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A25_VAR67
ID   A25_VAR67               Reviewed;          76 AA.
AC   Q07032; Q9QNI1;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   02-JUN-2021, entry version 57.
DE   RecName: Full=Protein A2.5;
GN   ORFNames=A2.5L;
OS   Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=587200;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8384129; DOI=10.1016/0014-5793(93)80041-r;
RA   Shchelkunov S.N., Blinov V.M., Sandakhchiev L.S.;
RT   "Genes of variola and vaccinia viruses necessary to overcome the host
RT   protective mechanisms.";
RL   FEBS Lett. 319:80-83(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7856312; DOI=10.1016/0168-1702(94)90125-2;
RA   Shchelkunov S.N., Blinov V.M., Resenchuk S.M., Totmenin A.V., Olenina L.V.,
RA   Chirikova G.B., Sandakhchiev L.S.;
RT   "Analysis of the nucleotide sequence of 53 kbp from the right terminus of
RT   the genome of variola major virus strain India-1967.";
RL   Virus Res. 34:207-236(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7597802; DOI=10.1007/bf01702879;
RA   Shchelkunov S.N., Totmenin A.V.;
RT   "Two types of deletions in orthopoxvirus genomes.";
RL   Virus Genes 9:231-245(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8725113; DOI=10.1016/0168-1702(95)01269-9;
RA   Shchelkunov S.N., Totmenin A.V., Sandakhchiev L.S.;
RT   "Analysis of the nucleotide sequence of 23.8 kbp from the left terminus of
RT   the genome of variola major virus strain India-1967.";
RL   Virus Res. 40:169-183(1996).
CC   -!- FUNCTION: Late protein which probably participates in disulfide bond
CC       formation by functioning as a thiol-disulfide transfer 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}.
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DR   EMBL; X69198; CAA49047.1; -; Genomic_DNA.
DR   PIR; H72163; H72163.
DR   PIR; T28544; T28544.
DR   RefSeq; NP_042150.1; NC_001611.1.
DR   PRIDE; Q07032; -.
DR   GeneID; 1486507; -.
DR   KEGG; vg:1486507; -.
DR   Proteomes; UP000002060; 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_0000411965"
FT   DISULFID        17..21
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   76 AA;  8929 MW;  D2A11E577B534F4E CRC64;
     MSWYEKYNIV LNPPKRCFSS CADNLTTILA EDGNNIRAIL YSQPQKLKVL QDFLATSRNK
     MFLYKILDDE IRRVLT
 
 
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