Q08358 (PP220_ASFB7) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polyprotein pp220

Alternative name(s):
220 kDa polyprotein

Cleaved into the following 4 chains:

1. p34
2. p14
3. p37
4. p150

Gene names

Ordered Locus Names:	Ba71V-92
ORF Names:	CP2475L

Organism

African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) (ASFV) [Reference proteome]

Taxonomic identifier

10498 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Asfarviridae › Asfivirus › African swine fever virus

Virus host

Ornithodoros (relapsing fever ticks) [TaxID: 6937]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length	2475 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Polyprotein pp220 is essential for the core assembly. Its myristoyl moiety may function as a membrane-anchoring signal to bind the developing core shell to the inner viral envelope. Ref.4 Ref.5 The structural protein p34 is a component of the virus core shell. Ref.4 Ref.5 The structural protein p14 is a component of the virus core shell. Ref.4 Ref.5 The structural protein p37 is a component of the virus core shell. Ref.4 Ref.5 The structural protein p150 is a component of the virus core shell. Ref.4 Ref.5
Subcellular location	Polyprotein pp220: Host cytoplasm › host perinuclear region. Note: Found in perinuclear cytoplasmic viral factories during assembly. Ref.4 Ref.6 Ref.7 Ref.8 p34: Virion Potential. Host cytoplasm › host perinuclear region. Note: Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope. Ref.4 Ref.6 Ref.7 Ref.8 p14: Virion Potential. Host cytoplasm › host perinuclear region. Note: Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope. Ref.4 Ref.6 Ref.7 Ref.8 p37: Virion Potential. Host cytoplasm › host perinuclear region. Host nucleus. Note: Nuclear at early stages of infection. Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope. Ref.4 Ref.6 Ref.7 Ref.8 p150: Virion Potential. Host cytoplasm › host perinuclear region. Note: Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope. Ref.4 Ref.6 Ref.7 Ref.8
Induction	Expressed late in the infection.
Post-translational modification	The polyprotein is not glycosylated. Specific enzymatic cleavages in vivo yield mature proteins.
Sequence similarities	Belongs to the asfivirus polyprotein pp220 family.
Sequence caution	The sequence CAA61203.1 differs from that shown. Reason: Frameshift at position 713.

Ontologies

Keywords
Cellular component	Host cytoplasm Host nucleus Virion
Developmental stage	Late protein
Domain	Coiled coil
PTM	Lipoprotein Myristate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell host cell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell virion Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed; by host
	Propeptide	2 – 45	44			PRO_0000036722
	Chain	46 – 894	849	Polyprotein pp220 Potential		PRO_0000355531
	Chain	46 – 369	324	p34 Potential		PRO_0000036723
	Chain	370 – 523	154	p14 Potential		PRO_0000036724
	Chain	524 – 894	371	p37 Potential		PRO_0000036725
	Chain	895 – 2475	1581	p150 Potential		PRO_0000036726
Regions
	Coiled coil	2185 – 2212	28	Potential
	Compositional bias	551 – 554	4	Poly-Tyr
Sites
	Site	45 – 46	2	Cleavage; by viral protease S273R Potential
	Site	369 – 370	2	Cleavage; by viral protease S273R Potential
	Site	523 – 524	2	Cleavage; by viral protease S273R Potential
	Site	894 – 895	2	Cleavage; by viral protease S273R Potential
Amino acid modifications
	Lipidation	2	1	N-myristoyl glycine; by host Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q08358 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 5D0415A506BE218E	FASTA	2,475	281,482
	10 20 30 40 50 60 MGNRGSSTSS RPPLSSEANL YAKLQDHIQR QTRPFSGGGY FNGGGDKNPV QHIKDYHIDS 70 80 90 100 110 120 VSSKAKLRVI EGIIRAIAKI GFKVDTKQPI EDILKDIKKQ LPDPRAGSTF VKNAEKQETV 130 140 150 160 170 180 CKMIADAINQ EFIDLGQDKL IDTTDGAASI CRQIVLYINS LTHGLRAEYL DVHGSIENTL 190 200 210 220 230 240 ENIKLLNDAI KQLHERMVTE VTKAAPNEEV INAVTMIEAV YRRLLNEQNL QINILTNFID 250 260 270 280 290 300 NILTPTQKEL DKLQTDEVDI IKLLNDTNSV LGTKNFGKVL SYTLCNLGIA ASVANKINKA 310 320 330 340 350 360 LQKVGLKVEQ YLQSKNWAEF DKELDLKRFS GLVSAENIAE FEKAVNLLRQ TFNERHKILE 370 380 390 400 410 420 NSCAKKGGDE EKTPLDRRIE AQRLDRKHIL MEFLNKSTQA YNDFLENVKK IGIKLVKEIA 430 440 450 460 470 480 LTPNITRLRD ALSRINDMGT IALDLSLIGF YTNAAAREER ETFLTQFMLV KNVLEEQSKI 490 500 510 520 530 540 DPNFKNLYDS CSRLLQIIDF YTDIVQKKYG GGEDCECTRV GGAALTVEEL GLSKAARSQV 550 560 570 580 590 600 DLNQAINTFM YYYYVAQIYS NLTHNKQEFQ SYEENYATIL GDAIAGRLMQ LDTEKNARIN 610 620 630 640 650 660 SPAVDLARGH VGPNPGGAQE ADWKAAVSAI ELEYDVKRRF YRALEGLDLY LKNITKTFVN 670 680 690 700 710 720 NIDSIQTVQQ MLDGVRIIGR WFTEATGDTL AQVFESFPTS AGNDSNVFTD NAPAGHYYEK 730 740 750 760 770 780 VAAEIQQGRS VGTLRPVRAS QAKNIRDLIG RSLSNFQALK NIINAFARIG DMLGGEELRQ 790 800 810 820 830 840 MVPMSPLQIY KTLLEYIQHS ALSVGLKNLN QSEIGGQRVA LARTPEEAAQ RVYLSTVRVN 850 860 870 880 890 900 DALSTRWETE DVFFTFMLKS MAAKIFIVLG IYDMFERPEP VYKLIPTRMI LGGADELEPE 910 920 930 940 950 960 VIPEAAELYF RLPRLAEFYQ KLFSFRDENV QISMLPELEG IFSGLIRIIF MRPIELINIG 970 980 990 1000 1010 1020 DYSETEIRQL IKEINVIYQH FNLEYGEQEA TKKALIHFVN EINRRFGVIT RTEWEKFQRI 1030 1040 1050 1060 1070 1080 VQEARTMNDF GMMNQTNYSI LPDEDGYTQS SQLLPSDRFI SPSTQPTPKW RPALYNIDSV 1090 1100 1110 1120 1130 1140 DVQTGMLQPN SQWDLVQKFR KQLSEMFEDP SLQQELGKVS YQELIRQAIN ELKKEHTDKI 1150 1160 1170 1180 1190 1200 QIVSKLIQGS ESLADTDVNK IFLFHETVIT GLNLLSAIYV LLNNFRNNIK GLDLDTIQKS 1210 1220 1230 1240 1250 1260 IIEWLRETQA ANVNRANLID WLGRKHGAIS EIRNPGLVVK ENDVRLSRVY PDPTTNATAP 1270 1280 1290 1300 1310 1320 QDQNLVTETL FAWIVPYVGI PAGGGVRAEQ ELAARYLVDN QRIMQLLLTN IFEMTSSFNK 1330 1340 1350 1360 1370 1380 MVQVRFPETS TAQVHLDFTG LISLIDSLMA DTKYFLNLLR PHIDKNIIQY YENRSNPGSF 1390 1400 1410 1420 1430 1440 YWLEEHLIDK LIKPPTDAGG RPLPGGELGL EGVNQIINKT YILLTKPYNV LQLRGGVQRR 1450 1460 1470 1480 1490 1500 DAANIQINNN PQPSERFEQY GRVFSRLVFY DALENNSGLR VEQVVLGDFR LSNLIRTNNA 1510 1520 1530 1540 1550 1560 QEENTLSYWD NMAPRTYANV NDAANNLRRY RLYGSDYGIQ NNRSMMMVFN QLVASYIARF 1570 1580 1590 1600 1610 1620 YDAPSGKIYL NLINAFANGN FSQAVMELGY THPDLARDNI AFGHRGDPTE QSVLLLSLGL 1630 1640 1650 1660 1670 1680 MLQRLIKDTN RQGLSQHLIS TLTEIPIYLK ENYRANLPLF NKMFNILISQ GELLKQFIQY 1690 1700 1710 1720 1730 1740 TNVQLARPNL MGLLGANNDS VIYYNNNINV PMTGLSVGQA ALRGIGGVFR PNVTLMPLGD 1750 1760 1770 1780 1790 1800 AQNNTSDVVR KRLVAVIDGI IRGSHTLADS AMEVLHELTD HPIYLETEEH FIQNYMSRYN 1810 1820 1830 1840 1850 1860 KEPLMPFSLS LYYLRDLRIE NNEVYDPLLY PNLESGSPEF KLLYGTRKLL GNDPVQLSDM 1870 1880 1890 1900 1910 1920 PGVQLIMKNY NETVVAREQI TPTRFEHFYT HAIQALRFIV NIRSFKTVMM YNENTFGGVN 1930 1940 1950 1960 1970 1980 LISENRDDKP IITAGIGMNA VYSLRKTLQD VISFVESSYQ EEQINHIHKI VSPKGQTRTL 1990 2000 2010 2020 2030 2040 GSNRERERIF NLFDMNIIPI NVNALMRSIP LANIYNYDYS FEEIACLMYG ISAEKVRSLN 2050 2060 2070 2080 2090 2100 TAAPQPDIAE VLNIPNRPPM NTREFMLKLL INPYVSVSIT QYGNELMSKG SAGYMSRIFR 2110 2120 2130 2140 2150 2160 GDNALNMGRP KFLSDQIFNK VLFGSLYPTQ FDYDEAGPGL AAGIQRGREQ WGQPLSEYIN 2170 2180 2190 2200 2210 2220 QALHELVRTI RIPQKLRVLR NIIVKNQLIA DLTTIREQLV SMRREVENMI QTPEIQNNPT 2230 2240 2250 2260 2270 2280 PEVIAAAQNW TQQYRARVDT LINFIGNIGQ PNSMLDLIQT ITPVTVRAQL GVIFNRHGIP 2290 2300 2310 2320 2330 2340 VPHPRQILQT DDEATQWFMT NILNIPAIIM TPFTDLANDL RTFLETLERY VFNVPRWLGP 2350 2360 2370 2380 2390 2400 STGRVARAPV RMAPRDMRHP ISYTENSVLT YITEQNREEG PWSIVKQVGV GIQKPTLVQI 2410 2420 2430 2440 2450 2460 GKDRFDTRLI RNLIFITNIQ RLLRLRLNLE LSQFRNVLVS PDHIINPSIT EYGFSITGPS 2470 ETFSDKQYDS DIRIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Polyprotein processing in African swine fever virus: a novel gene expression strategy for a DNA virus." Simon-Mateo C., Andres G., Vinuela E. EMBO J. 12:2977-2987(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEOLYTIC PROCESSING OF POLYPROTEIN, MYRISTOYLATION AT GLY-2.
[2]	"Analysis of the complete nucleotide sequence of African swine fever virus." Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C., Rodriguez J.F., Vinuela E. Virology 208:249-278(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Mapping and sequence of the gene encoding protein p37, a major structural protein of African swine fever virus." Lopez-Otin C., Simon C., Mendez E., Vinuela E. Virus Genes 1:291-303(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 391-808.
[4]	"Assembly of African swine fever virus: role of polyprotein pp220." Andres G., Simon-Mateo C., Vinuela E. J. Virol. 71:2331-2341(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION OF POLYPROTEIN PP220.
[5]	"Repression of African swine fever virus polyprotein pp220-encoding gene leads to the assembly of icosahedral core-less particles." Andres G., Garcia-Escudero R., Salas M.L., Rodriguez J.M. J. Virol. 76:2654-2666(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF POLYPROTEIN PP220.
[6]	"African swine fever virus polyproteins pp220 and pp62 assemble into the core shell." Andres G., Alejo A., Salas J., Salas M.L. J. Virol. 76:12473-12482(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"Membrane association facilitates the correct processing of pp220 during production of the major matrix proteins of African swine fever virus." Heath C.M., Windsor M., Wileman T. J. Virol. 77:1682-1690(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION OF P150 AND P34.
[8]	"African swine fever virus p37 structural protein is localized in nuclear foci containing the viral DNA at early post-infection times." Eulalio A., Nunes-Correia I., Salas J., Salas M.L., Simoes S., Pedroso de Lima M.C. Virus Res. 130:18-27(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION OF P37.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z22777 Genomic DNA. Translation: CAA80455.1. U18466 Genomic DNA. Translation: AAA65321.1. X87965 Genomic DNA. Translation: CAA61203.1. Frameshift.
PIR	S35307.
RefSeq	NP_042785.1. NC_001659.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1488856.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

PP220_ASFB7

Accession

Primary (citable) accession number: Q08358
Secondary accession number(s): Q65287

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 58 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program