PP220_ASFB7
ID PP220_ASFB7 Reviewed; 2475 AA.
AC Q08358; Q65287;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Polyprotein pp220 {ECO:0000303|PubMed:30185597};
DE AltName: Full=220 kDa polyprotein;
DE Contains:
DE RecName: Full=p34 {ECO:0000303|PubMed:30185597};
DE Contains:
DE RecName: Full=p14 {ECO:0000303|PubMed:30185597};
DE Contains:
DE RecName: Full=p37 {ECO:0000303|PubMed:30185597};
DE Contains:
DE RecName: Full=p150 {ECO:0000303|PubMed:30185597};
DE Contains:
DE RecName: Full=p5 {ECO:0000303|PubMed:30185597};
DE Flags: Precursor;
GN OrderedLocusNames=Ba71V-92; ORFNames=CP2475L;
OS African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10498;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MYRISTOYLATION AT GLY-2, AND PROTEOLYTIC
RP CLEAVAGE (POLYPROTEIN PP220).
RX PubMed=8335009; DOI=10.1002/j.1460-2075.1993.tb05960.x;
RA Simon-Mateo C., Andres G., Vinuela E.;
RT "Polyprotein processing in African swine fever virus: a novel gene
RT expression strategy for a DNA virus.";
RL EMBO J. 12:2977-2987(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA Rodriguez J.F., Vinuela E.;
RT "Analysis of the complete nucleotide sequence of African swine fever
RT virus.";
RL Virology 208:249-278(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 391-808.
RX PubMed=3245132; DOI=10.1007/bf00572708;
RA Lopez-Otin C., Simon C., Mendez E., Vinuela E.;
RT "Mapping and sequence of the gene encoding protein p37, a major structural
RT protein of African swine fever virus.";
RL Virus Genes 1:291-303(1988).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION (POLYPROTEIN PP220).
RX PubMed=9032369; DOI=10.1128/jvi.71.3.2331-2341.1997;
RA Andres G., Simon-Mateo C., Vinuela E.;
RT "Assembly of African swine fever virus: role of polyprotein pp220.";
RL J. Virol. 71:2331-2341(1997).
RN [5]
RP FUNCTION (POLYPROTEIN PP220).
RX PubMed=11861832; DOI=10.1128/jvi.76.6.2654-2666.2002;
RA Andres G., Garcia-Escudero R., Salas M.L., Rodriguez J.M.;
RT "Repression of African swine fever virus polyprotein pp220-encoding gene
RT leads to the assembly of icosahedral core-less particles.";
RL J. Virol. 76:2654-2666(2002).
RN [6]
RP SUBCELLULAR LOCATION (P150), SUBCELLULAR LOCATION (P34), SUBCELLULAR
RP LOCATION (P37), SUBCELLULAR LOCATION (P14), FUNCTION (P34), FUNCTION (P37),
RP FUNCTION (P14), AND FUNCTION (P150).
RX PubMed=12438573; DOI=10.1128/jvi.76.24.12473-12482.2002;
RA Andres G., Alejo A., Salas J., Salas M.L.;
RT "African swine fever virus polyproteins pp220 and pp62 assemble into the
RT core shell.";
RL J. Virol. 76:12473-12482(2002).
RN [7]
RP SUBCELLULAR LOCATION (P150), AND SUBCELLULAR LOCATION (P34).
RX PubMed=12525602; DOI=10.1128/jvi.77.3.1682-1690.2003;
RA Heath C.M., Windsor M., Wileman T.;
RT "Membrane association facilitates the correct processing of pp220 during
RT production of the major matrix proteins of African swine fever virus.";
RL J. Virol. 77:1682-1690(2003).
RN [8]
RP SUBCELLULAR LOCATION (P37).
RX PubMed=17580096; DOI=10.1016/j.virusres.2007.05.009;
RA Eulalio A., Nunes-Correia I., Salas J., Salas M.L., Simoes S.,
RA Pedroso de Lima M.C.;
RT "African swine fever virus p37 structural protein is localized in nuclear
RT foci containing the viral DNA at early post-infection times.";
RL Virus Res. 130:18-27(2007).
RN [9]
RP SUBCELLULAR LOCATION (P34), SUBCELLULAR LOCATION (P150), SUBCELLULAR
RP LOCATION (P37), SUBCELLULAR LOCATION (P14), AND SUBCELLULAR LOCATION (P5).
RX PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA Alejo A., Matamoros T., Guerra M., Andres G.;
RT "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL J. Virol. 92:0-0(2018).
RN [10]
RP INDUCTION (POLYPROTEIN PP220).
RX PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA Dixon L., Werner F.;
RT "The African Swine Fever Virus Transcriptome.";
RL J. Virol. 94:0-0(2020).
RN [11]
RP SUBCELLULAR LOCATION (P34).
RX PubMed=33429879; DOI=10.3390/v13010077;
RA Aicher S.M., Monaghan P., Netherton C.L., Hawes P.C.;
RT "Unpicking the Secrets of African Swine Fever Viral Replication Sites.";
RL Viruses 13:0-0(2021).
CC -!- FUNCTION: [Polyprotein pp220]: Essential for the core assembly. Its
CC myristoyl moiety may function as a membrane-anchoring signal to bind
CC the developing core shell to the inner viral envelope.
CC {ECO:0000269|PubMed:11861832}.
CC -!- FUNCTION: [p34]: The structural protein p34 is a component of the virus
CC core shell. {ECO:0000269|PubMed:12438573}.
CC -!- FUNCTION: [p14]: The structural protein p14 is a component of the virus
CC core shell. {ECO:0000269|PubMed:12438573}.
CC -!- FUNCTION: [p37]: The structural protein p37 is a component of the virus
CC core shell. {ECO:0000269|PubMed:12438573}.
CC -!- FUNCTION: [p150]: The structural protein p150 is a component of the
CC virus core shell. {ECO:0000269|PubMed:12438573}.
CC -!- SUBCELLULAR LOCATION: [Polyprotein pp220]: Host cytoplasm, host
CC perinuclear region {ECO:0000269|PubMed:9032369}. Note=Found in
CC perinuclear cytoplasmic viral factories during assembly.
CC {ECO:0000269|PubMed:9032369}.
CC -!- SUBCELLULAR LOCATION: [p34]: Virion {ECO:0000269|PubMed:30185597}. Host
CC cytoplasm, host perinuclear region {ECO:0000269|PubMed:12525602}.
CC Note=Localizes to the viral factory at 16 hpi (PubMed:33429879). In the
CC virion, located in the core shell, which functions like a matrix
CC between the DNA-containing nucleoid and the inner envelope
CC (PubMed:12438573). {ECO:0000269|PubMed:12438573,
CC ECO:0000269|PubMed:33429879}.
CC -!- SUBCELLULAR LOCATION: [p14]: Virion {ECO:0000269|PubMed:30185597}. Host
CC cytoplasm, host perinuclear region. Note=Found in perinuclear
CC cytoplasmic viral factories during assembly. In the virion, located in
CC the core shell, which functions like a matrix between the DNA-
CC containing nucleoid and the inner envelope (PubMed:12438573).
CC {ECO:0000269|PubMed:12438573}.
CC -!- SUBCELLULAR LOCATION: [p37]: Virion {ECO:0000269|PubMed:30185597}. Host
CC cytoplasm, host perinuclear region {ECO:0000269|PubMed:17580096}. Host
CC nucleus {ECO:0000269|PubMed:17580096}. Note=Found in perinuclear
CC cytoplasmic viral factories during assembly. In the virion, located in
CC the core shell, which functions like a matrix between the DNA-
CC containing nucleoid and the inner envelope (PubMed:12438573).
CC {ECO:0000269|PubMed:12438573}.
CC -!- SUBCELLULAR LOCATION: [p150]: Virion {ECO:0000269|PubMed:12438573,
CC ECO:0000269|PubMed:30185597}. Host cytoplasm, host perinuclear region
CC {ECO:0000269|PubMed:12525602}. Note=Found in perinuclear cytoplasmic
CC viral factories during assembly. In the virion, located in the core
CC shell, which functions like a matrix between the DNA-containing
CC nucleoid and the inner envelope (PubMed:12438573).
CC {ECO:0000269|PubMed:12438573}.
CC -!- SUBCELLULAR LOCATION: [p5]: Virion {ECO:0000269|PubMed:30185597}.
CC -!- INDUCTION: [Polyprotein pp220]: Expressed in the late phase of the
CC viral replicative cycle. {ECO:0000269|PubMed:32075923}.
CC -!- PTM: [Polyprotein pp220]: The polyprotein is not glycosylated.
CC -!- PTM: [Polyprotein pp220]: Specific enzymatic cleavages in vivo by the
CC viral pS273R protease yield mature proteins.
CC {ECO:0000269|PubMed:8335009}.
CC -!- SIMILARITY: Belongs to the asfivirus polyprotein pp220 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA61203.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z22777; CAA80455.1; -; Genomic_DNA.
DR EMBL; U18466; AAA65321.1; -; Genomic_DNA.
DR EMBL; X87965; CAA61203.1; ALT_FRAME; Genomic_DNA.
DR PIR; S35307; S35307.
DR RefSeq; NP_042785.1; NC_001659.2.
DR ELM; Q08358; -.
DR iPTMnet; Q08358; -.
DR GeneID; 22220321; -.
DR KEGG; vg:22220321; -.
DR Proteomes; UP000000624; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019069; P:viral capsid assembly; IDA:CACAO.
PE 1: Evidence at protein level;
KW Coiled coil; Host cytoplasm; Host nucleus; Late protein; Lipoprotein;
KW Myristate; Reference proteome; Virion.
FT INIT_MET 1
FT /note="Removed; by host"
FT CHAIN 2..44
FT /note="p5"
FT /id="PRO_0000454695"
FT CHAIN 45..2475
FT /note="Polyprotein pp220"
FT /id="PRO_0000355531"
FT CHAIN 45..368
FT /note="p34"
FT /id="PRO_0000036723"
FT CHAIN 369..522
FT /note="p14"
FT /id="PRO_0000036724"
FT CHAIN 523..893
FT /note="p37"
FT /id="PRO_0000036725"
FT CHAIN 894..2475
FT /note="p150"
FT /id="PRO_0000036726"
FT COILED 2185..2212
FT /evidence="ECO:0000255"
FT SITE 44..45
FT /note="Cleavage; by viral protease S273R"
FT /evidence="ECO:0000305|PubMed:30185597"
FT SITE 368..369
FT /note="Cleavage; by viral protease S273R"
FT /evidence="ECO:0000305|PubMed:30185597"
FT SITE 522..523
FT /note="Cleavage; by viral protease S273R"
FT /evidence="ECO:0000305|PubMed:30185597"
FT SITE 893..894
FT /note="Cleavage; by viral protease S273R"
FT /evidence="ECO:0000305|PubMed:30185597"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000269|PubMed:8335009"
SQ SEQUENCE 2475 AA; 281482 MW; 5D0415A506BE218E CRC64;
MGNRGSSTSS RPPLSSEANL YAKLQDHIQR QTRPFSGGGY FNGGGDKNPV QHIKDYHIDS
VSSKAKLRVI EGIIRAIAKI GFKVDTKQPI EDILKDIKKQ LPDPRAGSTF VKNAEKQETV
CKMIADAINQ EFIDLGQDKL IDTTDGAASI CRQIVLYINS LTHGLRAEYL DVHGSIENTL
ENIKLLNDAI KQLHERMVTE VTKAAPNEEV INAVTMIEAV YRRLLNEQNL QINILTNFID
NILTPTQKEL DKLQTDEVDI IKLLNDTNSV LGTKNFGKVL SYTLCNLGIA ASVANKINKA
LQKVGLKVEQ YLQSKNWAEF DKELDLKRFS GLVSAENIAE FEKAVNLLRQ TFNERHKILE
NSCAKKGGDE EKTPLDRRIE AQRLDRKHIL MEFLNKSTQA YNDFLENVKK IGIKLVKEIA
LTPNITRLRD ALSRINDMGT IALDLSLIGF YTNAAAREER ETFLTQFMLV KNVLEEQSKI
DPNFKNLYDS CSRLLQIIDF YTDIVQKKYG GGEDCECTRV GGAALTVEEL GLSKAARSQV
DLNQAINTFM YYYYVAQIYS NLTHNKQEFQ SYEENYATIL GDAIAGRLMQ LDTEKNARIN
SPAVDLARGH VGPNPGGAQE ADWKAAVSAI ELEYDVKRRF YRALEGLDLY LKNITKTFVN
NIDSIQTVQQ MLDGVRIIGR WFTEATGDTL AQVFESFPTS AGNDSNVFTD NAPAGHYYEK
VAAEIQQGRS VGTLRPVRAS QAKNIRDLIG RSLSNFQALK NIINAFARIG DMLGGEELRQ
MVPMSPLQIY KTLLEYIQHS ALSVGLKNLN QSEIGGQRVA LARTPEEAAQ RVYLSTVRVN
DALSTRWETE DVFFTFMLKS MAAKIFIVLG IYDMFERPEP VYKLIPTRMI LGGADELEPE
VIPEAAELYF RLPRLAEFYQ KLFSFRDENV QISMLPELEG IFSGLIRIIF MRPIELINIG
DYSETEIRQL IKEINVIYQH FNLEYGEQEA TKKALIHFVN EINRRFGVIT RTEWEKFQRI
VQEARTMNDF GMMNQTNYSI LPDEDGYTQS SQLLPSDRFI SPSTQPTPKW RPALYNIDSV
DVQTGMLQPN SQWDLVQKFR KQLSEMFEDP SLQQELGKVS YQELIRQAIN ELKKEHTDKI
QIVSKLIQGS ESLADTDVNK IFLFHETVIT GLNLLSAIYV LLNNFRNNIK GLDLDTIQKS
IIEWLRETQA ANVNRANLID WLGRKHGAIS EIRNPGLVVK ENDVRLSRVY PDPTTNATAP
QDQNLVTETL FAWIVPYVGI PAGGGVRAEQ ELAARYLVDN QRIMQLLLTN IFEMTSSFNK
MVQVRFPETS TAQVHLDFTG LISLIDSLMA DTKYFLNLLR PHIDKNIIQY YENRSNPGSF
YWLEEHLIDK LIKPPTDAGG RPLPGGELGL EGVNQIINKT YILLTKPYNV LQLRGGVQRR
DAANIQINNN PQPSERFEQY GRVFSRLVFY DALENNSGLR VEQVVLGDFR LSNLIRTNNA
QEENTLSYWD NMAPRTYANV NDAANNLRRY RLYGSDYGIQ NNRSMMMVFN QLVASYIARF
YDAPSGKIYL NLINAFANGN FSQAVMELGY THPDLARDNI AFGHRGDPTE QSVLLLSLGL
MLQRLIKDTN RQGLSQHLIS TLTEIPIYLK ENYRANLPLF NKMFNILISQ GELLKQFIQY
TNVQLARPNL MGLLGANNDS VIYYNNNINV PMTGLSVGQA ALRGIGGVFR PNVTLMPLGD
AQNNTSDVVR KRLVAVIDGI IRGSHTLADS AMEVLHELTD HPIYLETEEH FIQNYMSRYN
KEPLMPFSLS LYYLRDLRIE NNEVYDPLLY PNLESGSPEF KLLYGTRKLL GNDPVQLSDM
PGVQLIMKNY NETVVAREQI TPTRFEHFYT HAIQALRFIV NIRSFKTVMM YNENTFGGVN
LISENRDDKP IITAGIGMNA VYSLRKTLQD VISFVESSYQ EEQINHIHKI VSPKGQTRTL
GSNRERERIF NLFDMNIIPI NVNALMRSIP LANIYNYDYS FEEIACLMYG ISAEKVRSLN
TAAPQPDIAE VLNIPNRPPM NTREFMLKLL INPYVSVSIT QYGNELMSKG SAGYMSRIFR
GDNALNMGRP KFLSDQIFNK VLFGSLYPTQ FDYDEAGPGL AAGIQRGREQ WGQPLSEYIN
QALHELVRTI RIPQKLRVLR NIIVKNQLIA DLTTIREQLV SMRREVENMI QTPEIQNNPT
PEVIAAAQNW TQQYRARVDT LINFIGNIGQ PNSMLDLIQT ITPVTVRAQL GVIFNRHGIP
VPHPRQILQT DDEATQWFMT NILNIPAIIM TPFTDLANDL RTFLETLERY VFNVPRWLGP
STGRVARAPV RMAPRDMRHP ISYTENSVLT YITEQNREEG PWSIVKQVGV GIQKPTLVQI
GKDRFDTRLI RNLIFITNIQ RLLRLRLNLE LSQFRNVLVS PDHIINPSIT EYGFSITGPS
ETFSDKQYDS DIRIL
