VL1_HPV33
ID VL1_HPV33 Reviewed; 499 AA.
AC P06416;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 33.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=10586;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3009902; DOI=10.1128/jvi.58.3.991-995.1986;
RA Cole S.T., Streeck R.E.;
RT "Genome organization and nucleotide sequence of human papillomavirus type
RT 33, which is associated with cervical cancer.";
RL J. Virol. 58:991-995(1986).
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; M12732; AAA46964.1; -; Genomic_DNA.
DR PIR; A03641; P1WL33.
DR PDB; 6IGE; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J=1-499.
DR PDBsum; 6IGE; -.
DR SMR; P06416; -.
DR PRIDE; P06416; -.
DR Proteomes; UP000009118; 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..499
FT /note="Major capsid protein L1"
FT /id="PRO_0000133517"
FT REGION 476..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 176
FT /note="Interchain (with C-427)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT DISULFID 427
FT /note="Interchain (with C-176)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:6IGE"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6IGE"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 97..110
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 154..163
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:6IGE"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:6IGE"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:6IGE"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 247..262
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:6IGE"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:6IGE"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:6IGE"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 342..349
FT /evidence="ECO:0007829|PDB:6IGE"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 359..381
FT /evidence="ECO:0007829|PDB:6IGE"
FT HELIX 384..393
FT /evidence="ECO:0007829|PDB:6IGE"
FT HELIX 396..401
FT /evidence="ECO:0007829|PDB:6IGE"
FT HELIX 439..442
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:6IGE"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:6IGE"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:6IGE"
FT HELIX 462..470
FT /evidence="ECO:0007829|PDB:6IGE"
SQ SEQUENCE 499 AA; 55903 MW; 283474DA993DE01D CRC64;
MSVWRPSEAT VYLPPVPVSK VVSTDEYVSR TSIYYYAGSS RLLAVGHPYF SIKNPTNAKK
LLVPKVSGLQ YRVFRVRLPD PNKFGFPDTS FYNPDTQRLV WACVGLEIGR GQPLGVGISG
HPLLNKFDDT ETGNKYPGQP GADNRECLSM DYKQTQLCLL GCKPPTGEHW GKGVACTNAA
PANDCPPLEL INTIIEDGDM VDTGFGCMDF KTLQANKSDV PIDICGSTCK YPDYLKMTSE
PYGDSLFFFL RREQMFVRHF FNRAGTLGEA VPDDLYIKGS GTTASIQSSA FFPTPSGSMV
TSESQLFNKP YWLQRAQGHN NGICWGNQVF VTVVDTTRST NMTLCTQVTS DSTYKNENFK
EYIRHVEEYD LQFVFQLCKV TLTAEVMTYI HAMNPDILED WQFGLTPPPS ASLQDTYRFV
TSQAITCQKT VPPKEKEDPL GKYTFWEVDL KEKFSADLDQ FPLGRKFLLQ AGLKAKPKLK
RAAPTSTRTS SAKRKKVKK
