P07299 (CAPSD_PAVHU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Capsid protein VP1 Alternative name(s): Coat protein VP1 Cleaved into the following chain: Capsid protein VP2 Alternative name(s): Coat protein VP2
Organism	Human parvovirus B19 (isolate AU) (HPV B19) [Complete proteome]
Taxonomic identifier	648238 [NCBI]
Taxonomic lineage	Viruses › ssDNA viruses › Parvoviridae › Parvovirinae › Erythrovirus
Virus host	Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	781 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	Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptors, such as the glycosphingolipid globoside or the integrin heterodimer ITGAV/ITGB1. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell. Intracytoplasmic transport involves microtubules and interaction between capsid proteins and host dynein. Exposure of nuclear localization signal probably allows nuclear import of capsids By similarity. Ref.2 Ref.3
Subunit structure	Interacts with host integrins ITGAV/ITGB1; this interaction participates in the attachment and entry into host cell. Ref.2
Subcellular location	Virion By similarity. Host nucleus Potential.
Domain	The N-terminus of VP1 is sequestered within the mature capsid. It contains a phospholipase A2-like region and nuclear localization signals that might be exposed by capsid modifications during virus entry By similarity.
Miscellaneous	The capsids of autonomous parvoviruses expose a proportion of VP2 N-terminus and part of that sequence can be cleaved of to form VP3 By similarity.
Sequence similarities	Belongs to the parvoviridae capsid protein family.

Ontologies

Keywords
Biological process	Clathrin-mediated endocytosis of virus by host Cytoplasmic active transport of viral material Host-virus interaction Initiation of viral infection Microtubule-dependent active transport of viral material Viral attachment to host cell Viral penetration into host cytoplasm Viral penetration into host nucleus Viral penetration via permeabilization of host organellar membrane Virus endocytosis by host
Cellular component	Host nucleus Virion
Ligand	Magnesium Metal-binding
Molecular function	Capsid protein T=1 icosahedral capsid protein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell viral capsid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 781	781	Capsid protein VP1		PRO_0000222459
	Chain	228 – 781	554	Capsid protein VP2		PRO_0000406519
Regions
	Region	130 – 175	46	Phospholipase A2-like
	Region	577 – 677	101	Binding to globoside Potential
	Compositional bias	95 – 99	5	Poly-Ser
	Compositional bias	239 – 244	6	Poly-Gly

Sequences

	Sequence		Length	Mass (Da)
	P07299 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 8C6254DBD0576B07	FASTA	781	86,015
	10 20 30 40 50 60 MSKKSGKWWE SDDKFAKAVY QQFVEFYEKV TGTDLELIQI LKDHYNISLD NPLENPSSLF 70 80 90 100 110 120 DLVARIKNNL KNSPDLYSHH FQSHGQLSDH PHALSSSSSH AEPRGENAVL SSEDLHKPGQ 130 140 150 160 170 180 VSVQLPGTNY VGPGNELQAG PPQSAVDSAA RIHDFRYSQL AKLGINPYTH WTVADEELLK 190 200 210 220 230 240 NIKNETGFQA QVVKDYFTLK GAAAPVAHFQ GSLPEVPAYN ASEKYPSMTS VNSAEASTGA 250 260 270 280 290 300 GGGGSNSVKS MWSEGATFSA NSVTCTFSRQ FLIPYDPEHH YKVFSPAASS CHNASGKEAK 310 320 330 340 350 360 VCTISPIMGY STPWRYLDFN ALNLFFSPLE FQHLIENYGS IAPDALTVTI SEIAVKDVTD 370 380 390 400 410 420 KTGGGVQVTD STTGRLCMLV DHEYKYPYVL GQGQDTLAPE LPIWVYFPPQ YAYLTVGDVN 430 440 450 460 470 480 TQGISGDSKK LASEESAFYV LEHSSFQLLG TGGTASMSYK FPPVPPENLE GCSQHFYEMY 490 500 510 520 530 540 NPLYGSRLGV PDTLGGDPKF RSLTHEDHAI QPQNFMPGPL VNSVSTKEGD SSNTGAGKAL 550 560 570 580 590 600 TGLSTGTSQN TRISLRPGPV SQPYHHWDTD KYVTGINAIS HGQTTYGNAE DKEYQQGVGR 610 620 630 640 650 660 FPNEKEQLKQ LQGLNMHTYF PNKGTQQYTD QIERPLMVGS VWNRRALHYE SQLWSKIPNL 670 680 690 700 710 720 DDSFKTQFAA LGGWGLHQPP PQIFLKILPQ SGPIGGIKSM GITTLVQYAV GIMTVTMTFK 730 740 750 760 770 780 LGPRKATGRW NPQPGVYPPH AAGHLPYVLY DPTATDAKQH HRHGYEKPEE LWTAKSRVHP L

References

[1]	"Nucleotide sequence and genome organization of human parvovirus B19 isolated from the serum of a child during aplastic crisis." Shade R.O., Blundell M.C., Cotmore S.F., Tattersall P., Astell C.R. J. Virol. 58:921-936(1986) [PubMed: 3701931] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Alpha5beta1 integrin as a cellular coreceptor for human parvovirus B19: requirement of functional activation of beta1 integrin for viral entry." Weigel-Kelley K.A., Yoder M.C., Srivastava A. Blood 102:3927-3933(2003) [PubMed: 12907437] [Abstract] Cited for: FUNCTION, INTERACTION WITH INTEGRIN HETERODIMER ITGAV/ITGB1.
[3]	"The globoside receptor triggers structural changes in the B19 virus capsid that facilitate virus internalization." Boensch C., Zuercher C., Lieby P., Kempf C., Ros C. J. Virol. 84:11737-11746(2010) [PubMed: 20826697] [Abstract] Cited for: FUNCTION, BINDING TO HOST GLOBOSIDE.
[4]	"Advances in human B19 erythrovirus biology." Servant-Delmas A., Lefrere J.J., Morinet F., Pillet S. J. Virol. 84:9658-9665(2010) [PubMed: 20631151] [Abstract] Cited for: REVIEW.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

Sequence databases
EMBL GenBank DDBJ	M13178 Genomic DNA. Translation: AAA66867.1.
PIR	VCPV19. A24299.
3D structure databases
ProteinModelPortal	P07299.
SMR	P07299. Positions 246-781.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR016184. Capsid/spike_ssDNA_virus. IPR001403. Parvovirus_coat. IPR013607. Parvovirus_coat_VP1_N. [Graphical view]
Gene3D	G3DSA:2.170.30.10. Parvo_coat. 1 hit.
Pfam	PF00740. Parvo_coat. 1 hit. PF08398. Parvo_coat_N. 1 hit. [Graphical view]
SUPFAM	SSF88645. Capsid/spike_ssDNA_virus. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CAPSD_PAVHU

Accession

Primary (citable) accession number: P07299

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program