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CAP6_ADECR
ID   CAP6_ADECR              Reviewed;         238 AA.
AC   Q96686;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   23-FEB-2022, entry version 86.
DE   RecName: Full=Pre-protein VI {ECO:0000255|HAMAP-Rule:MF_04048};
DE            Short=pVI {ECO:0000255|HAMAP-Rule:MF_04048};
DE   Contains:
DE     RecName: Full=Endosome lysis protein {ECO:0000255|HAMAP-Rule:MF_04048};
DE   Contains:
DE     RecName: Full=Protease cofactor {ECO:0000255|HAMAP-Rule:MF_04048};
DE     AltName: Full=pVI-C {ECO:0000255|HAMAP-Rule:MF_04048};
GN   Name=L3 {ECO:0000255|HAMAP-Rule:MF_04048};
OS   Canine adenovirus serotype 1 (strain RI261) (CAdV-1) (Canine adenovirus 1
OS   (strain RI261)).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Canine mastadenovirus A.
OX   NCBI_TaxID=69151;
OH   NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9129661; DOI=10.1099/0022-1317-78-4-873;
RA   Morrison M.D., Onions D.E., Nicolson L.;
RT   "Complete DNA sequence of canine adenovirus type 1.";
RL   J. Gen. Virol. 78:873-878(1997).
CC   -!- FUNCTION: [Pre-protein VI]: During virus assembly, promotes hexon
CC       trimers nuclear import through nuclear pore complexes via an importin
CC       alpha/beta-dependent mechanism. By analogy to herpesviruses capsid
CC       assembly, might act as a chaperone to promote the formation of the
CC       icosahedral capsid. {ECO:0000255|HAMAP-Rule:MF_04048}.
CC   -!- FUNCTION: [Endosome lysis protein]: Structural component of the virion
CC       that provides increased stability to the particle shell through its
CC       interaction with the core-capsid bridging protein and the hexon-linking
CC       protein VIII. Fibers shedding during virus entry into host cell allows
CC       the endosome lysis protein to be exposed as a membrane-lytic peptide.
CC       Exhibits pH-independent membrane fragmentation activity and probably
CC       mediates viral rapid escape from host endosome via organellar membrane
CC       lysis. It is not clear if it then remains partially associated with the
CC       capsid and involved in the intracellular microtubule-dependent
CC       transport of capsid to the nucleus, or if it is lost during endosomal
CC       penetration. {ECO:0000255|HAMAP-Rule:MF_04048}.
CC   -!- FUNCTION: [Protease cofactor]: Cofactor that activates the viral
CC       protease. Binds to viral protease in a 1:1 ratio. {ECO:0000255|HAMAP-
CC       Rule:MF_04048}.
CC   -!- SUBUNIT: [Pre-protein VI]: Interacts with hexon protein; this
CC       interaction allows nuclear import of hexon trimers and possibly pre-
CC       capsid assembly. Interacts (via C-terminal NLS) with importin
CC       alpha/beta. {ECO:0000255|HAMAP-Rule:MF_04048}.
CC   -!- SUBUNIT: [Endosome lysis protein]: Interacts (via PPxY motif) with host
CC       NEDD4 ubiquitine ligase; this interaction might play a role in virus
CC       intracellular transport during entry. Part of a complex composed of the
CC       core-capsid bridging protein, the endosome lysis protein VI and the
CC       hexon-linking protein VIII; these interactions bridge the virus core to
CC       the capsid. Interacts with peripentonal hexons; this interaction
CC       stabilizes the capsid by gluing two peripentonal hexons together and
CC       joining them with an adjacent group-of-nine hexon. {ECO:0000255|HAMAP-
CC       Rule:MF_04048}.
CC   -!- SUBUNIT: [Protease cofactor]: Heterodimer with the viral protease;
CC       disulfide-linked. Interacts with the viral protease.
CC       {ECO:0000255|HAMAP-Rule:MF_04048}.
CC   -!- SUBCELLULAR LOCATION: [Pre-protein VI]: Host nucleus
CC       {ECO:0000255|HAMAP-Rule:MF_04048}. Host cytoplasm {ECO:0000255|HAMAP-
CC       Rule:MF_04048}. Note=Shuttles between host cytoplasm and nucleus.
CC       {ECO:0000255|HAMAP-Rule:MF_04048}.
CC   -!- SUBCELLULAR LOCATION: [Endosome lysis protein]: Virion
CC       {ECO:0000255|HAMAP-Rule:MF_04048}. Note=Associates with the base of
CC       each peripentonal hexon on the capsid interior. Present in around 360
CC       copies per virion. {ECO:0000255|HAMAP-Rule:MF_04048}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000255|HAMAP-Rule:MF_04048}.
CC   -!- DOMAIN: N-terminal amphipathic alpha-helix domain is essential for the
CC       membrane lytic activity. {ECO:0000255|HAMAP-Rule:MF_04048}.
CC   -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC       essential for viral particle release. They can occur individually or in
CC       close proximity within structural proteins. They interacts with sorting
CC       cellular proteins of the multivesicular body (MVB) pathway. Most of
CC       these proteins are class E vacuolar protein sorting factors belonging
CC       to ESCRT-I, ESCRT-II or ESCRT-III complexes. Minor capsid protein 6
CC       contains one L domain: a PPXY motif which binds to the WW domains of
CC       HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases, like NEDD4.
CC       In adenoviruses, this motif seems to play a role in microtubule-
CC       dependent intracellular trafficking toward the nucleus during virus
CC       entry into host cell and in suppression of DAXX-mediated repression of
CC       the immediate early E1A promoter. {ECO:0000255|HAMAP-Rule:MF_04048}.
CC   -!- PTM: Ubiquitinated by Nedd4 following partial capsid disassembly; which
CC       might play a role in intracellular virus movement during entry.
CC       {ECO:0000255|HAMAP-Rule:MF_04048}.
CC   -!- PTM: [Protease cofactor]: Contains the major nuclear import and export
CC       signals. Proteolytically removed during virion maturation. The
CC       processing of the C-terminus turns the precursor into a mature viral
CC       structural protein and abrogates its ability to promote hexon import
CC       and act as a potential chaperone protein. {ECO:0000255|HAMAP-
CC       Rule:MF_04048}.
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_04048}.
CC   -!- SIMILARITY: Belongs to the adenoviridae protein VI family.
CC       {ECO:0000255|HAMAP-Rule:MF_04048}.
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DR   EMBL; Y07760; CAA69065.1; -; Genomic_DNA.
DR   RefSeq; AP_000058.1; AC_000003.1.
DR   RefSeq; NP_044197.1; NC_001734.1.
DR   GeneID; 1488930; -.
DR   KEGG; vg:1488930; -.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0046729; C:viral procapsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0039664; P:lysis of host organelle involved in viral entry into host cell; IEA:UniProtKB-UniRule.
DR   GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-UniRule.
DR   GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04048; ADV_CAP6; 1.
DR   InterPro; IPR004243; McpVI.
DR   Pfam; PF02993; MCPVI; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Cytoplasmic inwards viral transport; Disulfide bond;
KW   Host cytoplasm; Host nucleus; Host-virus interaction; Late protein;
KW   Microtubular inwards viral transport; Phosphoprotein; Ubl conjugation;
KW   Viral capsid assembly; Viral penetration into host cytoplasm;
KW   Viral penetration via lysis of host organellar membrane;
KW   Viral release from host cell; Virion; Virus entry into host cell.
FT   CHAIN           1..238
FT                   /note="Pre-protein VI"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT                   /id="PRO_0000421431"
FT   PROPEP          1..33
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT                   /id="PRO_0000036563"
FT   CHAIN           34..227
FT                   /note="Endosome lysis protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT                   /id="PRO_0000036564"
FT   CHAIN           228..238
FT                   /note="Protease cofactor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT                   /id="PRO_0000036565"
FT   REGION          34..54
FT                   /note="Amphipathic alpha-helix essential for membrane lytic
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT   REGION          36..53
FT                   /note="Involved in endosomal membrane lysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT   REGION          48..74
FT                   /note="Interaction with hexon protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT   REGION          187..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..227
FT                   /note="Interaction with hexon protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT   REGION          228..238
FT                   /note="Binds to importin alpha/beta, involved in hexon
FT                   nuclear import"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT   MOTIF           67..76
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT   MOTIF           153..156
FT                   /note="PPXY motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT   MOTIF           219..230
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT   MOTIF           233..236
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT   SITE            33..34
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT   SITE            227..228
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT   DISULFID        237
FT                   /note="Interchain (with Adenovirus protease)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
SQ   SEQUENCE   238 AA;  26337 MW;  F24503E83D14F054 CRC64;
     MDAVNFSILA PRYGSHPMMS AWSGIGTSDM NGGAFNWGGI WSGIKNFGSN VKNWGSRAWN
     SQTGKLLRQK LNDTKVREKL VEGISTGVHG ALDIANQEIA KQIERRLERQ QPLEPEVEEE
     TVETKSEAKA PLVVEMPLKR PRDEDLVITA DEPPSYEETI KTMAPLVPMT RPHPSMARPV
     IADRPTTLEL KPSDQPPPYS PQSSNMPVTA PVRSRGWQGT LANIVGVGLS NVKRRRCF
 
 
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