ID B5SNS2_ADE41 Unreviewed; 348 AA.
AC B5SNS2;
DT 04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Core-capsid bridging protein {ECO:0000256|HAMAP-Rule:MF_04053};
DE AltName: Full=Core protein V {ECO:0000256|HAMAP-Rule:MF_04053};
GN Name=L2 {ECO:0000256|HAMAP-Rule:MF_04053};
OS Human adenovirus F serotype 41 (HAdV-41) (Human adenovirus 41).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus F.
OX NCBI_TaxID=10524 {ECO:0000313|EMBL:ACH90450.1, ECO:0000313|Proteomes:UP000158144};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ACH90450.1, ECO:0000313|Proteomes:UP000158144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tak {ECO:0000313|EMBL:ACH90450.1};
RX PubMed=17250935; DOI=10.1016/j.vaccine.2006.11.025;
RA Lemiale F., Haddada H., Nabel G.J., Brough D.E., King C.R., Gall J.G.;
RT "Novel adenovirus vaccine vectors based on the enteric-tropic serotype
RT 41.";
RL Vaccine 25:2074-2084(2007).
RN [2] {ECO:0007829|PDB:6Z7N}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.77 ANGSTROMS).
RX PubMed=33523995; DOI=10.1126/sciadv.abe0974;
RA Rafie K., Lenman A., Fuchs J., Rajan A., Arnberg N., Carlson L.A.;
RT "The structure of enteric human adenovirus 41-A leading cause of diarrhea
RT in children. .";
RL Sci. Adv. 7:eabe0974-eabe0974(2021).
CC -!- FUNCTION: Associates loosely with the viral DNA to form an outer shell
CC around the nucleoprotein-DNA complex and links it with the capsid by
CC binding the endosome lysis protein. Dissociates from the viral genome
CC during entry. Might be involved in nuclear capsid assembly of the viral
CC particles through its association with NPM1/nucleophosmin.
CC {ECO:0000256|HAMAP-Rule:MF_04053}.
CC -!- SUBUNIT: Monomer. Homodimer. Exists in equilibrium between monomers and
CC dimers in solution. Interacts with the histone-like nucleoprotein; this
CC interactions bridge the virus core to the capsid. Interacts with core
CC protein X; this interactions bridge the virus core to the capsid.
CC Interacts with the endosome lysis protein VI; this interactions bridge
CC the virus core to the capsid. Interacts with the peripentonal hexons.
CC Interacts with host NPM1; this interaction might play a role in virus
CC assembly. {ECO:0000256|HAMAP-Rule:MF_04053}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|HAMAP-Rule:MF_04053}. Host
CC nucleus, host nucleolus {ECO:0000256|HAMAP-Rule:MF_04053}. Note=Located
CC inside the capsid (core). Present in 157 copies per virion. Localizes
CC in the nucleoli during infection, then translocates from the nucleoli
CC to the nucleoplasm as the infection progresses and is finally
CC incorporated into the viral particles. {ECO:0000256|HAMAP-
CC Rule:MF_04053}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000256|HAMAP-Rule:MF_04053}.
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:0000256|HAMAP-Rule:MF_04053}.
CC -!- MISCELLANEOUS: This protein is only encoded by mastadenoviruses, and
CC may therefore play a role in mammals tropism. {ECO:0000256|HAMAP-
CC Rule:MF_04053}.
CC -!- SIMILARITY: Belongs to the adenoviridae core-capsid bridging protein
CC family. {ECO:0000256|ARBA:ARBA00008293, ECO:0000256|HAMAP-
CC Rule:MF_04053}.
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DR EMBL; DQ315364; ACH90450.1; -; Genomic_DNA.
DR PDB; 6Z7N; EM; 3.77 A; N=1-348.
DR EMDB; EMD-11108; -.
DR SMR; B5SNS2; -.
DR Proteomes; UP000158144; Genome.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04053; ADV_CORE5; 1.
DR InterPro; IPR005608; Adeno_V.
DR Pfam; PF03910; Adeno_PV; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6Z7N};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_04053};
KW Host nucleus {ECO:0000256|HAMAP-Rule:MF_04053};
KW Late protein {ECO:0000256|HAMAP-Rule:MF_04053};
KW Viral capsid assembly {ECO:0000256|HAMAP-Rule:MF_04053};
KW Viral release from host cell {ECO:0000256|HAMAP-Rule:MF_04053};
KW Virion {ECO:0000256|HAMAP-Rule:MF_04053}.
FT REGION 286..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..318
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 39772 MW; BF63B2CC5E149BF0 CRC64;
MSKRKFKEEL LEALVPEIYG PAADVKPDIK PRALKRVKKR EKKEETGLLD DDVEFVRTFA
PRRQVQWRGR KVKRVLRPGT TVVFTPGERS ATRALKREYD EVYADEDILE QAAQQIGEFA
YGKRGRYGEV GLLLDQSNPT PSLKPATQQQ ILPVTETKRG VKRENKDELQ PTMQLMVPKR
QKLEEVLENM KVDPSVEPEV KVRPIKEIGP GLGVQTVDIQ IPVRTTPAVA MAEAMETQTD
QPAAVTTREI GLQTDPRYES VTSTRRSRGR KYTAANSILP EYALHPSITP TPGYRGTIFR
PSRPRTTRRR RTTRRRSRRI TPISVHRVTR RGRTITLPNA RYHPSILI
//
