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CAPSP_ADES1
ID   CAPSP_ADES1             Reviewed;         450 AA.
AC   A9CB90;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   23-FEB-2022, entry version 36.
DE   RecName: Full=Penton protein {ECO:0000255|HAMAP-Rule:MF_04052};
DE            Short=CP-P {ECO:0000255|HAMAP-Rule:MF_04052};
DE   AltName: Full=Penton base protein {ECO:0000255|HAMAP-Rule:MF_04052};
DE   AltName: Full=Protein III {ECO:0000255|HAMAP-Rule:MF_04052};
GN   Name=L2 {ECO:0000255|HAMAP-Rule:MF_04052};
OS   Snake adenovirus serotype 1 (SnAdV-1).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Atadenovirus.
OX   NCBI_TaxID=189830;
OH   NCBI_TaxID=94885; Pantherophis guttatus (Corn snake) (Elaphe guttata).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12237421; DOI=10.1099/0022-1317-83-10-2403;
RA   Farkas S.L., Benko M., Elo P.T., Ursu K., Dan A., Ahne W., Harrach B.;
RT   "Genetic analysis of an adenovirus isolated from corn snake (Elaphe
RT   guttata) implies common origin with the members of the proposed new genus
RT   Atadenovirus.";
RL   J. Gen. Virol. 83:2403-2410(2002).
CC   -!- FUNCTION: Major capsid protein that self-associates to form penton base
CC       pentamers, each in the shape of a pentagon, situated at the 12 vertices
CC       of the pseudo T=25 capsid. Involved in virus secondary attachment to
CC       host cell after initial attachment by the fiber protein, and in
CC       endocytosis of virions. As the virus enters the host cell, penton
CC       proteins are shed concomitant with virion acidification in the
CC       endosome. {ECO:0000255|HAMAP-Rule:MF_04052}.
CC   -!- SUBUNIT: Interacts with the fiber protein (via N-terminal tail region).
CC       Interacts with the capsid vertex protein; this interaction binds the
CC       penton base to neighboring peripentonal hexons. {ECO:0000255|HAMAP-
CC       Rule:MF_04052}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04052}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04052}. Note=Located at each vertex
CC       of the virion. {ECO:0000255|HAMAP-Rule:MF_04052}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000255|HAMAP-Rule:MF_04052}.
CC   -!- MISCELLANEOUS: All late proteins expressed from the major late promoter
CC       are produced by alternative splicing and alternative polyadenylation of
CC       the same gene giving rise to non-overlapping ORFs. A leader sequence is
CC       present in the N-terminus of all these mRNAs and is recognized by the
CC       viral shutoff protein to provide expression although conventional
CC       translation via ribosome scanning from the cap has been shut off in the
CC       host cell. {ECO:0000255|HAMAP-Rule:MF_04052}.
CC   -!- SIMILARITY: Belongs to the adenoviridae penton family.
CC       {ECO:0000255|HAMAP-Rule:MF_04052}.
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DR   EMBL; DQ106414; ABA47240.1; -; Genomic_DNA.
DR   RefSeq; YP_001552251.1; NC_009989.1.
DR   SMR; A9CB90; -.
DR   GeneID; 10973893; -.
DR   KEGG; vg:10973893; -.
DR   Proteomes; UP000136605; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0039623; C:T=25 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   HAMAP; MF_04052; ADV_CAPSP; 1.
DR   InterPro; IPR002605; Adeno_Penton_B.
DR   Pfam; PF01686; Adeno_Penton_B; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Host nucleus; Host-virus interaction; Late protein;
KW   Reference proteome; T=25 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..450
FT                   /note="Penton protein"
FT                   /id="PRO_0000425922"
SQ   SEQUENCE   450 AA;  50165 MW;  298DAE75FF4AC3ED CRC64;
     MEVYVPPPRV LAPTEGRNSI SYNPLAPLQD TTHIYMIDNK TSDIQNMNIA KDHSNFFTNI
     IQNVDVAPSD AATQDIKLDS RSRWGGQLDT ILKTNCPNVT EFFNSNSFKA LLMSDKTDPT
     NPVFTWFELT IPEENYTLSS LIDMLNEAVV ENYLEVGRQH GVEVSDIGVK FDTRNFKLGR
     DPVTTLVTPG AYTHKAFHPD VVLLPGCGVD FTNSRISNML GIRKRAPYEP GFTILYDDLQ
     GGNVPALLDL AKYPAQTVPL EVDENGLTYH VQEVAPKSWQ TLYRSWCLAY QAGGKIKTTH
     VLTVPDITGG LGQVYWSLPD TFKAPVSFTN NTTDPATLPV VGMHLFPLSS RVVYNTTAVY
     SQLVEQMTNT TKVFNRFPKN AILMQPPYDT VQFISENVPY VADHGTQPLR NSLSGVQRVT
     LTDDRRRACP YIYKTLATVT PKVLSSATLQ
 
 
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