P68617 (A33_VACCW) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein A33

Gene names

Ordered Locus Names:	VACWR156
ORF Names:	A33R

Organism

Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))

Taxonomic identifier

10254 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Poxviridae › Chordopoxvirinae › Orthopoxvirus › Vaccinia virus

Virus host

Bos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length	185 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Coordinates the incorporation of A36 into wrapped enveloped virion (EV) membranes and, subsequently, the production of actin tails. Therefore plays an essential role in efficient cell-to-cell spread of viral particles. Ref.5 Ref.7 Ref.8
Subunit structure	Homodimer, disulfide-linked. Interacts with protein B5. Interacts (via C-terminus) with protein A36. Ref.6 Ref.9 Ref.11
Subcellular location	Host membrane; Single-pass type II membrane protein Potential. Note: Present in the enveloped virion (EV) membrane. Ref.4
Sequence similarities	Belongs to the chordopoxvirinae A33 protein family.

Ontologies

Keywords
Cellular component	Host membrane Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	host cell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	binding 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 – 185

185

Protein A33

PRO_0000099317

Regions

Topological domain

1 – 33

33

Cytoplasmic Potential

Transmembrane

34 – 56

23

Helical; Potential

Topological domain

57 – 185

129

Extracellular Potential

Region

98 – 185

88

C-type lectin-like domain

Amino acid modifications

Glycosylation

125

1

N-linked (GlcNAc...); by host Potential

Glycosylation

135

1

N-linked (GlcNAc...); by host Potential

Disulfide bond

62

Interchain

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

185

Helix Strand Turn

Details...

Beta strand

109 – 117

9

Helix

119 – 128

10

Helix

136 – 139

4

Helix

145 – 148

4

Beta strand

176 – 182

7

Sequences

	Sequence		Length	Mass (Da)
	P68617 [UniParc]. Last modified December 7, 2004. Version 1. Checksum: 201CF65C2D2076A4	FASTA	185	20,506
	10 20 30 40 50 60 MMTPENDEEQ TSVFSATVYG DKIQGKNKRK RVIGLCIRIS MVISLLSMIT MSAFLIVRLN 70 80 90 100 110 120 QCMSANEAAI TDAAVAVAAA SSTHRKVASS TTQYDHKESC NGLYYQGSCY ILHSDYQLFS 130 140 150 160 170 180 DAKANCTAES STLPNKSDVL ITWLIDYVED TWGSDGNPIT KTTSDYQDSD VSQEVRKYFC VKTMN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the right inverted terminal repeat." Smith G.L., Chan Y.S., Howard S.T. J. Gen. Virol. 72:1349-1376(1991) [PubMed: 2045793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Identification, sequence, and expression of the gene encoding a Mr 35,000 subunit of the vaccinia virus DNA-dependent RNA polymerase." Amegadzie B.Y., Ahn B.-Y., Moss B. J. Biol. Chem. 266:13712-13718(1991) [PubMed: 1856205] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequencing of the coding region of Vaccinia-WR to an average 9-fold redundancy and an error rate of 0.16/10kb." Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J., Wohlhueter R. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Extracellular vaccinia virus envelope glycoprotein encoded by the A33R gene." Roper R.L., Payne L.G., Moss B. J. Virol. 70:3753-3762(1996) [PubMed: 8648710] [Abstract] Cited for: SUBCELLULAR LOCATION.
[5]	"The envelope protein encoded by the A33R gene is required for formation of actin-containing microvilli and efficient cell-to-cell spread of vaccinia virus." Roper R.L., Wolffe E.J., Weisberg A., Moss B. J. Virol. 72:4192-4204(1998) [PubMed: 9557708] [Abstract] Cited for: FUNCTION.
[6]	"Interactions between vaccinia virus IEV membrane proteins and their roles in IEV assembly and actin tail formation." Rottger S., Frischknecht F., Reckmann I., Smith G.L., Way M. J. Virol. 73:2863-2875(1999) [PubMed: 10074134] [Abstract] Cited for: INTERACTION WITH PROTEIN A36.
[7]	"The vaccinia virus A33R protein provides a chaperone function for viral membrane localization and tyrosine phosphorylation of the A36R protein." Wolffe E.J., Weisberg A.S., Moss B. J. Virol. 75:303-310(2001) [PubMed: 11119600] [Abstract] Cited for: FUNCTION.
[8]	"Mutations in the vaccinia virus A33R and B5R envelope proteins that enhance release of extracellular virions and eliminate formation of actin-containing microvilli without preventing tyrosine phosphorylation of the A36R protein." Katz E., Ward B.M., Weisberg A.S., Moss B. J. Virol. 77:12266-12275(2003) [PubMed: 14581563] [Abstract] Cited for: FUNCTION.
[9]	"Interaction between vaccinia virus extracellular virus envelope A33 and B5 glycoproteins." Perdiguero B., Blasco R. J. Virol. 80:8763-8777(2006) [PubMed: 16912323] [Abstract] Cited for: INTERACTION WITH B5.
[10]	"Pox proteomics: mass spectrometry analysis and identification of Vaccinia virion proteins." Yoder J.D., Chen T.S., Gagnier C.R., Vemulapalli S., Maier C.S., Hruby D.E. Virol. J. 3:10-10(2006) [PubMed: 16509968] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[11]	"The inability of vaccinia virus A33R protein to form intermolecular disulfide-bonded homodimers does not affect the production of infectious extracellular virus." Chan W.M., Kalkanoglu A.E., Ward B.M. Virology 408:109-118(2010) [PubMed: 20947114] [Abstract] Cited for: SUBUNIT.
[12]	"Protein A33 responsible for antibody-resistant spread of Vaccinia virus is homologous to C-type lectin-like proteins." Krupovic M., Cvirkaite-Krupovic V., Bamford D.H. Virus Res. 151:97-101(2010) [PubMed: 20302896] [Abstract] Cited for: DOMAIN.
[13]	"The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains." Su H.P., Singh K., Gittis A.G., Garboczi D.N. J. Virol. 84:2502-2510(2010) [PubMed: 20032175] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 90-185.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D11079 Genomic DNA. Translation: BAA01805.1.
M61187 Genomic DNA. Translation: AAA48330.1.
X57318 Genomic DNA. Translation: CAA40583.1.
AY243312 Genomic DNA. Translation: AAO89435.1.

PIR

H42520.

RefSeq

YP_233038.1. NC_006998.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3K7B	X-ray	2.10	A/B	90-185	[»]

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-6740399.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3707686.

Phylogenomic databases

ProtClustDB

PHA3093.

Family and domain databases

InterPro

IPR016186. C-type_lectin-like.
IPR009238. Chordopox_A33R.
[Graphical view]

Gene3D

G3DSA:3.10.100.10. C-type_lectin-like. 1 hit.

Pfam

PF05966. Chordopox_A33R. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

A33_VACCW

Accession

Primary (citable) accession number: P68617
Secondary accession number(s): P21056, Q76ZP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	December 7, 2004
Last modified:	October 19, 2011
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program