CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014678
UniProt Accession
Genbank Protein ID
 U22521 
Genbank Nucleotide ID
Protein Name
 Genome polyprotein 
Protein Synonyms/Alias
 Protein VP0; VP4-VP2; Protein VP4; P1A; Virion protein 4; Protein VP2; P1B; Virion protein 2; Protein VP3; P1C; Virion protein 3; Protein VP1; P1D; Virion protein 1; Protease 2A; P2A; Protein 2A; Protein 2B; P2B; Protein 2C; P2C; Protein 3A; P3A; Protein 3B; P3B; VPg; Protease 3C; P3C; Picornain 3C; RNA-directed RNA polymerase 3D-POL; P3D-POL 
Gene Name
  
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Human enterovirus 71 (strain BrCr) (Ev 71) 
NCBI Taxa ID
 69153 
Lysine Modification
Position
Peptide
Type
References
52SLKQDPDKFANPVKDsumoylation[1]
1600KTIWVEHKLINVLDAsumoylation[1]
Reference
 [1] Sumoylation-promoted enterovirus 71 3C degradation correlates with a reduction in viral replication and cell apoptosis.
 Chen SC, Chang LY, Wang YW, Chen YC, Weng KF, Shih SR, Shih HM.
 J Biol Chem. 2011 Sep 9;286(36):31373-84. [PMID: 21784861] 
Functional Description
 Protein VP1: Forms, together with VP2 and VP3, an icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Protein VP1 mainly forms the vertices of the capsid. VP1 interacts with host cell receptor to provide virion attachment to target cell. After binding to its receptor, the capsid undergoes conformational changes. VP1 N- terminus (that contains an amphipathic alpha-helix) is externalized, VP4 is released and together, they shape a virion- cell connecting channel and a pore in the host membrane through which RNase-protected transfer of the viral genome takes place. After genome has been released, the channel shrinks (By similarity). 
Sequence Annotation
 DOMAIN 1216 1374 SF3 helicase.
 DOMAIN 1958 2073 RdRp catalytic.
 NP_BIND 1240 1247 ATP (Potential).
 ACT_SITE 883 883 For protease 2A activity (By similarity).
 ACT_SITE 901 901 For protease 2A activity (By similarity).
 ACT_SITE 972 972 For protease 2A activity (By similarity).
 ACT_SITE 1588 1588 For protease 3C activity (Potential).
 ACT_SITE 1619 1619 For protease 3C activity (Potential).
 ACT_SITE 1695 1695 For protease 3C activity (By similarity).
 MOD_RES 1529 1529 O-(5'-phospho-RNA)-tyrosine (By
 LIPID 2 2 N-myristoyl glycine; by host (By  
Keyword
 Activation of host autophagy by virus; ATP-binding; Capsid protein; Clathrin-mediated endocytosis of virus by host; Complete proteome; Covalent protein-RNA linkage; Helicase; Host cytoplasm; Host cytoplasmic vesicle; Host gene expression shutoff by virus; Host membrane; Host translation shutoff by virus; Host-virus interaction; Hydrolase; Inhibition of host IFN-mediated response initiation by virus; Inhibition of host innate immune response by virus; Inhibition of host RIG-I by virus; Ion channel; Ion transport; Lipoprotein; Membrane; Myristate; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Pore-mediated penetration of viral genome into host cell; Protease; RNA-binding; RNA-directed RNA polymerase; Thiol protease; Transferase; Transport; Viral attachment to host cell; Viral immunoevasion; Viral ion channel; Viral penetration into host cytoplasm; Viral RNA replication; Virion; Virus endocytosis by host; Virus entry into host cell. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2193 AA 
Protein Sequence
MGSQVSTQRS GSHENSNSAT EGSTINYTTI NYYKDSYAAT AGKQSLKQDP DKFANPVKDI 60
FTEMAAPLKS PSAEACGYSD RVAQLTIGNS TITTQEAANI IVGYGEWPSY CSDNDATAVD 120
KPTRPDVSVN RFYTLDTKLW EKSSKGWYWK FPDVLTETGV FGPNAQFHYL YRSGFCIHVQ 180
CNASKFHQGA LLVAVLPEYV IGTVAGGTGT ENSHPPYKQT QPGADGFELQ HPYVLDAGIP 240
ISQLTVCPHQ WINLRTNNCA TIIVPYMNTL PFDSALNHCN FGLLVVPISP LDFDQGATPV 300
IPITITLAPM CSEFAGLRQA VTQGFPTELK PGTNQFLTTD DGVSAPILPN FHPTPCIHIP 360
GEVRNLLELC QVETILEVNN VPTNATSLME RLRFPVSAQA GKGELCAVFR ADPGRDGPWQ 420
STMLGQLCGY YTQWSGSLEV TFMFTGSFMA TGKMLIAYTP PGGPLPKDRA TAMLGTHVIW 480
DFGLQSSVTL VIPWISNTHY RAHARDGVFD YYTTGLVSIW YQTNYVVPIG APNTAYIIAL 540
AAAQKNFTMK LCKDTSDILE TATIQGDRVA DVIESSIGDS VSKALTPALP APTGPDTQVS 600
SHRLDTGKVP ALQAAEIGAS SNASDESMIE TRCVLNSHST AETTLDSFFS RAGLVGEIDL 660
PLKGTTNPNG YANWDIDITG YAQMRRKVEL FTYMRFDAEF TFVACTPTGR VVPQLLQYMF 720
VPPGAPKPDS RDSLAWPTAT NPSVFVKSSD PPAQVSVPFM SPASAYQWFY DGYPTFGEHK 780
QEKDLEYGAC PNNMMGTFSV RTVGSSKSEY SLVIRIYMRM KHVRAWIPRP MRNQNYLFKS 840
NPNYAGDSIK PTGTSRTAIT TLGKFGQQSG AIYVGNFRVV NRHLATHTDW ANLVWEDSSR 900
DLLVSSTTAQ GCDTIARCNC QTGVYYCNSR RKHYPVSFSK PSLVFVEASE YYPARYQSHL 960
MLAEGHSEPG DCGGILRCQH GVVGIVSTGG SGLVGFADVR DLLWLDEEAM EQGVSDYIKG 1020
LGRAFGTGFT DAVSREVEAL KNHLIGSEGA VEKILKNLVK LISALVIVIR SDYDMVTLTA 1080
TLALIGCHGS PWAWIKSKTA SILGIPMAQK QSASWLKKFN DMANAAKGLE WIFNKISKFI 1140
DWLKEKIIPA AKEKVEFLNN LKQLPLLENQ VSNLEQSAAS QEDLEAMFGN VIYLAHFCRK 1200
FQPLYATEAK RVYALEKRMN NYMQFKSKHR IEPVCLIIRG SPGTGKSLAT GIIARAIADK 1260
YRSSVYSLPP DPDHFDGYKQ QVVAVMDDLC QNPDGKDMSL FCQMVSTVDF VPPMASLEEK 1320
GVSFTSKFVI ASTNASNIIV PTVSDSDAIR RRFYMDCDIE VTDSYKTDLG RLDAGRAAKL 1380
CTENNTANFK RCSPLVCGKA IQLRDRKSKV RYSVDTVVSE LIREYNNRSA IGNTIEALFQ 1440
GPPKFRPIRI SLEEKPAPDA ISDLLASVDS EEVRQYCREQ GWIIPETPTN VERHLNRAVL 1500
VMQSIATVVA VVSLVYVIYK LFAGFQGAYS GAPKPILKKP VLRTATVQGP SLDFALSLLR 1560
RNIRQAQTDQ GHFTMLGVRD RLAILPRHSQ PGKTIWVEHK LINVLDAVEL VDEQGVNLEL 1620
TLVTLDTNEK FRDITKCIPE VITGASDATL VINTEHIPSM FVPVGDVVQY GFLNLSGKPT 1680
HRTMMYNFPT KPGQCGGVVT SVGKIIGIHI GGNGRQAFCA GLKRSYFASE QGEIQWMKPN 1740
RETGRLNING PTRTKLEPSV FHDVFEGNKE PAVLTSKDPR LEVDFEQALF SKYVGNTLHE 1800
PDEYVTQAAL HYANQLKQLD INTSKMSMEE ACYGTEYLEA IDLHTSAGYP YSALGIKKRD 1860
ILDPVTRDTS RMKLYMDKYG LDLPNSTYVK DELSSLDKIR KGESRLIEAS SLNDPVYPRL 1920
TFGHLYEVFH ANPGTVTGSA VGCNPDVFWS KLPILLPGSL FAFDYSGYDA SLSPVWFRAL 1980
ELVLREIGYS EEAVSLIEGI NHTHHVYRNK TYCVLGGMPS GCSGTSIFNS MINNIIIRTL 2040
LIKTFKGIDL DELKMVAYGD DVLASYPFPI DCLEWGKTGK EYGLTMTPAD KSPCFNEVTW 2100
ENATFLKRGF LPDHQFPFLI HPTMPMREIH ESIRWTKDAR NTQDHVRSLC LLAWHNGKEE 2160
YEKFVSTIRS VPIGRALAIP NLENLRRNWL ELF 2193 
Gene Ontology
 GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IEA:UniProtKB-KW.
 GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0003724; F:RNA helicase activity; IEA:InterPro.
 GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
 GO:0006811; P:ion transport; IEA:UniProtKB-KW.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
 GO:0039540; P:suppression by virus of host RIG-I activity; IEA:UniProtKB-KW.
 GO:0039501; P:suppression by virus of host type I interferon production; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:InterPro.
 GO:0019062; P:viral attachment to host cell; IEA:UniProtKB-KW.
 GO:0075512; P:viral entry into host cell via clathrin-mediated endocytosis; IEA:UniProtKB-KW.
 GO:0019079; P:viral genome replication; IEA:InterPro. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR000605; Helicase_SF3_ssDNA/RNA_vir.
 IPR014759; Helicase_SF3_ssRNA_vir.
 IPR027417; P-loop_NTPase.
 IPR014838; P3A.
 IPR000081; Peptidase_C3.
 IPR000199; Peptidase_C3A/C3B_picornavir.
 IPR003138; Pico_P1A.
 IPR002527; Pico_P2B.
 IPR001676; Picornavirus_capsid.
 IPR001205; RNA-dir_pol_C.
 IPR007094; RNA-dir_pol_PSvirus.
 IPR009003; Trypsin-like_Pept_dom. 
Pfam
 PF08727; P3A
 PF00548; Peptidase_C3
 PF02226; Pico_P1A
 PF00947; Pico_P2A
 PF01552; Pico_P2B
 PF00680; RdRP_1
 PF00073; Rhv
 PF00910; RNA_helicase 
SMART
 SM00382; AAA 
PROSITE
 PS50507; RDRP_SSRNA_POS
 PS51218; SF3_HELICASE_2 
PRINTS