VP2_ROTBU
ID VP2_ROTBU Reviewed; 881 AA.
AC P17462;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 29-SEP-2021, entry version 78.
DE RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04127};
OS Rotavirus A (strain RVA/Cow/United Kingdom/UK/1975/G6P7[5]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10934;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2165258; DOI=10.1093/nar/18.13.4015;
RA Tian Y., Tarlow O., McCrae M.A.;
RT "Nucleotide sequence of gene 2 of the UK tissue culture adapted strain of
RT bovine rotavirus.";
RL Nucleic Acids Res. 18:4015-4015(1990).
RN [2] {ECO:0007744|PDB:3KZ4}
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS), FUNCTION, SUBUNIT, INTERACTION WITH
RP THE INTERMEDIATE CAPSID PROTEIN VP6, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=20122940; DOI=10.1016/j.jmb.2010.01.055;
RA McClain B., Settembre E., Temple B.R., Bellamy A.R., Harrison S.C.;
RT "X-ray crystal structure of the rotavirus inner capsid particle at 3.8 A
RT resolution.";
RL J. Mol. Biol. 397:587-599(2010).
CC -!- FUNCTION: Inner capsid protein that self-assembles to form an
CC icosahedral capsid with a T=2 symmetry, which consists of 120 copies of
CC VP2, with channels at each of its five-fold vertices. This capsid
CC constitutes the innermost concentric layer of the viral mature particle
CC (PubMed:20122940). It encapsidates the polymerase VP1, the capping
CC enzyme VP3 and the genomic dsRNA, thereby defining the core
CC (PubMed:20122940). The innermost VP2 capsid and the intermediate VP6
CC capsid remain intact following cell entry to protect the dsRNA from
CC degradation and to prevent unfavorable antiviral responses in the host
CC cell during all the replication cycle of the virus (PubMed:20122940).
CC Nascent transcripts are transcribed within the structural confines of
CC this double-layered particle (DLP) and are extruded through the
CC channels formed by VP2 N-termini (PubMed:20122940). VP2 is required for
CC the replicase activity of VP1 polymerase (By similarity). Probably
CC recruits a copy of a VP1-VP3 complex, potentially along with a segment
CC of plus-strand RNA, as a decamer of VP2 assembles (PubMed:20122940).
CC May activate the autoinhibited VP1/RNA complex to coordinate packaging
CC and genome replication (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_04127, ECO:0000305|PubMed:20122940}.
CC -!- SUBUNIT: Homodecamer; each decamer is made up of two conformers of VP2,
CC called VP2A and VP2B (PubMed:20122940). Interacts with a VP1-VP3
CC complex (PubMed:20122940). Interacts with the intermediate capsid
CC protein VP6 (PubMed:20122940). Interacts with NSP5 (By similarity).
CC Interacts (via N-terminus) with NSP2 (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_04127, ECO:0000269|PubMed:20122940}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04127,
CC ECO:0000269|PubMed:20122940}. Note=Inner capsid protein. Also found in
CC spherical cytoplasmic structures, called virus factories, that appear
CC early after infection and are the site of viral replication and
CC packaging (Potential). {ECO:0000255|HAMAP-Rule:MF_04127,
CC ECO:0000269|PubMed:20122940}.
CC -!- DOMAIN: The N-terminus binds RNA (By similarity). It is necessary for
CC encapsidation of VP1 and VP3 (By similarity). The N-termini of 10 VP2
CC molecules form a cylindrical hub underneath each 5-fold axis of the
CC inner capsid (PubMed:20122940). {ECO:0000255|HAMAP-Rule:MF_04127,
CC ECO:0000269|PubMed:20122940}.
CC -!- PTM: Sumoylated with SUMO1 and SUMO2. Sumoylation of viral proteins
CC seems to have a positive role on viral replication. {ECO:0000255|HAMAP-
CC Rule:MF_04127}.
CC -!- SIMILARITY: Belongs to the rotavirus VP2 family. {ECO:0000255|HAMAP-
CC Rule:MF_04127}.
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DR EMBL; X52589; CAA36825.1; -; Genomic_RNA.
DR PDB; 3KZ4; X-ray; 3.80 A; A/B=1-881.
DR PDBsum; 3KZ4; -.
DR SMR; P17462; -.
DR Proteomes; UP000008657; Genome.
DR GO; GO:0039616; C:T=2 icosahedral viral capsid; IDA:UniProtKB.
DR GO; GO:0039625; C:viral inner capsid; IDA:UniProtKB.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04123; Rota_VP2; 1.
DR HAMAP; MF_04127; Rota_VP2_A; 1.
DR InterPro; IPR007779; Rotavirus_VP2.
DR Pfam; PF05087; Rota_VP2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Inner capsid protein; Repeat; RNA-binding;
KW T=2 icosahedral capsid protein; Ubl conjugation; Virion.
FT CHAIN 1..881
FT /note="Inner capsid protein VP2"
FT /id="PRO_0000149532"
FT REGION 1..80
FT /note="5-fold hub; involved in the encapsidation of VP1 and
FT VP3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127,
FT ECO:0000269|PubMed:20122940"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..414
FT /note="Hydrophobic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT REGION 422..442
FT /note="Hydrophobic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT COMPBIAS 16..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 220
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127,
FT ECO:0000269|PubMed:20122940"
FT SITE 224
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127,
FT ECO:0000269|PubMed:20122940"
FT SITE 228
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127,
FT ECO:0000269|PubMed:20122940"
FT SITE 840
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127,
FT ECO:0000269|PubMed:20122940"
FT SITE 842
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127,
FT ECO:0000269|PubMed:20122940"
SQ SEQUENCE 881 AA; 102488 MW; 7CFCDF653E4CF2CC CRC64;
MAYRKRGATV EADINNNDRM QEKDDEKQDQ NNRMQLSDKV LSKKEEVVTD SQEEIKIRDE
VKKSTKEESK QLLEVLKTKE EHQKEIQYEI LQKTIPTFEP KESILKKLED IKPEQAKKQT
KLFRIFEPRQ LPIYRANGEK ELRNRWYWKL KKDTLPDGDY DVREYFLNLY DQVLTEMPDY
LLLKDMAVEN KNSRDAGKVV DSETASICDA IFQDEETEGA VRRFIAEMRQ RVQADRNVVN
YPSILHPIDY AFNEYFLQHQ LVEPLNNDII FNYIPERIRN DVNYILNMDR NLPSTARYIR
PNLLQDRLNL HDNFESLWDT ITTSNYILAR SVVPDLKELV STEAQIQKMS QDLQLEALTI
QSETQFLTGI NSQAANDCFK TLIAAMLSQR TMSLDFVTTN YMSLISGMWL LTVVPNDMFI
RESLVACQLA IVNTIIYPAF GMQRMHYRNG DPQTPFQIAE QQIRKFSGSG IGWHFVNNNQ
FRQVVIDGVL NQVLNDNIRN VHVIKQLMQA LMQLSRQQFP TMPVDYKRSI QRGILLLSNR
LGQLVDLTRL LAYNYETLMA CVTMNMQHVQ TLTTEKLQLT SVTSLCMLIG NATVIPSPQT
LFHYYNVNVN FHSNYNERIN DAVAIITAAN RLNLYQKKMK AIVEDFLKRL HIFDVARVPD
DQMYRLRDRL RLLPVEVRRL DIFNLILMNM DQIERASDKI AQGVIIAYRD MQLERDEMYG
YVNIARNLDG FQQINLEELM RTGDYAQITN MLLNNQPVAL VGALPFVTDS SVISLIAKLD
ATVFAQIVKL RKVDTLKPIL YKINSDSNDF YLVANYDWVP TSTTKVYKQV PQQFDFRNSM
HMLTSNLTFT VYSDLLAFVS ADTVEPINAV AFDNMRIMNE L
