P07297 (CAPSD_PAVBP) 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	Bovine parvovirus (isolate pAT153/1986) (BPV)
Taxonomic identifier	648243 [NCBI]
Taxonomic lineage	Viruses › ssDNA viruses › Parvoviridae › Parvovirinae › Bocavirus
Virus host	Bos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length	673 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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. This attachment induces virion internalization predominantly through clathrin-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
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 Reference 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 – 673	673	Capsid protein VP1		PRO_0000039421
	Chain	138 – 673	536	Capsid protein VP2		PRO_0000039422
Regions
	Region	20 – 65	46	Phospholipase A2-like By similarity
	Compositional bias	163 – 187	25	Gly-rich

Sequences

	Sequence		Length	Mass (Da)
	P07297 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 5F244642B2214831	FASTA	673	75,103
	10 20 30 40 50 60 MPPTNKANSK KGLTLPGYNY LGPFNSLFAG APVNKADAAA RKHDFGYSDL LKEGKNPYLY 70 80 90 100 110 120 FNTHDQNLID ELKDDTSFGG KLARGVFQIK KALAPALPGT SKGGDRALKR KLYFARSNKG 130 140 150 160 170 180 AKKANREPAP STSNQQNMEV SNDIPNDEAG NQPIELATRS VVGSGSVGGG GRGGSGVGYS 190 200 210 220 230 240 TGGWTGGTIF SENIVVTKNT RQFICDIKNG HLYKSEVLNT GDTAHRQYAI TTPWSYFNFN 250 260 270 280 290 300 QYSSHFSPND WQHLVNDYER FRPKAMIVRV YNLQIKQIMT DGAMGTVYNN DLTAGMHIFC 310 320 330 340 350 360 DGDHRYPYVQ HPWDDQCMPE LPNSIWELPQ YAYIPAPISV VDNNTTNTVE EHLLKGVPLY 370 380 390 400 410 420 MLENSDHEVL RNGRIYRIYI QLWRLRMDRK QHHIQHASDD VQSTGQKQKN LLIQRTKQPN 430 440 450 460 470 480 KQRFQNAALR TSNWMSGPGI ARGTHNATLQ TQSAGALVTM VTNGADVSGV RAVRVGYSTD 490 500 510 520 530 540 PIYGGQQPES DLLRLRYSAS AAEGQQNPIL ENAARHTFTR EARTKLITGS NGADGDYKEW 550 560 570 580 590 600 WMLPNQMWDS APISRYNPIW VKVPRVNRKT LLDTQDGSIP MSHPPGTIFI KLARIPVPGN 610 620 630 640 650 660 GDSFLNIYVT GQVSCEVVWE VEKRGTKNWR PEYMHSATNM SVDAYTINNA GVYAGAVQNA 670 DVMQTRFNHH KVL

References

[1]	"Complete nucleotide sequence and genome organization of bovine parvovirus." Chen K.C., Shull B.C., Moses E.A., Lederman M., Stout E.R., Bates R.C. J. Virol. 60:1085-1097(1986) [PubMed: 3783814] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Bovine parvovirus uses clathrin-mediated endocytosis for cell entry." Dudleenamjil E., Lin C.Y., Dredge D., Murray B.K., Robison R.A., Johnson F.B. J. Gen. Virol. 91:3032-3041(2010) [PubMed: 20810750] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M14363 Genomic DNA. Translation: AAB59848.1. M14363 Genomic DNA. Translation: AAB59849.1.
PIR	VCPVB5. A26104.
RefSeq	NP_041404.1. NC_001540.1.
3D structure databases
ProteinModelPortal	P07297.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1489584.
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_PAVBP

Accession

Primary (citable) accession number: P07297
Secondary accession number(s): Q84374

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	September 21, 2011
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program