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A33_VACCW
ID   A33_VACCW               Reviewed;         185 AA.
AC   P68617; P21056; Q76ZP3;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Protein A33;
GN   OrderedLocusNames=VACWR156; ORFNames=A33R;
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=2045793; DOI=10.1099/0022-1317-72-6-1349;
RA   Smith G.L., Chan Y.S., Howard S.T.;
RT   "Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the
RT   right inverted terminal repeat.";
RL   J. Gen. Virol. 72:1349-1376(1991).
RN   [2]
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   [3]
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   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8648710; DOI=10.1128/jvi.70.6.3753-3762.1996;
RA   Roper R.L., Payne L.G., Moss B.;
RT   "Extracellular vaccinia virus envelope glycoprotein encoded by the A33R
RT   gene.";
RL   J. Virol. 70:3753-3762(1996).
RN   [5]
RP   FUNCTION.
RX   PubMed=9557708; DOI=10.1128/jvi.72.5.4192-4204.1998;
RA   Roper R.L., Wolffe E.J., Weisberg A., Moss B.;
RT   "The envelope protein encoded by the A33R gene is required for formation of
RT   actin-containing microvilli and efficient cell-to-cell spread of vaccinia
RT   virus.";
RL   J. Virol. 72:4192-4204(1998).
RN   [6]
RP   INTERACTION WITH PROTEIN A36.
RX   PubMed=10074134; DOI=10.1128/jvi.73.4.2863-2875.1999;
RA   Rottger S., Frischknecht F., Reckmann I., Smith G.L., Way M.;
RT   "Interactions between vaccinia virus IEV membrane proteins and their roles
RT   in IEV assembly and actin tail formation.";
RL   J. Virol. 73:2863-2875(1999).
RN   [7]
RP   FUNCTION.
RX   PubMed=11119600; DOI=10.1128/jvi.75.1.303-310.2001;
RA   Wolffe E.J., Weisberg A.S., Moss B.;
RT   "The vaccinia virus A33R protein provides a chaperone function for viral
RT   membrane localization and tyrosine phosphorylation of the A36R protein.";
RL   J. Virol. 75:303-310(2001).
RN   [8]
RP   FUNCTION.
RX   PubMed=14581563; DOI=10.1128/jvi.77.22.12266-12275.2003;
RA   Katz E., Ward B.M., Weisberg A.S., Moss B.;
RT   "Mutations in the vaccinia virus A33R and B5R envelope proteins that
RT   enhance release of extracellular virions and eliminate formation of actin-
RT   containing microvilli without preventing tyrosine phosphorylation of the
RT   A36R protein.";
RL   J. Virol. 77:12266-12275(2003).
RN   [9]
RP   INTERACTION WITH B5.
RX   PubMed=16912323; DOI=10.1128/jvi.00598-06;
RA   Perdiguero B., Blasco R.;
RT   "Interaction between vaccinia virus extracellular virus envelope A33 and B5
RT   glycoproteins.";
RL   J. Virol. 80:8763-8777(2006).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16509968; DOI=10.1186/1743-422x-3-10;
RA   Yoder J.D., Chen T.S., Gagnier C.R., Vemulapalli S., Maier C.S.,
RA   Hruby D.E.;
RT   "Pox proteomics: mass spectrometry analysis and identification of Vaccinia
RT   virion proteins.";
RL   Virol. J. 3:10-10(2006).
RN   [11]
RP   SUBUNIT.
RX   PubMed=20947114; DOI=10.1016/j.virol.2010.09.021;
RA   Chan W.M., Kalkanoglu A.E., Ward B.M.;
RT   "The inability of vaccinia virus A33R protein to form intermolecular
RT   disulfide-bonded homodimers does not affect the production of infectious
RT   extracellular virus.";
RL   Virology 408:109-118(2010).
RN   [12]
RP   DOMAIN.
RX   PubMed=20302896; DOI=10.1016/j.virusres.2010.03.004;
RA   Krupovic M., Cvirkaite-Krupovic V., Bamford D.H.;
RT   "Protein A33 responsible for antibody-resistant spread of Vaccinia virus is
RT   homologous to C-type lectin-like proteins.";
RL   Virus Res. 151:97-101(2010).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 90-185.
RX   PubMed=20032175; DOI=10.1128/jvi.02247-09;
RA   Su H.P., Singh K., Gittis A.G., Garboczi D.N.;
RT   "The structure of the poxvirus A33 protein reveals a dimer of unique C-type
RT   lectin-like domains.";
RL   J. Virol. 84:2502-2510(2010).
CC   -!- FUNCTION: Coordinates the incorporation of A36 into wrapped enveloped
CC       virion (EV) membranes and, subsequently, the production of actin tails.
CC       Therefore plays an essential role in efficient cell-to-cell spread of
CC       viral particles. {ECO:0000269|PubMed:11119600,
CC       ECO:0000269|PubMed:14581563, ECO:0000269|PubMed:9557708}.
CC   -!- SUBUNIT: Homodimer, disulfide-linked. Interacts with protein B5.
CC       Interacts (via C-terminus) with protein A36.
CC       {ECO:0000269|PubMed:10074134, ECO:0000269|PubMed:16912323,
CC       ECO:0000269|PubMed:20947114}.
CC   -!- INTERACTION:
CC       P68617; P04021: VACWR052; NbExp=2; IntAct=EBI-7133633, EBI-7736497;
CC       P68617; P68619: VACWR159; NbExp=7; IntAct=EBI-7133633, EBI-7133540;
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type
CC       II membrane protein {ECO:0000305}. Host membrane {ECO:0000305}; Single-
CC       pass type II membrane protein {ECO:0000305}. Note=Component of the
CC       enveloped virion (EV) membrane. {ECO:0000269|PubMed:8648710}.
CC   -!- SIMILARITY: Belongs to the chordopoxvirinae A33 protein family.
CC       {ECO:0000305}.
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DR   EMBL; D11079; BAA01805.1; -; Genomic_DNA.
DR   EMBL; M61187; AAA48330.1; -; Genomic_DNA.
DR   EMBL; X57318; CAA40583.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89435.1; -; Genomic_DNA.
DR   PIR; H42520; H42520.
DR   RefSeq; YP_233038.1; NC_006998.1.
DR   PDB; 3K7B; X-ray; 2.10 A; A/B=90-185.
DR   PDBsum; 3K7B; -.
DR   SMR; P68617; -.
DR   IntAct; P68617; 4.
DR   MINT; P68617; -.
DR   ABCD; P68617; 9 sequenced antibodies.
DR   DNASU; 3707686; -.
DR   GeneID; 3707686; -.
DR   KEGG; vg:3707686; -.
DR   EvolutionaryTrace; P68617; -.
DR   Proteomes; UP000000344; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR009238; Chordopox_A33R.
DR   Pfam; PF05966; Chordopox_A33R; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Glycoprotein; Host membrane; Membrane;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Viral envelope protein; Virion.
FT   CHAIN           1..185
FT                   /note="Protein A33"
FT                   /id="PRO_0000099317"
FT   TOPO_DOM        1..33
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        34..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..185
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000250"
FT   REGION          98..185
FT                   /note="C-type lectin-like domain"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        62
FT                   /note="Interchain"
FT   STRAND          101..105
FT                   /evidence="ECO:0007829|PDB:3K7B"
FT   STRAND          108..117
FT                   /evidence="ECO:0007829|PDB:3K7B"
FT   HELIX           119..128
FT                   /evidence="ECO:0007829|PDB:3K7B"
FT   HELIX           136..139
FT                   /evidence="ECO:0007829|PDB:3K7B"
FT   HELIX           145..148
FT                   /evidence="ECO:0007829|PDB:3K7B"
FT   STRAND          156..159
FT                   /evidence="ECO:0007829|PDB:3K7B"
FT   STRAND          176..183
FT                   /evidence="ECO:0007829|PDB:3K7B"
SQ   SEQUENCE   185 AA;  20506 MW;  201CF65C2D2076A4 CRC64;
     MMTPENDEEQ TSVFSATVYG DKIQGKNKRK RVIGLCIRIS MVISLLSMIT MSAFLIVRLN
     QCMSANEAAI TDAAVAVAAA SSTHRKVASS TTQYDHKESC NGLYYQGSCY ILHSDYQLFS
     DAKANCTAES STLPNKSDVL ITWLIDYVED TWGSDGNPIT KTTSDYQDSD VSQEVRKYFC
     VKTMN
 
 
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