ID   A25_VACCW               Reviewed;          76 AA.
AC   P07608; Q76ZR1; Q8JQ91;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   02-JUN-2021, entry version 49.
DE   RecName: Full=Protein A2.5;
GN   OrderedLocusNames=VACWR121; ORFNames=A2.5L;
OS   Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS   WR)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10254;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=3008103; DOI=10.1093/nar/14.7.3003;
RA   Weinrich S.L., Hruby D.E.;
RT   "A tandemly-oriented late gene cluster within the vaccinia virus genome.";
RL   Nucleic Acids Res. 14:3003-3016(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA   Wohlhueter R.;
RT   "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT   redundancy and an error rate of 0.16/10kb.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH E10, INTERACTION WITH
RP   G4, AND FUNCTION.
RX   PubMed=11983854; DOI=10.1073/pnas.062163799;
RA   Senkevich T.G., White C.L., Koonin E.V., Moss B.;
RT   "Complete pathway for protein disulfide bond formation encoded by
RT   poxviruses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:6667-6672(2002).
RN   [4]
RP   FUNCTION, SUBUNIT, AND MUTAGENESIS OF CYS-17 AND CYS-21.
RX   PubMed=12350360; DOI=10.1006/viro.2002.1608;
RA   Senkevich T.G., White C.L., Weisberg A., Granek J.A., Wolffe E.J.,
RA   Koonin E.V., Moss B.;
RT   "Expression of the vaccinia virus A2.5L redox protein is required for
RT   virion morphogenesis.";
RL   Virology 300:296-303(2002).
CC   -!- FUNCTION: Late protein which probably participates in disulfide bond
CC       formation by functioning as a thiol-disulfide transfer protein between
CC       membrane-associated E10 and G4. The complete pathway for formation of
CC       disulfide bonds in intracellular virion membrane proteins sequentially
CC       involves oxidation of E10, A2.5 and G4. {ECO:0000269|PubMed:11983854,
CC       ECO:0000269|PubMed:12350360}.
CC   -!- SUBUNIT: Interacts with sulfhydryl oxidase E10; this interaction
CC       involves formation of a transient disulfide-bonded intermediate,
CC       allowing disulfide bond transfer. Interacts with G4; this interaction
CC       involves formation of a transient disulfide-bonded intermediate,
CC       allowing disulfide bond transfer. {ECO:0000269|PubMed:11983854,
CC       ECO:0000269|PubMed:12350360}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:3008103}.
CC   -!- SIMILARITY: Belongs to the chordopoxvirinae A2.5 family. {ECO:0000305}.
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DR   EMBL; X03729; CAA27365.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89400.1; -; Genomic_DNA.
DR   EMBL; AF516336; AAM49617.1; -; Genomic_DNA.
DR   PIR; A23768; WMVZR0.
DR   RefSeq; YP_233003.1; NC_006998.1.
DR   PRIDE; P07608; -.
DR   DNASU; 3707519; -.
DR   GeneID; 3707519; -.
DR   KEGG; vg:3707519; -.
DR   Proteomes; UP000000344; Genome.
DR   InterPro; IPR007952; Poxvirus_A3L.
DR   Pfam; PF05288; Pox_A3L; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Late protein; Redox-active center; Reference proteome.
FT   CHAIN           1..76
FT                   /note="Protein A2.5"
FT                   /id="PRO_0000099744"
FT   DISULFID        17..21
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255"
FT   VARIANT         12..13
FT                   /note="NP -> KS"
FT   VARIANT         35
FT                   /note="N -> H"
FT   MUTAGEN         17
FT                   /note="C->S: Accumulation of reduced G4, L1, and F9."
FT                   /evidence="ECO:0000269|PubMed:12350360"
FT   MUTAGEN         21
FT                   /note="C->S: Accumulation of reduced G4, L1, and F9."
FT                   /evidence="ECO:0000269|PubMed:12350360"
SQ   SEQUENCE   76 AA;  8927 MW;  2FEDFE4E8DBC5A55 CRC64;
     MSWYEKYNIV LNPPKRCSFA CADNLTTILA EDGNNIRAIL YSQPKKLKIL QDFLATSRNK
     MFLYKILDDE IRRVLT