP HVMRQGDGWM KKFTEACNAA
1150 1160 1170 1180 1190 1200
KGLRWVSNKI SKFVDWLKCK IIPEAKDKVE FLTKLKQLDM LENQIATIHQ SCPSQEQQEI
1210 1220 1230 1240 1250 1260
LFNNVRWLAV QSRRFAPLYA VEARRISKME STINNYIQFK SKHRIEPVCM LVHGSPGTGK
1270 1280 1290 1300 1310 1320
GIASSLIGRA IAERETTSVY SVPLAPSHFD GYKQQGYDMD DLNQNPDGMD MKLFCQMVST
1330 1340 1350 1360 1370 1380
VEFIPPMASL EEKGILFTSD YVLASTNSHS IAPPTVAHSD ALTRRFAFDV EVYTMSEHSV
1390 1400 1410 1420 1430 1440
KGKLNMATAT QLCKDCPTPA NFKKCCPLVC GKALQLMDRY TRQRFTVDEI TTLIMNEKNR
1450 1460 1470 1480 1490 1500
RANIGNCMEA LFQGPLRYKD LKIDVKTVPP PECISDLLQA VDSQEVRDYC EKKGWIVNVT
1510 1520 1530 1540 1550 1560
SQIQLERNIN RAMTILQAVT TFAAVAGVVY VMYKLFAGQQ GAYTGLPNKK PNVPTIRIAK
1570 1580 1590 1600 1610 1620
VQGPGFDYAV AMAKRNIVTA TTTKGEFTML GVHDNVAILP THAAPGETII VDGKEVEILD
1630 1640 1650 1660 1670 1680
ARALEDQAGT NLEITIITLK RNEKFRDIRP HIPTQITETN DGVLIVNTSK YPNMYVPVGA
1690 1700 1710 1720 1730 1740
VTEQGYLNLS GRQTARTLMY NFPTRAGQCG GIITCTGKVI GMHVGGNGSH GFAAALKRSY
1750 1760 1770 1780 1790 1800
FTQNQGEIQW MRSSKEVGYP IINAPSKTKL EPSAFHYVFE GVKEPAVLTK NDPRLKTDFE
1810 1820 1830 1840 1850 1860
EAIFSKYVGN KITEVDEYMK EAVDHYAGQL MSLDINTEQM CLEDAMYGTD GLEALDLSTS
1870 1880 1890 1900 1910 1920
AGYPYVAMGK KKRDILDKQT RDTKEMQRLL DTYGINLPLV TYVKDELRSK TKVEQGKSRL
1930 1940 1950 1960 1970 1980
IEASSLNDSV AMRMAFGNLY AAFHKNPGVV TGSAVGCDPD LFWSKIPVLM EEKLFAFDYT
1990 2000 2010 2020 2030 2040
GYDASLSPAW FEALKMVLEK IGFGNRVDYI DYLNHSHHLY KNKTYCVKGG MPSGCSGTSI
2050 2060 2070 2080 2090 2100
FNSMINNLII RTLLLRTYKG IDLDHLKMIA YGDDVIASYP HEVDASLLAQ SGKDYGLTMT
2110 2120 | |
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