VL1_HPV35
ID VL1_HPV35 Reviewed; 502 AA.
AC P27232; Q90077;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 25-MAY-2022, entry version 114.
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 35.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=10587;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate 35H;
RX PubMed=8205838; DOI=10.1007/978-3-642-78487-3_2;
RA Delius H., Hofmann B.;
RT "Primer-directed sequencing of human papillomavirus types.";
RL Curr. Top. Microbiol. Immunol. 186:13-31(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1310198; DOI=10.1016/0042-6822(92)90045-q;
RA Marich J.E., Pontsler A.V., Rice S.M., McGraw K.A., Dubensky T.W.;
RT "The phylogenetic relationship and complete nucleotide sequence of human
RT papillomavirus type 35.";
RL Virology 186:770-776(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 335-367.
RX PubMed=1321168; DOI=10.1128/jcm.30.7.1716-1721.1992;
RA van den Brule A.J., Snijders P.J., Raaphorst P.M., Schrijnemakers H.F.,
RA Delius H., Gissmann L., Meijer C.J., Walboomers J.M.;
RT "General primer polymerase chain reaction in combination with sequence
RT analysis for identification of potentially novel human papillomavirus
RT genotypes in cervical lesions.";
RL J. Clin. Microbiol. 30:1716-1721(1992).
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; X74477; CAA52566.1; -; Genomic_DNA.
DR EMBL; M74117; AAA46972.1; -; Genomic_DNA.
DR EMBL; S40240; AAB22564.1; -; Genomic_DNA.
DR PIR; G40824; P1WL35.
DR PIR; S36526; S36526.
DR PDB; 2R5J; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=21-401, A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=437-472.
DR PDBsum; 2R5J; -.
DR SMR; P27232; -.
DR EvolutionaryTrace; P27232; -.
DR Proteomes; UP000007711; Genome.
DR Proteomes; UP000113298; 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..502
FT /note="Major capsid protein L1"
FT /id="PRO_0000133519"
FT REGION 479..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 175
FT /note="Interchain (with C-426)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT DISULFID 426
FT /note="Interchain (with C-175)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT CONFLICT 94..95
FT /note="AS -> CL (in Ref. 2; AAA46972)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="S -> L (in Ref. 2; AAA46972)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="G -> GNSG (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="K -> R (in Ref. 2; AAA46972)"
FT /evidence="ECO:0000305"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:2R5J"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:2R5J"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:2R5J"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:2R5J"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:2R5J"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 249..262
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:2R5J"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:2R5J"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:2R5J"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:2R5J"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 358..380
FT /evidence="ECO:0007829|PDB:2R5J"
FT HELIX 383..392
FT /evidence="ECO:0007829|PDB:2R5J"
FT HELIX 394..398
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:2R5J"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:2R5J"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:2R5J"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:2R5J"
FT HELIX 461..470
FT /evidence="ECO:0007829|PDB:2R5J"
SQ SEQUENCE 502 AA; 56149 MW; 68F6C43508F92267 CRC64;
MSLWRSNEAT VYLPPVSVSK VVSTDEYVTR TNIYYHAGSS RLLAVGHPYY AIKKQDSNKI
AVPKVSGLQY RVFRVKLPDP NKFGFPDTSF YDPASQRLVW ACTGVEVGRG QPLGVGISGH
PLLNKLDDTE NSNKYVGNSG TDNRECISMD YKQTQLCLIG CRPPIGEHWG KGTPCNANQV
KAGECPPLEL LNTVLQDGDM VDTGFGAMDF TTLQANKSDV PLDICSSICK YPDYLKMVSE
PYGDMLFFYL RREQMFVRHL FNRAGTVGET VPADLYIKGT TGTLPSTSYF PTPSGSMVTS
DAQIFNKPYW LQRAQGHNNG ICWSNQLFVT VVDTTRSTNM SVCSAVSSSD STYKNDNFKE
YLRHGEEYDL QFIFQLCKIT LTADVMTYIH SMNPSILEDW NFGLTPPPSG TLEDTYRYVT
SQAVTCQKPS APKPKDDPLK NYTFWEVDLK EKFSADLDQF PLGRKFLLQA GLKARPNFRL
GKRAAPASTS KKSSTKRRKV KS
