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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2987518 [NCBI, ExPASy, EBI, Israel, Japan]
Robertson B.H.,
Grubman M.J.,
Weddell G.N.,
Moore D.M.,
Welsh J.D.,
Fischer T.,
Dowbenko D.J.,
Yansura D.G.,
Small B.,
Kleid D.G.;
"Nucleotide and amino acid sequence coding for polypeptides of foot-and-mouth disease virus type A12.";
J. Virol. 54:651-660(1985).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1863-2332.
DOI=10.1016/S0042-6822(83)80017-8; PubMed=6305004 [NCBI, ExPASy, EBI, Israel, Japan]
Robertson B.H.,
Morgan D.O.,
Moore D.M.,
Grubman M.J.,
Card J.,
Fischer T.,
Weddell G.N.,
Dowbenko D.J.,
Yansura D.G.;
"Identification of amino acid and nucleotide sequence of the foot-and-mouth disease virus RNA polymerase.";
Virology 126:614-623(1983).
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[3]
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NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 715-955.
PubMed=6272395 [NCBI, ExPASy, EBI, Israel, Japan]
Kleid D.G.,
Yansura D.G.,
Small B.,
Dowbenko D.J.,
Moore D.M.,
Grubman M.J.,
McKercher P.D.,
Morgan D.O.,
Robertson B.H.,
Bachrach H.L.;
"Cloned viral protein vaccine for foot-and-mouth disease: responses in cattle and swine.";
Science 214:1125-1129(1981).
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[4]
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ALTERNATIVE INITIATION.
DOI=10.1093/nar/15.8.3305; PubMed=3033601 [NCBI, ExPASy, EBI, Israel, Japan]
Sangar D.V.,
Newton S.E.,
Rowlands D.J.,
Clarke B.E.;
"All foot and mouth disease virus serotypes initiate protein synthesis at two separate AUGs.";
Nucleic Acids Res. 15:3305-3315(1987).
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- FUNCTION: The leader protease autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. It cleaves the host translation initiation factors EIF4G1 and EIF4G3, in order to shut down the capped cellular mRNA transcription (By similarity).
- 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).
- FUNCTION: VP0 precursor is a component of immature procapsids (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 (By similarity).
- FUNCTION: Protein 3B-1, 3B-2 and 3B-3 are covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. They acts as a genome-linked replication primer (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: Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
- CATALYTIC ACTIVITY: NTP + H2O = NDP + phosphate.
- 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: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
- 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-1: Virion (Potential).
- SUBCELLULAR LOCATION: Protein 3B-2: Virion (Potential).
- SUBCELLULAR LOCATION: Protein 3B-3: 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).
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative initiation.
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| Name | Lb |
| Isoform ID | P03308-2 |
| Features which should be applied to build the isoform sequence: VSP_018980. |
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- 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. The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip from one codon to the next without formation of a peptide bond. This process would release the L-P1-2A peptide from the translational complex (By similarity).
- PTM: Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle (By similarity).
- PTM: VPg is covalently linked to the genomic RNA (By similarity).
- SIMILARITY: Belongs to the picornaviruses polyprotein family.
- SIMILARITY: Contains 1 peptidase C28 domain [view classification].
- SIMILARITY: Contains 1 peptidase C3 domain [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: 2332 AA [This is the length of the unprocessed precursor] |
Molecular weight: 259410 Da [This is the MW of the unprocessed precursor] |
CRC64: EE77DA739CBEDC6A [This is a checksum on the sequence] |
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10 20 30 40 50 60
MNTTNCFIAL VHAIREIRAF FLSRATGKME FTLYNGERKT FYSRPNNHDN CWLNTILQLF
70 80 90 100 110 120
RYVDEPFFDW VYNSPENLTL AAIKQLEELT GLELHEGGPP ALVIWNIKHL LQTGIGTASR
130 140 150 160 170 180
PARCMVDGTN MCLADFHAGI FLKEQEHAVF ACVTSNGWYA IDDEDFYPWT PDPSDVLVFV
190 200 210 220 230 240
PYDQEPLNGG WKANVQRKLK GAGQSSPATG SQNQSGNTGS IINNYYMQQY QNSMDTQLGD
250 260 270 280 290 300
NAISGGSNEG STDTTSTHTT NTQNNDWFSK LASSAFTGLF GALLADKKTE ETTLLEDRIL
310 320 330 340 350 360
TTRNGHTTST TQSSVGVTYG YSTEEDHVAG PNTSGLETRV VQAERFFKKF LFDWTPDKPF
370 380 390 400 410 420
GHRTKLELPT DHHGVFGHLV DSYAYMRNGW DVEVSAVGNQ FNGGCLLVAM VPEWKTFDTR
430 440 450 460 470 480
EEYQLTLFPH QFISPRTNMT AHITVPYLGV NRYDQYKKHK PWTLVIMVLS PLTVSNTAAT
490 500 510 520 530 540
QIKVYANIAP TYVHVAGELP SKVGIFPVAC SDGYGGLVTT DPKTADPVYG KEYNPPKTNY
550 560 570 580 590 600
PRRFTNLLDV AEACPTFLCF DDGKPYVVTR TDDTRLLAKF DVSLAAKHMS NTYLSGIAQY
610 620 630 640 650 660
YTQYSGTINL HFMFTGSTDS KARYMVAYIP PGVETPPETP EGAAHCIHAE WDTGLNSKFT
670 680 690 700 710 720
FSIPYVSAAD YAYTASDTAE TTNVQGWVCI YQITHGKAED DTLVVSASAG KDFELRLPID
730 740 750 760 770 780
PRSQTTATGE SADPVTTTVE NYGGETQVQR RHHTDVSFIM DRFVKIKSLN PTHVIDLMQT
790 800 810 820 830 840
HQHGLVGALL RAATYYFSDL EIVVRHDGNL TWVPNGAPEA ALSNTGNPTA YNKAPFTRLA
850 860 870 880 890 900
LPYTAPHRVL ATVYNGTNKY SASGSGVRGD FGSLAPRVAR QLPASFNYGA IKAETIHELL
910 920 930 940 950 960
VRMKRAELYC PRPLLAIEVS SQDRHKQKII APGKQLLNFD LLKLAGDVES NPRPFFFADV
970 980 990 1000 1010 1020
RSNFSKLVDT INQMQEDMST KHGPDFNRLV SAFEELATGV KAIRTGLDEA KPWYKLIKLL
1030 1040 1050 1060 1070 1080
SRLSCMAAVA ARTKDPVLVA IMLADTGLEI LDSTFVVKKI SDSLSSLFHV PAPVFSFGAP
1090 1100 1110 1120 1130 1140
VLLAGLVKVA SSFLRSTPED LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW
1150 1160 1170 1180 1190 1200
IASEEKFVTM TDLVLGILEK QRDLNDPSKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA
1210 1220 1230 1240 1250 1260
PAPSKSRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RTDSVWYCPP DPDHFDGYNQ
1270 1280 1290 1300 1310 1320
QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK GKPFNSKVII ATTNLYSGFT
1330 1340 1350 1360 1370 1380
PRTMVCPDAL NRRFHFDIDV SAKDGYKINN KLDIVKALED THTNPVAMFQ YDCALLNGMA
1390 1400 1410 1420 1430 1440
VEMKRMQQDM FKPQPPLQNV YQLVQEVIER VELHEKVSSH PIFKQISIPS QKSVLYFLIE
1450 1460 1470 1480 1490 1500
KGQHEAAIEF FEGMVHDSIK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM
1510 1520 1530 1540 1550 1560
IRETRKRQKM VDDAVNEYIE KANITTDDTT LDEAEKNPLE TSGASTVGFR ERTLTGQRAC
1570 1580 1590 1600 1610 1620
NDVNSEPARP AEEQPQAEGP YTGPLERQRP LKVRAKLPQQ EGPYAGPLER QKPLKVKAKA
1630 1640 1650 1660 1670 1680
PVVKEGPYEG PVKKPVALKV KAKNLIVTES GAPPTDLQKM VMGNTKPVEL ILDGKTVAIC
1690 1700 1710 1720 1730 1740
CATGVFGTAY LVPRHLFAEK YDKIMLDGRA MTDSDYRVFE FEIKVKGQDM LSDAALMVLH
1750 1760 1770 1780 1790 1800
RGNRVRDITK HFRDTARMKK GTPVVGVVNN ADVGRLIFSG EALTYKDIVV CMDGDTMPSL
1810 1820 1830 1840 1850 1860
FAYKAATKAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSKSMLLR MKAHVDPEPQ
1870 1880 1890 1900 1910 1920
HEGLIVDTRD VEERVHVMRK TKLAPTVAHG VFNPEFGPAA LSNKDPRLNE GVVLDEVIFS
1930 1940 1950 1960 1970 1980
KHKGDTKMSA EDKALFRACA ADYASRLHSV LGTANAPLSI YEAIKGVDGL DAMESDTAPG
1990 2000 2010 2020 2030 2040
LPWAFQGKRR GALIDFENGT VGPEVEAALK LMEKREYKFV CQTFLKDEIR PMEKVRAGKT
2050 2060 2070 2080 2090 2100
RIVDVLPVEH ILYTRMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD
2110 2120 2130 2140 2150 2160
VDYSAFDTNH CSDAMNIMFE EVFRTDFGFH PNAEWILKTL VNTEHAYENK RITVEGGMPS
2170 2180 2190 2200 2210 2220
DCSATGIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD DIVVASDYDL DFEALKPHFK
2230 2240 2250 2260 2270 2280
SLGQTITPAD KSDKGFVLGH SITDVTFLKR HFHIDYGTGF YKPVMASKTL EAILSFARRG
2290 2300 2310 2320 2330
TIQEKLTSVA GLAVHSGPDE YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA
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P03308 in FASTA format |
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