VL1_HPV70
ID VL1_HPV70 Reviewed; 504 AA.
AC P50793;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 70.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=39457;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8815087; DOI=10.1128/jcm.34.4.802-809.1996;
RA Forslund O., Hansson B.G.;
RT "Human papillomavirus type 70 genome cloned from overlapping PCR products:
RT complete nucleotide sequence and genomic organization.";
RL J. Clin. Microbiol. 34:802-809(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8904450; DOI=10.1128/jcm.34.3.738-744.1996;
RA Longuet M., Beaudenon S., Orth G.;
RT "Two novel genital human papillomavirus (HPV) types, HPV68 and HPV70,
RT related to the potentially oncogenic HPV39.";
RL J. Clin. Microbiol. 34:738-744(1996).
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; U21941; AAC54857.1; -; Genomic_DNA.
DR EMBL; U22461; AAC54879.1; -; Genomic_DNA.
DR SMR; P50793; -.
DR PRIDE; P50793; -.
DR Proteomes; UP000007677; 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; 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..504
FT /note="Major capsid protein L1"
FT /id="PRO_0000133552"
FT REGION 474..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 175
FT /note="Interchain (with C-427)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT DISULFID 427
FT /note="Interchain (with C-175)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT CONFLICT 39
FT /note="S -> T (in Ref. 2; AAC54879)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="T -> TTV (in Ref. 2; AAC54879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 56576 MW; 0E9029B5B3F3D6C5 CRC64;
MALWRSSDNT VYLPPPSVAK VVNTDDYVTR TGIYYYAGSS RLLTVGHPYF KVPVNGGRKQ
EIPKVSAYQY RVFRVSLPDP NKFGLPDPSL YNPDTQRLVW ACIGVEIGRG QPLGVGVSGH
PLYNRLDDTE NSHFSSAVST QDSRDNVSVD YKQTQLCIIG CVPAMGEHWA KGKACKSTQQ
GDCPPLELVN TAIEDGDMID TGYGAMDFRT LQETKSEVPL DICQSVCKYP DYLQMSADVY
GDSMFFCLRK EQLFARHFWN RGGMVGDTIP SELYIKGTDI RERPGTHVYS PSPSGSMVSS
DSQLFNKPYW LHKAQGHNNG ICWHNQLFIT VVDTTRSTNF TLSACTETAI PAVYSPTKFK
EYTRHVEEYD LQFIFQLCTI TLTADVMAYI HTMNPAILDN WNIGVTPPPS ASLVDTYRYL
QSAAIACQKD APTPEKKDPY DDLKFWNVDL KEKFSTELDQ FPLGRKFLLQ VGARRRPTIG
PRKRPASAKS SSSASKHKRK RVSK