P23008 (POLG_HRV1A) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Genome polyprotein Cleaved into the following 5 chains: Protein VP0 Alternative name(s): VP4-VP2 Protein VP4 Alternative name(s): P1A Virion protein 4 Protein VP2 Alternative name(s): P1B Virion protein 2 Protein VP3 Alternative name(s): P1C Virion protein 3 Protein VP1 Alternative name(s): Virion protein 1
Organism	Human rhinovirus 1A (HRV-1A)
Taxonomic identifier	12134 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Enterovirus › Rhinovirus A › Human rhinovirus A1
Virus host	Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	833 AA.
Sequence status	Fragments.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The capsid interacts with human VLDLR to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis By similarity. VP0 precursor is a component of immature procapsids By similarity.
Subunit structure	Capsid proteins interact with host VLDLR By similarity.
Subcellular location	Protein VP2: Virion. Host cytoplasm Potential. Protein VP3: Virion. Host cytoplasm Potential. Protein VP1: Virion. Host cytoplasm Potential.
Post-translational modification	Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle By similarity. Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle By similarity.
Sequence similarities	Belongs to the picornaviruses polyprotein family.

Ontologies

Keywords
Biological process	Clathrin-mediated endocytosis of virus by host Host-virus interaction Viral attachment to host cell Viral penetration into host cytoplasm Virus endocytosis by host Virus entry into host cell
Cellular component	Host cytoplasm Virion
Molecular function	Capsid protein
PTM	Lipoprotein Myristate
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	viral attachment to host cell Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell via clathrin-mediated endocytosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell viral capsid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	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

Initiator methionine

1

1

Removed; by host

Chain

2 – 308

307

Protein VP0 Potential

PRO_0000311070

Chain

2 – 45

44

Protein VP4 Potential

PRO_0000039995

Chain

46 – 308

263

Protein VP2 Potential

PRO_0000039996

Chain

309 – 546

238

Protein VP3 Potential

PRO_0000039997

Chain

547 – 833

287

Protein VP1 Potential

PRO_0000039998

Sites

Site

45 – 46

2

Cleavage Potential

Site

308 – 309

2

Cleavage; by picornain 3C Potential

Amino acid modifications

Lipidation

2

1

N-myristoyl glycine; by host By similarity

Experimental info

Non-adjacent residues

45 – 46

2

Non-terminal residue

833

1

Secondary structure

1

.

.

.

.

.

.

.

.

833

Helix Strand Turn

Details...

Beta strand

3 – 6

4

Beta strand

27 – 30

4

Beta strand

33 – 35

3

Helix

36 – 38

3

Sequences

	Sequence		Length	Mass (Da)
	P23008 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E1F013536C1A5EC8	FASTA	833	92,473
	10 20 30 40 50 60 MGAGVSRQNV GTHSTQNSVS NGSSLNYFNI NYFKDAASSG ASRLDSPSVE ACGYSDRIMQ 70 80 90 100 110 120 ITRGDSTISS DDVANAVVGY GVWPHYLTPQ DATAINKPTQ PDTSSNRFYT LESKHWNGSS 130 140 150 160 170 180 KGWWWKLPDA LKDMGIFGEN MYYHFLGRSG YTVHVQCNAS KFHQGTLLVA MIPEHQLASA 190 200 210 220 230 240 KHGSVTAGYK LTHPGEAGRD VSQERDASLR QPSDDSWLNF DGTLLGNLLI FPHQFINLRS 250 260 270 280 290 300 NNSATLIVPY VNAVPMDSML RHNNWCLVII PISPLRSETT SSNIVPITVS ISPMCAEFSG 310 320 330 340 350 360 ARAKNIKQGL PVYITPGSGQ FMTTDDMQSP CALPWYHPTK EISIPGEVKN LIEMCQVDTL 370 380 390 400 410 420 IPVNNVGNNV GNVSMYTVQL GNQTGMAQKV FSIKVDITST PLATTLIGEI ASYYTHWTGS 430 440 450 460 470 480 LRFSFMFCGT ANTTLKLLLA YTPPGIDEPT TRKDAMLGTH VVWDVGLQST ISLVVPWVSA 490 500 510 520 530 540 SHFRLTADNK YSMAGYITCW YQTNLVVPPS TPQTADMLCF VSACKDFCLR MARDTDLHIQ 550 560 570 580 590 600 SGPIEQNPVE NYIDEVLNEV LVVPNIKESH HTTSNSAPLL DAAETGHTSN VQPEDAIETR 610 620 630 640 650 660 YVITSQTRDE MSIESFLGRS GCVHISRIKV DYTDYNGQDI NFTKWKITLQ EMAQIRRKFE 670 680 690 700 710 720 LFTYVRFDSE ITLVPCIAGR GDDIGHIVMQ YMYVPPGAPI PSKRNDFSWQ SGTNMSIFWQ 730 740 750 760 770 780 HGQPFPRFSI PFLSIASAYY MFYDGYDGDN TSSKYGSVVT NDMGTICSRI VTEKQKLSVV 790 800 810 820 830 ITTHIYHKAK HTKAWCPRPP RAVPYTHSHV TNYMPETGDV TTAIVRRNTI TTA

References

[1]	"Crystal structure of human rhinovirus serotype 1A (HRV1A)." Kim S., Smith T.J., Chapman M.S., Rossmann M.G., Pevear D., Dutko F.J., Felock P.J., Diana G.D., McKinlay M.A. J. Mol. Biol. 210:91-111(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE, X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound Win56291

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound Win54954

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound R61837

Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AYM	X-ray	2.15	4	2-44	[»]
1AYN	X-ray	2.90	4	2-45	[»]
1R1A	X-ray	3.20	1	547-833	[»]
			2	46-308	[»]
			3	309-546	[»]
			4	2-45	[»]
2HWD	X-ray	3.80	1	547-833	[»]
			2	46-308	[»]
			3	309-546	[»]
			4	2-45	[»]
2HWE	X-ray	3.80	1	547-833	[»]
			2	46-308	[»]
			3	309-546	[»]
			4	2-45	[»]
2HWF	X-ray	3.80	1	547-833	[»]
			2	46-308	[»]
			3	309-546	[»]
			4	2-45	[»]

ProteinModelPortal

P23008.

SMR

P23008. Positions 2-45, 56-546, 551-833.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

4.10.80.10. 1 hit.

InterPro

IPR003138. Pico_P1A.
IPR001676. Picornavirus_capsid.
[Graphical view]

Pfam

PF02226. Pico_P1A. 1 hit.
PF00073. Rhv. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P23008.

Entry information

Entry name

POLG_HRV1A

Accession

Primary (citable) accession number: P23008

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program