VP2_ROTRF
ID VP2_ROTRF Reviewed; 880 AA.
AC P12472; Q86225;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 02-JUN-2021, entry version 86.
DE RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04127};
OS Rotavirus A (strain RVA/Cow/France/RF/1975/G6P6[1]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10933;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2538805; DOI=10.1093/nar/17.5.2126;
RA Kumar A., Charpilienne A., Cohen J.;
RT "Nucleotide sequence of the gene encoding for the RNA binding protein (VP2)
RT of RF bovine rotavirus.";
RL Nucleic Acids Res. 17:2126-2126(1989).
RN [2]
RP RNA-BINDING, AND DOMAIN.
RX PubMed=7996135; DOI=10.1099/0022-1317-75-12-3423;
RA Labbe M., Baudoux P., Charpilienne A., Poncet D., Cohen J.;
RT "Identification of the nucleic acid binding domain of the rotavirus VP2
RT protein.";
RL J. Gen. Virol. 75:3423-3430(1994).
RN [3]
RP DOMAIN.
RX PubMed=9420216; DOI=10.1128/jvi.72.1.201-208.1998;
RA Zeng C.Q.-Y., Estes M.K., Charpilienne A., Cohen J.;
RT "The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and
RT VP3.";
RL J. Virol. 72:201-208(1998).
RN [4]
RP INTERACTION WITH THE INTERMEDIATE CAPSID PROTEIN VP6.
RX PubMed=12097594; DOI=10.1128/jvi.76.15.7822-7831.2002;
RA Charpilienne A., Lepault J., Rey F.A., Cohen J.;
RT "Identification of rotavirus VP6 residues located at the interface with VP2
RT that are essential for capsid assembly and transcriptase activity.";
RL J. Virol. 76:7822-7831(2002).
RN [5]
RP INTERACTION WITH NSP5.
RX PubMed=12525609; DOI=10.1128/jvi.77.3.1757-1763.2003;
RA Berois M., Sapin C., Erk I., Poncet D., Cohen J.;
RT "Rotavirus nonstructural protein NSP5 interacts with major core protein
RT VP2.";
RL J. Virol. 77:1757-1763(2003).
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
CC particle. It encapsidates the polymerase VP1, the capping enzyme VP3
CC and the genomic dsRNA, thereby defining the core. The innermost VP2
CC capsid and the intermediate VP6 capsid remain intact following cell
CC entry to protect the dsRNA from degradation and to prevent unfavorable
CC antiviral responses in the host cell during all the replication cycle
CC of the virus. Nascent transcripts are transcribed within the structural
CC confines of this double-layered particle (DLP) and are extruded through
CC the channels formed by VP2 N-termini. VP2 is required for the replicase
CC activity of VP1 polymerase. Probably recruits a copy of a VP1-VP3
CC complex, potentially along with a segment of plus-strand RNA, as a
CC decamer of VP2 assembles. May activate the autoinhibited VP1/RNA
CC complex to coordinate packaging and genome replication.
CC {ECO:0000255|HAMAP-Rule:MF_04127}.
CC -!- SUBUNIT: Homodecamer; each decamer is made up of two conformers of VP2,
CC called VP2A and VP2B (By similarity). Interacts with a VP1-VP3 complex
CC (By similarity). Interacts with the intermediate capsid protein VP6
CC (PubMed:12097594). Interacts with NSP5 (PubMed:12525609). Interacts
CC (via N-terminus) with NSP2 (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_04127, ECO:0000269|PubMed:12097594,
CC ECO:0000269|PubMed:12525609}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04127}.
CC Note=Inner capsid protein. Also found in spherical cytoplasmic
CC structures, called virus factories, that appear early after infection
CC and are the site of viral replication and packaging.
CC {ECO:0000255|HAMAP-Rule:MF_04127}.
CC -!- DOMAIN: The N-terminus binds RNA (PubMed:7996135). It is necessary for
CC encapsidation of VP1 and VP3 (PubMed:9420216). The N-termini of 10 VP2
CC molecules form a cylindrical hub underneath each 5-fold axis of the
CC inner capsid (By similarity). {ECO:0000255|HAMAP-Rule:MF_04127,
CC ECO:0000269|PubMed:7996135, ECO:0000269|PubMed:9420216}.
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; X14057; CAA32213.1; -; Genomic_RNA.
DR EMBL; X14057; CAA32215.1; ALT_SEQ; Genomic_RNA.
DR SMR; P12472; -.
DR Proteomes; UP000007179; Genome.
DR GO; GO:0039616; C:T=2 icosahedral viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0039625; C:viral inner capsid; IEA:UniProtKB-UniRule.
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 Capsid protein; Inner capsid protein; Repeat; RNA-binding;
KW T=2 icosahedral capsid protein; Ubl conjugation; Virion.
FT CHAIN 1..880
FT /note="Inner capsid protein VP2"
FT /id="PRO_0000149531"
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:9420216"
FT REGION 1..43
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 SITE 220
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT SITE 224
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT SITE 228
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT SITE 839
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT SITE 841
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
SQ SEQUENCE 880 AA; 102496 MW; F4AFABECA7291412 CRC64;
MAYRKRGARR EANINNNDRM QEKDDEKQDQ NNRMQLSDKV LSKKEEVVTD SQEEIKIADE
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 DPQRPFQIAE QQIQNFQVAN WLHFVNNNQF
RQVVIDGVLN QVLNDNIRNG HVINQLMEAL MQLSRQQFPT MPVDYKRSIQ RGILLLSNRL
GQLVDLTRLL AYNYETLMAC VTMNMQHVQT LTTEKLQLTS VTSLCMLIGN ATVIPSPQTL
FHYYNVNVNF HSNYNERIND AVAIITGANR LNLYQKKMKA IVEDFLKRLH IFDVARVPDD
QMYRLRDRLR LLPVEVRRLD IFNLILMNMD QIERASDKIA QGVIIAYRDM QLERDEMYGY
VNIARNLDGF QQINLEELMR TGDYAQITNM LLNNQPVALV GALPFVTDSS VISLIANVDA
TVFAQIVKLR KVDTLKPILY KINSDSNDFY LVANYDWVPT STTKVYKQVP QQFDFRNSMH
MLTSNLTFTV YSDLLAFVSA DTVEPINAVA FDNMRIMNEL
