VL1_HPV18
ID VL1_HPV18 Reviewed; 568 AA.
AC P06794; Q84270;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 02-JUN-2021, entry version 105.
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 type 18.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=333761;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3039146; DOI=10.1016/0022-2836(87)90343-3;
RA Cole S.T., Danos O.;
RT "Nucleotide sequence and comparative analysis of the human papillomavirus
RT type 18 genome. Phylogeny of papillomaviruses and repeated structure of the
RT E6 and E7 gene products.";
RL J. Mol. Biol. 193:599-608(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 363-406.
RX PubMed=1326639; DOI=10.1128/jvi.66.10.5714-5725.1992;
RA Chan S.-Y., Bernard H.U., Ong C.K., Chan S.P., Birgit H., Delius H.;
RT "Phylogenetic analysis of 48 papillomavirus types and 28 subtypes and
RT variants: a showcase for the molecular evolution of DNA viruses.";
RL J. Virol. 66:5714-5725(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 501-568.
RX PubMed=3023691; DOI=10.1128/jvi.61.1.134-142.1987;
RA Thierry F., Heard J.-M., Dartmann K., Yaniv M.;
RT "Characterization of a transcriptional promoter of human papillomavirus 18
RT and modulation of its expression by simian virus 40 and adenovirus early
RT antigens.";
RL J. Virol. 61:134-142(1987).
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; X05015; CAA28671.1; -; Genomic_DNA.
DR EMBL; M96287; AAA47026.1; -; Genomic_DNA.
DR EMBL; M14710; AAA65508.1; -; Genomic_DNA.
DR EMBL; A06329; CAA00545.1; -; Unassigned_DNA.
DR PIR; A26251; P1WL18.
DR RefSeq; NP_040317.1; NC_001357.1.
DR PDB; 2R5I; X-ray; 3.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=82-465, A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=499-536.
DR PDB; 5W1X; X-ray; 3.37 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=82-465, A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=499-535.
DR PDBsum; 2R5I; -.
DR PDBsum; 5W1X; -.
DR SMR; P06794; -.
DR ChEMBL; CHEMBL3562174; -.
DR DNASU; 1489090; -.
DR GeneID; 1489090; -.
DR KEGG; vg:1489090; -.
DR EvolutionaryTrace; P06794; -.
DR Proteomes; UP000009109; 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..568
FT /note="Major capsid protein L1"
FT /id="PRO_0000133502"
FT REGION 537..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 236
FT /note="Interchain (with C-490)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT DISULFID 490
FT /note="Interchain (with C-236)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT CONFLICT 384
FT /note="V -> I (in Ref. 2; AAA47026)"
FT /evidence="ECO:0000305"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:2R5I"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 157..170
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:5W1X"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:2R5I"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 214..223
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:5W1X"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:2R5I"
FT STRAND 285..293
FT /evidence="ECO:0007829|PDB:5W1X"
FT HELIX 295..300
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 308..316
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:2R5I"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:5W1X"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:5W1X"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:2R5I"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:5W1X"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 389..396
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 403..412
FT /evidence="ECO:0007829|PDB:5W1X"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 422..444
FT /evidence="ECO:0007829|PDB:5W1X"
FT HELIX 447..456
FT /evidence="ECO:0007829|PDB:5W1X"
FT HELIX 458..463
FT /evidence="ECO:0007829|PDB:5W1X"
FT TURN 502..505
FT /evidence="ECO:0007829|PDB:5W1X"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:5W1X"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:5W1X"
FT HELIX 525..534
FT /evidence="ECO:0007829|PDB:5W1X"
SQ SEQUENCE 568 AA; 63624 MW; BB2B6F361177FC10 CRC64;
MCLYTRVLIL HYHLLPLYGP LYHPRPLPLH SILVYMVHII ICGHYIILFL RNVNVFPIFL
QMALWRPSDN TVYLPPPSVA RVVNTDDYVT PTSIFYHAGS SRLLTVGNPY FRVPAGGGNK
QDIPKVSAYQ YRVFRVQLPD PNKFGLPDTS IYNPETQRLV WACAGVEIGR GQPLGVGLSG
HPFYNKLDDT ESSHAATSNV SEDVRDNVSV DYKQTQLCIL GCAPAIGEHW AKGTACKSRP
LSQGDCPPLE LKNTVLEDGD MVDTGYGAMD FSTLQDTKCE VPLDICQSIC KYPDYLQMSA
DPYGDSMFFC LRREQLFARH FWNRAGTMGD TVPQSLYIKG TGMPASPGSC VYSPSPSGSI
VTSDSQLFNK PYWLHKAQGH NNGVCWHNQL FVTVVDTTPS TNLTICASTQ SPVPGQYDAT
KFKQYSRHVE EYDLQFIFQL CTITLTADVM SYIHSMNSSI LEDWNFGVPP PPTTSLVDTY
RFVQSVAITC QKDAAPAENK DPYDKLKFWN VDLKEKFSLD LDQYPLGRKF LVQAGLRRKP
TIGPRKRSAP SATTSSKPAK RVRVRARK
