Reviewed, UniProtKB/Swiss-Prot P07612 (VM25_VACCW)

Names and origin

Protein names

Recommended name:
    Virion membrane protein M25

Gene names

ORF Names:

F2

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

Virus host

Bos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length	250 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	Plays a role in virion assembly. Ref.3
Subcellular location	Virion membrane; Single-pass membrane protein. Virion membrane; Lipid-anchor. Note: Associated exclusively with the primary membranes surrounding the virion core. Constituent of both intracellular mature virus particles and extracellular enveloped virions which are released from the infected cell. Ref.4
Sequence similarities	Belongs to the poxviruses L1 family.

Ontologies

Keywords
Cellular component	Membrane Virion
Domain	Transmembrane
PTM	Disulfide bond Lipoprotein Myristate
Technical term	3D-structure
Gene Ontology (GO)
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell virion 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

Initiator methionine

1

1

Removed; by host

Chain

2 – 250

249

Virion membrane protein M25

PRO_0000099613

Regions

Transmembrane

184 – 204

21

Potential

Amino acid modifications

Lipidation

2

1

N-myristoyl glycine; by host

Disulfide bond

34 ↔ 57

Disulfide bond

49 ↔ 136

Disulfide bond

116 ↔ 158

Experimental info

Mutagenesis

2

1

G → A: Complete loss of myristoylation. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

250

Helix Strand Turn

Details...

Helix

5 – 25

21

Beta strand

35 – 55

21

Helix

61 – 77

17

Helix

81 – 84

4

Helix

87 – 95

9

Turn

101 – 103

3

Helix

104 – 115

12

Beta strand

116 – 118

3

Helix

119 – 122

4

Beta strand

127 – 137

11

Beta strand

144 – 150

7

Helix

154 – 174

21

Sequences

	Sequence		Length	Mass (Da)
	P07612-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 28FE89850863372D	FASTA	250	27,279
	10 20 30 40 50 60 MGAAASIQTT VNTLSERISS KLEQEANASA QTKCDIEIGN FYIRQNHGCN LTVKNMCSAD 70 80 90 100 110 120 ADAQLDAVLS AATETYSGLT PEQKAYVPAM FTAALNIQTS VNTVVRDFEN YVKQTCNSSA 130 140 150 160 170 180 VVDNKLKIQN VIIDECYGAP GSPTNLEFIN TGSSKGNCAI KALMQLTTKA TTQIAPKQVA 190 200 210 220 230 240 GTGVQFYMIV IGVIILAALF MYYAKRMLFT STNDKIKLIL ANKENVHWTT YMDTFFRTSP 250 MVIATTDMQN

References

[1]	"Nucleotide sequence of a cluster of early and late genes in a conserved segment of the vaccinia virus genome." Plucienniczak A., Schroeder E., Zettlmeissl G., Streeck R.E. Nucleic Acids Res. 13:985-998(1985) [PubMed: 2987815] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Use of a cell-free system to identify the vaccinia virus L1R gene product as the major late myristylated virion protein M25." Franke C.A., Wilson E.M., Hruby D.E. J. Virol. 64:5988-5996(1990) [PubMed: 2243383] [Abstract] Cited for: MYRISTOYLATION AT GLY-2.
[3]	"Conditional lethal expression of the vaccinia virus L1R myristylated protein reveals a role in virion assembly." Ravanello M.P., Hruby D.E. J. Virol. 68:6401-6410(1994) [PubMed: 8083978] [Abstract] Cited for: FUNCTION.
[4]	"Identification and analysis of three myristylated vaccinia virus late proteins." Martin K.H., Grosenbach D.W., Franke C.A., Hruby D.E. J. Virol. 71:5218-5226(1997) [PubMed: 9188589] [Abstract] Cited for: MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2.
[5]	"The 1.51-Angstrom structure of the poxvirus L1 protein, a target of potent neutralizing antibodies." Su H.P., Garman S.C., Allison T.J., Fogg C., Moss B., Garboczi D.N. Proc. Natl. Acad. Sci. U.S.A. 102:4240-4245(2005) [PubMed: 15761054] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) OF 1-185.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X01978 Genomic DNA. Translation: CAA26010.1.

PIR

QQVZF2. B23092.

RefSeq

YP_232970.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YPY	X-ray	1.51	A/B	2-185	[»]
2I9L	X-ray	3.10	I/J/K/L	2-184	[»]

ModBase

Search...

Genome annotation databases

GeneID

3707544.

Family and domain databases

InterPro

IPR003472. Virion_mem_poxvirus_L1.
[Graphical view]

Pfam

PF02442. L1R_F9L. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

VM25_VACCW

Accession

Primary (citable) accession number: P07612

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	October 13, 2009
This is version 57 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)