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H3_VACCW
ID   H3_VACCW                Reviewed;         324 AA.
AC   P07240; Q80HW3;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   02-JUN-2021, entry version 79.
DE   RecName: Full=Envelope protein H3;
DE   AltName: Full=Ag35;
DE   AltName: Full=Virion envelope protein p35;
GN   OrderedLocusNames=VACWR101; ORFNames=H3L;
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=3021979; DOI=10.1128/jvi.60.2.436-449.1986;
RA   Rosel J.L., Earl P.L., Weir J.P., Moss B.;
RT   "Conserved TAAATG sequence at the transcriptional and translational
RT   initiation sites of vaccinia virus late genes deduced by structural and
RT   functional analysis of the HindIII H genome fragment.";
RL   J. Virol. 60:436-449(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   FUNCTION.
RX   PubMed=2462305;
RA   Gordon J., Kovala T., Dales S.;
RT   "Molecular characterization of a prominent antigen of the vaccinia virus
RT   envelope.";
RL   Virology 167:361-369(1988).
RN   [4]
RP   FUNCTION.
RX   PubMed=10708453; DOI=10.1128/jvi.74.7.3353-3365.2000;
RA   Lin C.L., Chung C.-S., Heine H.G., Chang W.;
RT   "Vaccinia virus envelope H3L protein binds to cell surface heparan sulfate
RT   and is important for intracellular mature virion morphogenesis and virus
RT   infection in vitro and in vivo.";
RL   J. Virol. 74:3353-3365(2000).
RN   [5]
RP   TOPOLOGY, SIGNAL-ANCHOR, INDUCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10906204; DOI=10.1128/jvi.74.16.7508-7517.2000;
RA   da Fonseca F.G., Wolffe E.J., Weisberg A., Moss B.;
RT   "Characterization of the vaccinia virus H3L envelope protein: topology and
RT   posttranslational membrane insertion via the C-terminal hydrophobic tail.";
RL   J. Virol. 74:7508-7517(2000).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=10906205; DOI=10.1128/jvi.74.16.7518-7528.2000;
RA   da Fonseca F.G., Wolffe E.J., Weisberg A., Moss B.;
RT   "Effects of deletion or stringent repression of the H3L envelope gene on
RT   vaccinia virus replication.";
RL   J. Virol. 74:7518-7528(2000).
CC   -!- FUNCTION: Envelope protein that binds to heparan sulfate on the cell
CC       surface and might provide virion attachment to target cell.
CC       {ECO:0000250, ECO:0000269|PubMed:10708453, ECO:0000269|PubMed:2462305}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:10906204};
CC       Single-pass membrane protein {ECO:0000269|PubMed:10906204}.
CC       Note=Component of the mature virion (MV) membrane. Becomes membrane
CC       associated presumably during virus maturation. The mature virion is
CC       located in the cytoplasm of infected cells and is probably released by
CC       cell lysis.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:10906204}.
CC   -!- PTM: Does not contain disulfide bonds. {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Impaired virion assembly.
CC       {ECO:0000269|PubMed:10906205}.
CC   -!- MISCELLANEOUS: Immunodominant protein.
CC   -!- SIMILARITY: Belongs to the chordopoxvirinae protein H3 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally mixed up with the protein H5 encoded by encoded
CC       by H5R gene. {ECO:0000305|PubMed:2462305}.
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DR   EMBL; M13209; AAB59838.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89380.1; -; Genomic_DNA.
DR   PIR; C24481; QQVZH3.
DR   PDB; 5EJ0; X-ray; 1.90 A; A=4-240.
DR   PDBsum; 5EJ0; -.
DR   SMR; P07240; -.
DR   Proteomes; UP000000344; Genome.
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   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR004900; Poxvirus_P35.
DR   Pfam; PF03213; Pox_P35; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Host-virus interaction; Late protein; Membrane;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Viral attachment to host cell; Viral envelope protein; Virion;
KW   Virus entry into host cell.
FT   CHAIN           1..324
FT                   /note="Envelope protein H3"
FT                   /id="PRO_0000099208"
FT   TOPO_DOM        1..284
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        285..305
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        306..324
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        195
FT                   /note="E -> A (in Ref. 2; AAO89380)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..11
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   STRAND          13..16
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   HELIX           18..20
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   STRAND          62..67
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   HELIX           92..105
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   HELIX           108..115
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   STRAND          120..125
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   HELIX           136..145
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   STRAND          150..152
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   STRAND          164..169
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   STRAND          172..178
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   STRAND          186..191
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   HELIX           192..204
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   HELIX           212..222
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   STRAND          227..230
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   HELIX           233..235
FT                   /evidence="ECO:0007829|PDB:5EJ0"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:5EJ0"
SQ   SEQUENCE   324 AA;  37504 MW;  FF3734631040617F CRC64;
     MAAAKTPVIV VPVIDRLPSE TFPNVHEHIN DQKFDDVKDN EVMPEKRNVV VVKDDPDHYK
     DYAFIQWTGG NIRNDDKYTH FFSGFCNTMC TEETKRNIAR HLALWDSNFF TELENKKVEY
     VVIVENDNVI EDITFLRPVL KAMHDKKIDI LQMREIITGN KVKTELVMDK NHAIFTYTGG
     YDVSLSAYII RVTTELNIVD EIIKSGGLSS GFYFEIARIE NEMKINRQIL DNAAKYVEHD
     PRLVAEHRFE NMKPNFWSRI GTAATKRYPG VMYAFTTPLI SFFGLFDINV IGLIVILFIM
     FMLIFNVKSK LLWFLTGTFV TAFI
 
 
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