ID   A25_VACCC               Reviewed;          76 AA.
AC   P0CK20;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   29-SEP-2021, entry version 21.
DE   RecName: Full=Protein A2.5;
GN   ORFNames=A2.5L;
OS   Vaccinia virus (strain Copenhagen) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "The complete DNA sequence of vaccinia virus.";
RL   Virology 179:247-266(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL   Virology 179:517-563(1990).
RN   [3]
RP   IDENTIFICATION.
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC   -!- SIMILARITY: Belongs to the chordopoxvirinae A2.5 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M35027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Proteomes; UP000008269; Genome.
DR   InterPro; IPR007952; Poxvirus_A3L.
DR   Pfam; PF05288; Pox_A3L; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Late protein; Redox-active center; Reference proteome.
FT   CHAIN           1..76
FT                   /note="Protein A2.5"
FT                   /id="PRO_0000411964"
FT   DISULFID        17..21
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   76 AA;  8890 MW;  2FFF0CD0E6A95A55 CRC64;
     MSWYEKYNIV LNPPKRCSSA CADNLTTILA EDGNHIRAIL YSQPKKLKIL QDFLATSRNK
     MFLYKILDDE IRRVLT