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VL1_BPV3
ID   VL1_BPV3                Reviewed;         510 AA.
AC   P50805; Q705F7; Q8BDD3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   23-FEB-2022, entry version 94.
DE   RecName: Full=Major capsid protein L1 {ECO:0000255|HAMAP-Rule:MF_04002};
GN   Name=L1 {ECO:0000255|HAMAP-Rule:MF_04002};
OS   Bovine papillomavirus type 3.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Xipapillomavirus.
OX   NCBI_TaxID=10561;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12208979; DOI=10.1128/jvi.76.19.10020-10023.2002;
RA   Terai M., DeSalle R., Burk R.D.;
RT   "Lack of canonical E6 and E7 open reading frames in bird papillomaviruses:
RT   Fringilla coelebs papillomavirus and Psittacus erithacus timneh
RT   papillomavirus.";
RL   J. Virol. 76:10020-10023(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Delius H., de Villiers E.M.;
RT   "Sequencing of the complete genomes of BPV 3, BPV 5 and BPV 6.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 368-462.
RX   PubMed=7707535; DOI=10.1128/jvi.69.5.3074-3083.1995;
RA   Chan S.-Y., Delius H., Halpern A.L., Bernard H.U.;
RT   "Analysis of genomic sequences of 95 papillomavirus types: uniting typing,
RT   phylogeny, and taxonomy.";
RL   J. Virol. 69:3074-3083(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 422-510.
RX   PubMed=1849970; DOI=10.1099/0022-1317-72-4-877;
RA   Jackson M.E., Campo M.S.;
RT   "Positive and negative E2-independent regulatory elements in the long
RT   control region of bovine papillomavirus type 4.";
RL   J. Gen. Virol. 72:877-883(1991).
CC   -!- FUNCTION: Forms an icosahedral capsid with a T=7 symmetry and a 50 nm
CC       diameter. The capsid is composed of 72 pentamers linked to each other
CC       by disulfide bonds and associated with L2 proteins. Binds to heparan
CC       sulfate proteoglycans on cell surface of basal layer keratinocytes to
CC       provide initial virion attachment. This binding mediates a
CC       conformational change in the virus capsid that facilitates efficient
CC       infection. The virion enters the host cell via endocytosis. During
CC       virus trafficking, L1 protein dissociates from the viral DNA and the
CC       genomic DNA is released to the host nucleus. The virion assembly takes
CC       place within the cell nucleus. Encapsulates the genomic DNA together
CC       with protein L2. {ECO:0000255|HAMAP-Rule:MF_04002}.
CC   -!- SUBUNIT: Self-assembles into homopentamers. The capsid has an
CC       icosahedral symmetry and consists of 72 capsomers, with each capsomer
CC       being a pentamer of L1. Interacts with the minor capsid protein L2;
CC       this interaction is necessary for viral genome encapsidation. Interacts
CC       with protein E2; this interaction enhances E2-dependent replication and
CC       transcription activation. {ECO:0000255|HAMAP-Rule:MF_04002}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04002}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04002}.
CC   -!- SIMILARITY: Belongs to the papillomaviridae L1 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04002}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN09961.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAF05683.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF486184; AAN09961.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AJ620207; CAF05684.1; -; Genomic_DNA.
DR   EMBL; AJ620207; CAF05683.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U21862; AAA92825.1; -; Genomic_DNA.
DR   EMBL; X59062; CAA41786.1; -; Genomic_DNA.
DR   PIR; S15467; S15467.
DR   RefSeq; NP_694451.2; NC_004197.1.
DR   SMR; P50805; -.
DR   GeneID; 955382; -.
DR   KEGG; vg:955382; -.
DR   Proteomes; UP000006369; Genome.
DR   Proteomes; UP000185274; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0039620; C:T=7 icosahedral viral capsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.175.20; -; 2.
DR   HAMAP; MF_04002; PPV_L1; 1.
DR   InterPro; IPR002210; Capsid_L1_Papillomavir.
DR   InterPro; IPR036973; Capsid_L1_sf_Papillomavir.
DR   InterPro; IPR011222; dsDNA_vir_gr_I_capsid.
DR   Pfam; PF00500; Late_protein_L1; 1.
DR   PRINTS; PR00865; HPVCAPSIDL1.
DR   SUPFAM; SSF88648; SSF88648; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Disulfide bond; Host nucleus; Host-virus interaction;
KW   Late protein; Reference proteome; T=7 icosahedral capsid protein;
KW   Viral attachment to host cell; Viral penetration into host cytoplasm;
KW   Virion; Virus endocytosis by host; Virus entry into host cell.
FT   CHAIN           1..510
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133477"
FT   REGION          482..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        174
FT                   /note="Interchain (with C-432)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        432
FT                   /note="Interchain (with C-174)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   CONFLICT        398
FT                   /note="G -> C (in Ref. 3; AAA92825)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   510 AA;  58033 MW;  15E69973785C8517 CRC64;
     MSFWLPSQGK LYLPPPTAVT QYLDTDDFVT RTDTFYHTNT ERLLFVGHPY FDIKREDKVL
     VPKVSGSQFR VFRLKFPDPN KFSFPDPNVY NSDNQRLVWA LRGIEICRGQ PLGIGVTGHP
     SFNKFKDAEN NNNKTPDQTT DDRVNMAVDP KQVQMFIVGC TPCDGEHWDV AQACDRLEPG
     ACPPIELKNT IIEDGEMCDT GFGNMNFQKL QASKSGAPLD IVNQIVKYPD FLKMGSDPHG
     NSMFFYAKRE QMYVRHLWSR GGTIGEEIPP NGEASPYYLP GAGRATLPTS VYFGSPSGSL
     VSSDQQIYNR PFWIQRAQGR NNGICWNNQL FVTAVDSTRG TNFTISVHRD KPSLEDQDTY
     TAAEFKHYLR HVEEWEVSLV LQLCIVDLTP EALAHINGMD PRIIESWNLG FIHAPNNIED
     QYRYLQSIAT RCPPKEDAAA TEDPYAKYTF WDVDLTERFS MNLDQYSLGR KFLFQIGKKS
     RGIKRSAPKA VTFESSSRSK KAPKRRRKNV
 
 
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