P08563 (POLS_RUBVM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Structural polyprotein Alternative name(s): p110 Cleaved into the following 3 chains: Capsid protein Alternative name(s): Coat protein Short name=C E2 envelope glycoprotein Alternative name(s): Spike glycoprotein E2 E1 envelope glycoprotein Alternative name(s): Spike glycoprotein E1
Organism	Rubella virus (strain M33) (RUBV) [Complete proteome]
Taxonomic identifier	11043 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Togaviridae › Rubivirus › Rubella virus
Virus host	Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	1063 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 interacts with genomic RNA and assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion, but this interaction seems not to be important for its biological function. Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP/SF2P32. Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells. Induces apoptosis when expressed in transfected cells. Ref.14 Ref.15 E2 envelope glycoprotein is responsible for viral attachment to target host cell, by binding to the cell receptor. Its transport to the plasma membrane depends on interaction with E1 protein. Ref.14 Ref.15 E1 envelope glycoprotein is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and clathrin-mediated endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion By similarity. E1 cytoplasmic tail modulates virus release, and the tyrosines residues are critical for this function. Ref.14 Ref.15
Subunit structure	Capsid protein homooligomerizes. Forms a dimer shortly after synthesis, this dimer become disulfide-linked in the virion. Interacts with human C1QBP. E1 and E2 envelope glycoproteins heterodimerize. Ref.11
Subcellular location	Capsid protein: Virion. Host cytoplasm. Host mitochondrion. Note: The capsid protein is concentrated around Golgi region. Ref.5 Ref.6 Ref.8 E1 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein. Host Golgi apparatus membrane; Single-pass type I membrane protein. Note: E1 and E2 form heterodimer in the endoplasmic reticulum before they are transported to and retained in the Golgi complex, where virus assembly occurs. E1 possesses an endoplasmic reticulum retention signal, and unassembled E2 and E1 subunits are retained in the endoplasmic reticulum. Presumably, assembly of E2 and E1 would mask the signal, thereby allowing transport of the heterodimer to the Golgi complex. Ref.5 Ref.6 Ref.8 E2 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein. Host Golgi apparatus membrane; Single-pass type I membrane protein. Note: E1 and E2 form heterodimer in the endoplasmic reticulum before they are transported to and retained in the Golgi complex, where virus assembly occurs. E1 possesses an endoplasmic reticulum retention signal, and unassembled E2 and E1 subunits are retained in the endoplasmic reticulum. Presumably, assembly of E2 and E1 would mask the signal, thereby allowing transport of the heterodimer to the Golgi complex. Ref.5 Ref.6 Ref.8
Domain	The signal peptide at the C-terminus remains bound to the mature capsid protein. It may have a role as an anchor peptide, localizing the capsid assembly at the Golgi complex, where budding occurs.
Post-translational modification	Specific enzymatic cleavages in vivo yield mature proteins. An internal signal peptide at the capsid C-terminus directs E2-E1 sequences of the polyprotein precursor to the endoplasmic reticulum. Signal peptidase cleaves the precursor between Capsid and E2, releasing the capsid in the cytoplasm and the E2 N-terminus in ER. Another signal peptide at E2 C-terminus directs E1 to the ER, with a similar mechanism. Capsid is phosphorylated on Ser-46 by host. This phosphorylation negatively regulates capsid protein RNA-binding activity. Dephosphorylated by human PP1A By similarity. Ref.17
Miscellaneous	Structural polyprotein is translated from a subgenomic RNA synthesized during togaviruses replication.
Sequence caution	The sequence CAA28880.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Biological process	Clathrin-mediated endocytosis of virus by host Fusion of virus membrane with host endosomal membrane Fusion of virus membrane with host membrane 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 Golgi apparatus Host cytoplasm Host membrane Host mitochondrion Membrane Viral envelope protein Virion
Domain	Signal Transmembrane Transmembrane helix
Ligand	RNA-binding
Molecular function	Capsid protein T=4 icosahedral capsid protein
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome
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	T=4 icosahedral viral capsid Inferred from electronic annotation. Source: UniProtKB-KW host cell Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell host cell mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW viral envelope Inferred from electronic annotation. Source: UniProtKB-KW viral nucleocapsid Inferred from electronic annotation. Source: InterPro virion membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 300

300

Capsid protein

PRO_0000041302

Signal peptide

278 – 300

23

Not cleaved Potential

Chain

301 – 582

282

E2 envelope glycoprotein

PRO_0000041303

Signal peptide

563 – 582

20

Not cleaved Potential

Chain

583 – 1063

481

E1 envelope glycoprotein

PRO_0000041304

Regions

Topological domain

301 – 534

234

Extracellular Potential

Transmembrane

535 – 555

21

Helical; Note=Golgi retention signal; Potential

Topological domain

556 – 582

27

Cytoplasmic Potential

Topological domain

583 – 1028

446

Extracellular Potential

Transmembrane

1029 – 1049

21

Helical; Note=Endoplasmic reticulum retention signal; Potential

Topological domain

1050 – 1063

14

Cytoplasmic Potential

Region

30 – 69

40

Human C1QBP/SF2P32-binding

Sites

Site

300 – 301

2

Cleavage; by host signal peptidase Potential

Site

582 – 583

2

Cleavage; by host signal peptidase Potential

Amino acid modifications

Modified residue

46

1

Phosphoserine; by host Ref.17

Glycosylation

658

1

N-linked (GlcNAc...); by host Ref.16

Glycosylation

759

1

N-linked (GlcNAc...); by host Ref.16

Glycosylation

791

1

N-linked (GlcNAc...); by host Ref.16

Disulfide bond

590 ↔ 595

By similarity

Disulfide bond

619 ↔ 824

By similarity

Disulfide bond

641 ↔ 653

By similarity

Disulfide bond

699 ↔ 712

By similarity

Disulfide bond

758 ↔ 767

By similarity

Disulfide bond

807 ↔ 817

By similarity

Disulfide bond

931 ↔ 934

By similarity

Disulfide bond

950 ↔ 983

By similarity

Natural variations

Natural variant

272

1

H → R in strain: Isolate HPV77 vaccine.

Natural variant

411

1

S → Y in strain: Isolate HPV77 vaccine.

Natural variant

412

1

T → I in strain: Isolate HPV77 vaccine.

Natural variant

413

1

T → A in strain: Isolate HPV77 vaccine.

Natural variant

609

1

R → G in strain: Isolate HPV77 vaccine.

Experimental info

Mutagenesis

35 – 43

9

RRPRPPRQR → AAPAPPAQA: Complete loss of human C1QBP/SF2P32-binding. 90% loss of virus production from infected cell. Ref.18

Mutagenesis

60 – 68

9

RRRRGNRGR → AAAAGNAGA: Complete loss of human C1QBP/SF2P32-binding. 90% loss of virus production from infected cell. Ref.18

Mutagenesis

153

1

C → S: Complete loss of Capsid dimerization. No effect on particle budding. Ref.7

Mutagenesis

658

1

N → I: Complete loss of infectivity. Ref.16

Mutagenesis

664

1

C → S: Prevents E1-E2 heterodimer formation, and subsequent transport of to the plasma membrane. Complete loss of fusion activity in vitro. Ref.9

Mutagenesis

675

1

G → D: Complete loss of fusion activity in vitro. 90% loss of infectivity in vivo. No effect on virus assembly. Ref.9 Ref.13

Mutagenesis

686

1

P → G: 99.9% loss of infectivity. No effect on virus assembly. No effect on fusion activity in vitro. Ref.9 Ref.13

Mutagenesis

759

1

N → I: No effect on infectivity. Ref.16

Mutagenesis

791

1

N → I: Complete loss of infectivity. Ref.16

Mutagenesis

1046

1

L → A: No effect on virus production from infected cell. Ref.10

Mutagenesis

1048

1

C → A: No effect on virus production from infected cell. Ref.10

Mutagenesis

1049

1

C → A: No effect on virus production from infected cell. Ref.10

Mutagenesis

1052

1

C → A: No effect on virus production from infected cell. Ref.10 Ref.12

Mutagenesis

1053

1

L → A: 90% loss of virus production from infected cell. Ref.10 Ref.12

Mutagenesis

1054

1

Y → A: Complete loss of virus production from infected cell. Ref.12

Mutagenesis

1055

1

Y → S: Complete loss of virus production from infected cell. Ref.12

Mutagenesis

1056

1

L → A: 90% loss of virus production from infected cell. Ref.12

Mutagenesis

1057

1

R → S: 98% loss of virus production from infected cell. Ref.12

Mutagenesis

1058

1

G → C: 98% loss of virus production from infected cell. Ref.12

Mutagenesis

1059

1

A → S: 90% loss of virus production from infected cell. Ref.12

Mutagenesis

1060

1

I → V: No effect on virus production from infected cell. Ref.12

Mutagenesis

1061

1

A → S: 90% loss of virus production from infected cell. Ref.12

Mutagenesis

1062

1

P → S: 90% loss of virus production from infected cell. Ref.12

Mutagenesis

1063

1

R → S: 98% loss of virus production from infected cell. Ref.12

Sequence conflict

42 – 69

28

QRDSS…NRGRG → HARLQHLPEMTPAVTPEGPA PPRTGAW in CAA28880. Ref.1

Sequence conflict

175

1

T → I in CAA28880. Ref.1

Sequence conflict

445 – 471

27

RHGAD…PTRFG → PTALTPGAVGDLRAVHHRPV PAYPVC in CAA28880. Ref.1

Sequence conflict

485

1

V → I in CAA28880. Ref.1

Sequence conflict

562 – 577

16

RGAAA…LQGYN → PAPPPPSPQSSCRGTT in CAA28880. Ref.1

Sequence conflict

993 – 994

2

RV → GH in CAA28880. Ref.1

Sequence conflict

995 – 1063

69

Missing in CAA28880. Ref.1

Secondary structure

1

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1063

Helix Strand Turn

Details...

Beta strand

585 – 589

5

Beta strand

599 – 601

3

Beta strand

603 – 621

19

Beta strand

625 – 634

10

Turn

641 – 647

7

Helix

650 – 657

8

Beta strand

659 – 670

12

Beta strand

672 – 674

3

Beta strand

676 – 678

3

Helix

681 – 683

3

Helix

689 – 694

6

Beta strand

698 – 703

6

Beta strand

716 – 718

3

Beta strand

721 – 729

9

Helix

733 – 735

3

Beta strand

737 – 753

17

Beta strand

756 – 760

5

Beta strand

766 – 768

3

Beta strand

770 – 777

8

Beta strand

785 – 790

6

Beta strand

797 – 804

8

Turn

807 – 813

7

Helix

815 – 817

3

Beta strand

818 – 821

4

Beta strand

824 – 826

3

Beta strand

836 – 839

4

Helix

845 – 848

4

Beta strand

855 – 862

8

Beta strand

869 – 875

7

Helix

878 – 880

3

Beta strand

881 – 883

3

Helix

885 – 892

8

Beta strand

894 – 896

3

Beta strand

904 – 910

7

Beta strand

924 – 936

13

Beta strand

938 – 944

7

Beta strand

946 – 948

3

Beta strand

950 – 954

5

Beta strand

957 – 962

6

Beta strand

964 – 971

8

Beta strand

980 – 989

10

Beta strand

991 – 995

5

Helix

997 – 1001

5

Turn

1002 – 1004

3

Beta strand

1005 – 1008

4

Beta strand

1010 – 1014

5

Sequences

	Sequence		Length	Mass (Da)
	P08563 [UniParc]. Last modified May 30, 2006. Version 2. Checksum: B546067276483ECB	FASTA	1,063	114,736
	10 20 30 40 50 60 MASTTPITME DLQKALEAQS RALRAGLAAG ASQSRRPRPP RQRDSSTSGD DSGRDSGGPR 70 80 90 100 110 120 RRRGNRGRGQ RKDWSRAPPP PEERQESRSQ TPAPKPSRAP PQQPQPPRMQ TGRGGSAPRP 130 140 150 160 170 180 ELGPPTNPFQ AAVARGLRPP LHDPDTEAPT EACVTSWLWS EGEGAVFYRV DLHFTNLGTP 190 200 210 220 230 240 PLDEDGRWDP ALMYNPCGPE PPAHVVRAYN QPAGDVRGVW GKGERTYAEQ DFRVGGTRWH 250 260 270 280 290 300 RLLRMPVRGL DGDTAPLPPH TTERIETRSA RHPWRIRFGA PQAFLAGLLL AAVAVGTARA 310 320 330 340 350 360 GLQPRADMAA PPMPPQPPRA HGQHYGHHHH QLPFLGHDGH HGGTLRVGQH HRNASDVLPG 370 380 390 400 410 420 HWLQGGWGCY NLSDWHQGTH VCHTKHMDFW CVEHDRPPPA TPTSLTTAAN STTAATPATA 430 440 450 460 470 480 PPPCHAGLND SCGGFLSGCG PMRLRHGADT RCGRLICGLS TTAQYPPTRF GCAMRWGLPP 490 500 510 520 530 540 WELVVLTARP EDGWTCRGVP AHPGTRCPEL VSPMGRATCS PASALWLATA NALSLDHAFA 550 560 570 580 590 600 AFVLLVPWVL IFMVCRRACR RRGAAAALTA VVLQGYNPPA YGEEAFTYLC TAPGCATQTP 610 620 630 640 650 660 VPVRLAGVRF ESKIVDGGCF APWDLEATGA CICEIPTDVS CEGLGAWVPT APCARIWNGT 670 680 690 700 710 720 QRACTFWAVN AYSSGGYAQL ASYFNPGGSY YKQYHPTACE VEPAFGHSDA ACWGFPTDTV 730 740 750 760 770 780 MSVFALASYV QHPHKTVRVK FHTETRTVWQ LSVAGVSCNV TTEHPFCNTP HGQLEVQVPP 790 800 810 820 830 840 DPGDLVEYIM NYTGNQQSRW GLGSPNCHGP DWASPVCQRH SPDCSRLVGA TPERPRLRLV 850 860 870 880 890 900 DADDPLLRTA PGPGEVWVTP VIGSQARKCG LHIRAGPYGH ATVEMPEWIH AHTTSDPWHP 910 920 930 940 950 960 PGPLGLKFKT VRPVALPRAL APPRNVRVTG CYQCGTPALV EGLAPGGGNC HLTVNGEDVG 970 980 990 1000 1010 1020 AFPPGKFVTA ALLNTPPPYQ VSCGGESDRA SARVIDPAAQ SFTGVVYGTH TTAVSETRQT 1030 1040 1050 1060 WAEWAAAHWW QLTLGAICAL LLAGLLACCA KCLYYLRGAI APR

References

[1]	"Nucleotide sequence and in vitro expression of rubella virus 24S subgenomic messenger RNA encoding the structural proteins E1, E2 and C." Clarke D.M., Loo T.W., Hui I., Chong P., Gillam S. Nucleic Acids Res. 15:3041-3057(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Expression of rubella virus cDNA coding for the structural proteins." Clarke D.M., Loo T.W., McDonald H., Gillam S. Gene 65:23-30(1988) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[3]	"Nucleotide sequence of the 24S subgenomic messenger RNA of a vaccine strain (HPV77) of rubella virus: comparison with a wild-type strain (M33)." Zheng D., Dickens L., Liu T.Y., Nakhasi H.L. Gene 82:343-349(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate HPV77 vaccine.
[4]	"Analysis of rubella virus E1 glycosylation mutants expressed in COS cells." Hobman T.C., Qiu Z., Chaye H., Gillam S. Virology 181:768-772(1991) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION OF E1 ENVELOPE GLYCOPROTEIN.
[5]	"The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex." Hobman T.C., Woodward L., Farquhar M.G. J. Cell Biol. 121:269-281(1993) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION OF E1 AND E2 ENVELOPE GLYCOPROTEINS.
[6]	"Targeting of a heterodimeric membrane protein complex to the Golgi: rubella virus E2 glycoprotein contains a transmembrane Golgi retention signal." Hobman T.C., Woodward L., Farquhar M.G. Mol. Biol. Cell 6:7-20(1995) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"Dimerization of rubella virus capsid protein is not required for virus particle formation." Lee J.Y., Hwang D., Gillam S. Virology 216:223-227(1996) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-153.
[8]	"Characterization of an endoplasmic reticulum retention signal in the rubella virus E1 glycoprotein." Hobman T.C., Lemon H.F., Jewell K. J. Virol. 71:7670-7680(1997) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"Effects of mutations in the rubella virus E1 glycoprotein on E1-E2 interaction and membrane fusion activity." Yang D., Hwang D., Qiu Z., Gillam S. J. Virol. 72:8747-8755(1998) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-664; GLY-675 AND PRO-686.
[10]	"Mutational analysis, using a full-length rubella virus cDNA clone, of rubella virus E1 transmembrane and cytoplasmic domains required for virus release." Yao J., Gillam S. J. Virol. 73:4622-4630(1999) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF LEU-1046; CYS-1048; CYS-1049; CYS-1052 AND LEU-1053.
[11]	"Rubella virus capsid associates with host cell protein p32 and localizes to mitochondria." Beatch M.D., Hobman T.C. J. Virol. 74:5569-5576(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN C1QBP.
[12]	"A single-amino-acid substitution of a tyrosine residue in the rubella virus E1 cytoplasmic domain blocks virus release." Yao J., Gillam S. J. Virol. 74:3029-3036(2000) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-1052; LEU-1053; TYR-1054; TYR-1055; LEU-1056; ARG-1057; GLY-1058; ALA-1059; ILE-1060; ALA-1061; PRO-1062 AND ARG-1063.
[13]	"Mutations in the E1 hydrophobic domain of rubella virus impair virus infectivity but not virus assembly." Qiu Z., Yao J., Cao H., Gillam S. J. Virol. 74:6637-6642(2000) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF GLY-675 AND PRO-686.
[14]	"Rubella virus capsid protein induces apoptosis in transfected RK13 cells." Duncan R., Esmaili A., Law L.M., Bertholet S., Hough C., Hobman T.C., Nakhasi H.L. Virology 275:20-29(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF CAPSID PROTEIN.
[15]	"Rubella virus E2 signal peptide is required for perinuclear localization of capsid protein and virus assembly." Law L.M., Duncan R., Esmaili A., Nakhasi H.L., Hobman T.C. J. Virol. 75:1978-1983(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF CAPSID PROTEIN.
[16]	"Effect of site-directed asparagine to isoleucine substitutions at the N-linked E1 glycosylation sites on rubella virus viability." Ramanujam M., Hofmann J., Nakhasi H.L., Atreya C.D. Virus Res. 81:151-156(2001) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-658; ASN-759 AND ASN-791, MUTAGENESIS OF ASN-658; ASN-759 AND ASN-791.
[17]	"Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication." Law L.M., Everitt J.C., Beatch M.D., Holmes C.F., Hobman T.C. J. Virol. 77:1764-1771(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-46, RNA-BINDING.
[18]	"Interactions between rubella virus capsid and host protein p32 are important for virus replication." Beatch M.D., Everitt J.C., Law L.J., Hobman T.C. J. Virol. 79:10807-10820(2005) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF 35-ARG--ARG-43 AND 60-ARG--ARG-68.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X05259 mRNA. Translation: CAA28880.1. Sequence problems.
M30776 Genomic RNA. Translation: AAA47421.1. Sequence problems.

PIR

GNWVR3. A27505.
GNWV77. JQ0087.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4ADG	X-ray	2.18	A/B/C	583-1018	[»]
4ADI	X-ray	1.80	A/B/C	583-1018	[»]
4ADJ	X-ray	1.94	A/B/C	583-1018	[»]
4B3V	X-ray	1.98	A/B/C	583-1018	[»]

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR008819. Rubella_Capsid.
IPR008820. Rubella_E1.
IPR008821. Rubella_E2.
[Graphical view]

Pfam

PF05750. Rubella_Capsid. 1 hit.
PF05748. Rubella_E1. 1 hit.
PF05749. Rubella_E2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

POLS_RUBVM

Accession

Primary (citable) accession number: P08563
Secondary accession number(s): P21480 , Q86373, Q86374, Q86375

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	May 30, 2006
Last modified:	April 3, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program