VP2_ROTS1
ID VP2_ROTS1 Reviewed; 881 AA.
AC P22672;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 02-JUN-2021, entry version 83.
DE RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04127};
OS Rotavirus A (strain RVA/SA11-Both/G3P5B[2]) (RV-A) (Simian Agent 11 (strain
OS Both)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=37137;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2162107; DOI=10.1016/0042-6822(90)90487-c;
RA Mitchell D.B., Both G.W.;
RT "Completion of the genomic sequence of the simian rotavirus SA11:
RT nucleotide sequences of segments 1, 2, and 3.";
RL Virology 177:324-331(1990).
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. Interacts with a VP1-VP3 complex. Interacts with
CC the intermediate capsid protein VP6. Interacts with NSP5. Interacts
CC (via N-terminus) with NSP2. {ECO:0000255|HAMAP-Rule:MF_04127}.
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. It is necessary for encapsidation of
CC VP1 and VP3. The N-termini of 10 VP2 molecules form a cylindrical hub
CC underneath each 5-fold axis of the inner capsid. {ECO:0000255|HAMAP-
CC Rule:MF_04127}.
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; X16831; CAA34733.1; -; Genomic_RNA.
DR PIR; B35321; P2XRSR.
DR SMR; P22672; -.
DR Proteomes; UP000007180; 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 3: Inferred from homology;
KW Capsid protein; Inner capsid protein; Reference proteome; Repeat;
KW RNA-binding; T=2 icosahedral capsid protein; Ubl conjugation; Virion.
FT CHAIN 1..881
FT /note="Inner capsid protein VP2"
FT /id="PRO_0000149535"
FT REGION 1..82
FT /note="5-fold hub; involved in the encapsidation of VP1 and
FT VP3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..415
FT /note="Hydrophobic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT REGION 423..443
FT /note="Hydrophobic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 221
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT SITE 225
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT SITE 229
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT SITE 840
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT SITE 842
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
SQ SEQUENCE 881 AA; 102697 MW; 984AB341AD2F0B75 CRC64;
MAYRKRGARR ETNLKQDERM QEKEDSKNIN NDSPKSQLSE KVLSKKEEII TDNQEEVKIS
DEVKKSNKEE SKQLLEVLKT KEEHQKEVQY EILQKTIPTF EPKESILKKL EDIKPEQAKK
QTKLFRIFEP KQLPIYRANG ERELRNRWYW KLKRDTLPDG DYDVREYFLN LYDQVLMEMP
DYLLLKDMAV ENKNSRDAGK VVDSETAAIC DAIFQDEEPK AVRRFIAEMR QRVQADRNVV
NYPSILHPID HAFNEYFLQH QLVEPLNNVY IFNYIPERIR NDVNYILNMD RNLPSTARYI
RPNLLQDRLN LHDNFESLWD TITTSNYILA RSVVPDLKEL VSTEAQIQKM SQDLQLEALT
IQSETQFLTG INSQAANDCF KTLIAAMLSQ RTMSLDFVTT NYMSLISGMW LLTVIPNDMF
IRESLVACQL AIINTIVYPA FGMQRMHYRN GDPQTPFQIA EQQIQNFQVA NWLHFVNYNQ
FRQVVIDGVL NQVLNDNIRN GHVVNQLMEA LMQLSRQQFP TMPVDYKRSI QRGIFLLSNR
LGQLVDLTRL LSYINETLMA CITMNMQHVQ TLTTEKLQLT SVTSLCMLIG NATVIPSPQT
LFHYYNVNVN FHSNYNERIN DAVAIITAAN RLNLYQKKMK SIVEDFLKRL QIFDVARVPD
DQMYRLRDRL RLLPVEIRRL DIFNLIAMNM EQIERASDKI AQGVIIAYRD MQLERDEMYG
YVNIARNLDG FQQINLEELM RSGDYAQITN MLLNNQPVAL VGALPFITDS SVISLIAKLD
ATVFAQIVKL RKVDTLKPIL YKINSDSNDF YLVANYDWIP TSTTKVYKQV PQQFDFRASM
HMLTSNLTFT VYSDLLAFVS ADTVEPINAV AFDNMRIMNE L
