VL1_HPV11
ID VL1_HPV11 Reviewed; 501 AA.
AC P04012;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 23-FEB-2022, entry version 109.
DE RecName: Full=Major capsid protein L1 {ECO:0000255|HAMAP-Rule:MF_04002};
GN Name=L1 {ECO:0000255|HAMAP-Rule:MF_04002};
OS Human papillomavirus 11.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=10580;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3008427; DOI=10.1016/0042-6822(86)90110-8;
RA Dartmann K., Schwarz E., Gissmann L., zur Hausen H.;
RT "The nucleotide sequence and genome organization of human papilloma virus
RT type 11.";
RL Virology 151:124-130(1986).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 20-470.
RX PubMed=17804402; DOI=10.1074/jbc.m706380200;
RA Bishop B., Dasgupta J., Klein M., Garcea R.L., Christensen N.D., Zhao R.,
RA Chen X.S.;
RT "Crystal structures of four types of human papillomavirus L1 capsid
RT proteins: understanding the specificity of neutralizing monoclonal
RT antibodies.";
RL J. Biol. Chem. 282:31803-31811(2007).
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}.
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DR EMBL; M14119; AAA46935.1; -; Genomic_DNA.
DR PIR; A03639; P1WL11.
DR PDB; 2R5K; X-ray; 3.20 A; A/B/C/D/E=20-399, A/B/C/D/E=433-470.
DR PDBsum; 2R5K; -.
DR SMR; P04012; -.
DR MINT; P04012; -.
DR EvolutionaryTrace; P04012; -.
DR Proteomes; UP000008222; 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 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Disulfide bond; Host nucleus;
KW Host-virus interaction; Late protein; Reference proteome;
KW T=7 icosahedral capsid protein; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT CHAIN 1..501
FT /note="Major capsid protein L1"
FT /id="PRO_0000133495"
FT REGION 472..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 172
FT /note="Interchain (with C-424)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT DISULFID 424
FT /note="Interchain (with C-172)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:2R5K"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2R5K"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 93..106
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 150..159
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:2R5K"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:2R5K"
FT TURN 219..223
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:2R5K"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 244..259
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:2R5K"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:2R5K"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:2R5K"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:2R5K"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 327..332
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:2R5K"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 356..378
FT /evidence="ECO:0007829|PDB:2R5K"
FT HELIX 381..390
FT /evidence="ECO:0007829|PDB:2R5K"
FT HELIX 392..397
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:2R5K"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:2R5K"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:2R5K"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:2R5K"
FT HELIX 459..467
FT /evidence="ECO:0007829|PDB:2R5K"
SQ SEQUENCE 501 AA; 55835 MW; 88957D023CC182A7 CRC64;
MWRPSDSTVY VPPPNPVSKV VATDAYVKRT NIFYHASSSR LLAVGHPYYS IKKVNKTVVP
KVSGYQYRVF KVVLPDPNKF ALPDSSLFDP TTQRLVWACT GLEVGRGQPL GVGVSGHPLL
NKYDDVENSG GYGGNPGQDN RVNVGMDYKQ TQLCMVGCAP PLGEHWGKGT QCSNTSVQNG
DCPPLELITS VIQDGDMVDT GFGAMNFADL QTNKSDVPLD ICGTVCKYPD YLQMAADPYG
DRLFFYLRKE QMFARHFFNR AGTVGEPVPD DLLVKGGNNR SSVASSIYVH TPSGSLVSSE
AQLFNKPYWL QKAQGHNNGI CWGNHLFVTV VDTTRSTNMT LCASVSKSAT YTNSDYKEYM
RHVEEFDLQF IFQLCSITLS AEVMAYIHTM NPSVLEDWNF GLSPPPNGTL EDTYRYVQSQ
AITCQKPTPE KEKQDPYKDM SFWEVNLKEK FSSELDQFPL GRKFLLQSGY RGRTSARTGI
KRPAVSKPST APKRKRTKTK K
