A26_VACCW
ID A26_VACCW Reviewed; 500 AA.
AC P24758; Q80HU7;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Protein A26;
GN OrderedLocusNames=VACWR149; ORFNames=A26L;
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].
RX PubMed=1856205; DOI=10.1016/s0021-9258(18)92757-2;
RA Amegadzie B.Y., Ahn B.-Y., Moss B.;
RT "Identification, sequence, and expression of the gene encoding a Mr 35,000
RT subunit of the vaccinia virus DNA-dependent RNA polymerase.";
RL J. Biol. Chem. 266:13712-13718(1991).
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 INTERACTION WITH HOST LAMININ.
RX PubMed=17166913; DOI=10.1128/jvi.02302-06;
RA Chiu W.L., Lin C.L., Yang M.H., Tzou D.L., Chang W.;
RT "Vaccinia virus 4c (A26L) protein on intracellular mature virus binds to
RT the extracellular cellular matrix laminin.";
RL J. Virol. 81:2149-2157(2007).
RN [4]
RP INTERACTION WITH A17.
RX PubMed=18842719; DOI=10.1128/jvi.01524-08;
RA Howard A.R., Senkevich T.G., Moss B.;
RT "Vaccinia virus A26 and A27 proteins form a stable complex tethered to
RT mature virions by association with the A17 transmembrane protein.";
RL J. Virol. 82:12384-12391(2008).
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH A27, AND MUTAGENESIS OF CYS-441 AND
RP CYS-442.
RX PubMed=19369327; DOI=10.1128/jvi.02295-08;
RA Ching Y.C., Chung C.S., Huang C.Y., Hsia Y., Tang Y.L., Chang W.;
RT "Disulfide bond formation at the C termini of vaccinia virus A26 and A27
RT proteins does not require viral redox enzymes and suppresses
RT glycosaminoglycan-mediated cell fusion.";
RL J. Virol. 83:6464-6476(2009).
RN [6]
RP INTERACTION WITH PROTEIN A25.
RX PubMed=20484506; DOI=10.1128/jvi.00704-10;
RA Howard A.R., Weisberg A.S., Moss B.;
RT "Congregation of orthopoxvirus virions in cytoplasmic A-type inclusions is
RT mediated by interactions of a bridging protein (A26p) with a matrix protein
RT (ATIp) and a virion membrane-associated protein (A27p).";
RL J. Virol. 84:7592-7602(2010).
RN [7]
RP FUNCTION.
RX PubMed=20538855; DOI=10.1128/jvi.00599-10;
RA Chang S.J., Chang Y.X., Izmailyan R., Tang Y.L., Chang W.;
RT "Vaccinia virus A25 and A26 proteins are fusion suppressors for mature
RT virions and determine strain-specific virus entry pathways into HeLa, CHO-
RT K1, and L cells.";
RL J. Virol. 84:8422-8432(2010).
CC -!- FUNCTION: Plays a role in bridging the mature virion with structural
CC protein A25. Presence of protein A26 in the virion structurally
CC prevents direct virus-cell fusion mechanism.
CC {ECO:0000269|PubMed:20538855}.
CC -!- SUBUNIT: Interacts with proteins A17, A25 and A27. Interacts with host
CC laminin. {ECO:0000269|PubMed:17166913, ECO:0000269|PubMed:18842719,
CC ECO:0000269|PubMed:19369327, ECO:0000269|PubMed:20484506}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:19369327}.
CC Note=A26 is anchored to the mature virion (MV) membrane through
CC disulfide bonding with protein A27.
CC -!- SIMILARITY: Belongs to the chordopoxvirinae A26 protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA48323.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA40576.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M61187; AAA48323.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X57318; CAA40576.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY243312; AAO89428.1; -; Genomic_DNA.
DR PIR; S29910; S29910.
DR RefSeq; YP_233031.1; NC_006998.1.
DR PDB; 6A9S; X-ray; 1.18 A; A=1-397.
DR PDBsum; 6A9S; -.
DR SMR; P24758; -.
DR DNASU; 3707679; -.
DR GeneID; 3707679; -.
DR KEGG; vg:3707679; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:InterPro.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
DR InterPro; IPR003436; Chordopox_Fusion/A27.
DR InterPro; IPR009285; Orthopox_A30L/A26L.
DR Pfam; PF06086; Pox_A30L_A26L; 1.
DR Pfam; PF02346; Vac_Fusion; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Membrane; Reference proteome; Virion.
FT CHAIN 1..500
FT /note="Protein A26"
FT /id="PRO_0000099278"
FT DISULFID 43..342
FT DISULFID 441
FT /note="Interchain (with C-71 in A27)"
FT DISULFID 442
FT /note="Interchain (with C-72 in A27)"
FT MUTAGEN 441
FT /note="C->A: About 50% loss of interaction with A27.
FT Complete loss of interaction with A2; when associated with
FT A-442."
FT /evidence="ECO:0000269|PubMed:19369327"
FT MUTAGEN 442
FT /note="C->A: About 60% loss of interaction with A27.
FT Complete loss of interaction with A2; when associated with
FT A-441."
FT /evidence="ECO:0000269|PubMed:19369327"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 46..62
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 90..107
FT /evidence="ECO:0007829|PDB:6A9S"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:6A9S"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 151..176
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:6A9S"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:6A9S"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 255..261
FT /evidence="ECO:0007829|PDB:6A9S"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:6A9S"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:6A9S"
FT STRAND 285..294
FT /evidence="ECO:0007829|PDB:6A9S"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:6A9S"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:6A9S"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 325..331
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:6A9S"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:6A9S"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:6A9S"
SQ SEQUENCE 500 AA; 57994 MW; 52400EEADBFAB766 CRC64;
MANIINLWNG IVPTVQDVNV ASITAFKSMI DETWDKKIEA NTCISRKHRN IIHEVIRDFM
KAYPKMDENK KSPLGAPMQW LTQYYILKNE YHKTMLAYDN GSLNTKFKTL NIYMITNVGQ
YILYIVFCII SGKNHDGTPY IYDSEITSND KNFINERIKY ACKQILHGQL TIALRIRNKF
MFIGSPMYLW FNVNGSQVYH DIYDRNAGFH NKEIGRLLYA FMYYLSISGR FLNDFALLKF
TYLGESWTFS LSVPEYILYG LGYSVFDTIE KFSNDAILVY IRTNNRNGYD YVEFNKKGIA
KVTEDKPDND KRIHAIRLIN DSTDVQHIHF GFRNMVIIDN ECANIQSSAE NATDTGHHQD
SKINIEVEDD VIDDDDYNPK PTPIPEPHPR PPFPRHEYHK RPKLLPVEEP DPVKKDADRI
RLDNHILNTL DHNLNFIGHY CCDTAAVDRL EHHIETLGQY AVILARKINM QTLLFPWPLP
TVHPHAIDGS IPPHGRSTIL
