POLG_EC16H
ID POLG_EC16H Reviewed; 862 AA.
AC Q66790;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 02-DEC-2020, entry version 109.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=P1;
DE Contains:
DE RecName: Full=Capsid protein VP0;
DE AltName: Full=VP4-VP2;
DE Contains:
DE RecName: Full=Capsid protein VP4;
DE AltName: Full=P1A;
DE AltName: Full=Virion protein 4;
DE Contains:
DE RecName: Full=Capsid protein VP2;
DE AltName: Full=P1B;
DE AltName: Full=Virion protein 2;
DE Contains:
DE RecName: Full=Capsid protein VP3;
DE AltName: Full=P1C;
DE AltName: Full=Virion protein 3;
DE Contains:
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=P1D;
DE AltName: Full=Virion protein 1;
DE Flags: Fragment;
OS Echovirus 16 (strain Harrington).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Enterovirus; Enterovirus B.
OX NCBI_TaxID=103910;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8627260; DOI=10.1099/0022-1317-77-4-715;
RA Huttunen P., Santti J., Pulli T., Hyypiae T.;
RT "The major echovirus group is genetically coherent and related to coxsackie
RT B viruses.";
RL J. Gen. Virol. 77:715-725(1996).
CC -!- FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The
CC capsid is 300 Angstroms in diameter, composed of 60 copies of each
CC capsid protein and enclosing the viral positive strand RNA genome (By
CC similarity). Capsid protein VP1 mainly forms the vertices of the capsid
CC (By similarity). Capsid protein VP1 interacts with host cell receptor
CC to provide virion attachment to target host cells (By similarity). This
CC attachment induces virion internalization (By similarity). Tyrosine
CC kinases are probably involved in the entry process (By similarity).
CC After binding to its receptor, the capsid undergoes conformational
CC changes (By similarity). Capsid protein VP1 N-terminus (that contains
CC an amphipathic alpha-helix) and capsid protein VP4 are externalized (By
CC similarity). Together, they shape a pore in the host membrane through
CC which viral genome is translocated to host cell cytoplasm (By
CC similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The
CC capsid is 300 Angstroms in diameter, composed of 60 copies of each
CC capsid protein and enclosing the viral positive strand RNA genome (By
CC similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The
CC capsid is 300 Angstroms in diameter, composed of 60 copies of each
CC capsid protein and enclosing the viral positive strand RNA genome (By
CC similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid
CC shell (By similarity). After binding to the host receptor, the capsid
CC undergoes conformational changes (By similarity). Capsid protein VP4 is
CC released, Capsid protein VP1 N-terminus is externalized, and together,
CC they shape a pore in the host membrane through which the viral genome
CC is translocated into the host cell cytoplasm (By similarity).
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Capsid protein VP0]: Component of immature procapsids, which
CC is cleaved into capsid proteins VP4 and VP2 after maturation (By
CC similarity). Allows the capsid to remain inactive before the maturation
CC step (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Capsid protein VP0]: Interacts with capsid protein VP1 and
CC capsid protein VP3 to form heterotrimeric protomers.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Capsid protein VP1]: Interacts with capsid protein VP0, and
CC capsid protein VP3 to form heterotrimeric protomers (By similarity).
CC Five protomers subsequently associate to form pentamers which serve as
CC building blocks for the capsid (By similarity). Interacts with capsid
CC protein VP2, capsid protein VP3 and capsid protein VP4 following
CC cleavage of capsid protein VP0 (By similarity).
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Capsid protein VP2]: Interacts with capsid protein VP1 and
CC capsid protein VP3 in the mature capsid.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Capsid protein VP3]: Interacts with capsid protein VP0 and
CC capsid protein VP1 to form heterotrimeric protomers (By similarity).
CC Five protomers subsequently associate to form pentamers which serve as
CC building blocks for the capsid (By similarity). Interacts with capsid
CC protein VP4 in the mature capsid (By similarity). Interacts with
CC protein 2C; this interaction may be important for virion morphogenesis
CC (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Capsid protein VP4]: Interacts with capsid protein VP1 and
CC capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion
CC {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the
CC viral proteases yield processing intermediates and the mature proteins.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [Capsid protein VP0]: Myristoylation is required for the formation
CC of pentamers during virus assembly. Further assembly of 12 pentamers
CC and a molecule of genomic RNA generates the provirion.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [Capsid protein VP0]: During virion maturation, immature virions
CC are rendered infectious following cleavage of VP0 into VP4 and VP2.
CC This maturation seems to be an autocatalytic event triggered by the
CC presence of RNA in the capsid and it is followed by a conformational
CC change infectious virion. {ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [Capsid protein VP4]: Myristoylation is required during RNA
CC encapsidation and formation of the mature virus particle.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC {ECO:0000305}.
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DR EMBL; X89545; CAA61723.1; -; Genomic_RNA.
DR SMR; Q66790; -.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd00205; rhv_like; 3.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 4.10.80.10; -; 1.
DR InterPro; IPR003138; Pico_P1A.
DR InterPro; IPR036988; Pico_P1A_sf.
DR InterPro; IPR001676; Picornavirus_capsid.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF02226; Pico_P1A; 1.
DR Pfam; PF00073; Rhv; 3.
PE 3: Inferred from homology;
KW Autocatalytic cleavage; Capsid protein;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Host cytoplasm;
KW Host gene expression shutoff by virus; Host-virus interaction; Lipoprotein;
KW Magnesium; Myristate;
KW Pore-mediated penetration of viral genome into host cell;
KW Viral attachment to host cell; Viral penetration into host cytoplasm;
KW Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT CHAIN 2..>862
FT /note="Genome polyprotein"
FT /id="PRO_0000449115"
FT CHAIN 2..862
FT /note="P1"
FT /id="PRO_0000449116"
FT CHAIN 2..331
FT /note="Capsid protein VP0"
FT /id="PRO_0000311060"
FT CHAIN 2..69
FT /note="Capsid protein VP4"
FT /id="PRO_0000039725"
FT CHAIN 70..331
FT /note="Capsid protein VP2"
FT /id="PRO_0000039726"
FT CHAIN 332..570
FT /note="Capsid protein VP3"
FT /id="PRO_0000039727"
FT CHAIN 571..>862
FT /note="Capsid protein VP1"
FT /id="PRO_0000039728"
FT SITE 69..70
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT SITE 331..332
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT NON_TER 862
SQ SEQUENCE 862 AA; 95399 MW; 59587E197126595C CRC64;
MGAQVSTQKT GAHETLLEAA QGATINYTNI NYYKDAASNS ANRQDFSQDP SKFTEPVKDI
MIKSMPALNS PSAEECGYSD RVRSITLGNS TITTQESANV VVAYGRWPKY LEDDQATAED
QPTQPDVATC RFYTLESVQW EANSAGWWWK FPEALKDMGL FGQNMYYHYL GRAGYTIHVQ
CNASKFHQGC LLVVCVPEAE MGCAKPDENV DATNLTNGEN TCELTAGAAP AEKGKVQTAV
CNATMGVAVG NLTIFPHQWI NLRTNNCATI VMPYINSVPM DNMFRHYNFT LMVIPFVPLT
SMGGSTYVPI TVTIAPMCAE YNGLRLSTQH QGLPVMNVPG SNQFLTSDNF QSPCAMPEYD
VTPPLDIPGE VNNLMEVAEV DSVVPVNNLS DNVKTIKAYQ IPVSAGDSSR PEAVFKFQLD
PGSGSVLKHT LLGEIINYYA HWSGSIKLTF VFCGSAMATG KLLIAYSPPG ASAPATRKDA
MLGTHIIWDL GLQSSCVLCV PWISQTHYRM VERDEYTTAG YISCWYQTNI IVPPDTPSQC
YMLCLASACN DFSVRMLKDT PFIQQEAKLQ GEPGKAIESA ISRVADTISS GPTNSEQVPA
LTAAETGHTS QVVPGDTIQT RHVKNYHSRS ESTIENFLCR SACVHIARYE AGANASNEDR
FVRWEINNKE LVQLRRKCEM FTYLRYDVEV TFVITSQQDQ GTDLSQDMPV LTHQVMYVPP
GGSVTKQGDS YAWQTSTNPS VFWTEGNAPP RMSIPFISIG NAYSSFYDGW SHFSQKGVYG
YNTLNKMGTL FVRHVNKETP KPVTSTVRVY FKPKHIRAWI PRPPRLCPYK YKANVNFDVT
AITDSRLTIT TVPQVEHNLR TA
