MCP_HHV8P
ID MCP_HHV8P Reviewed; 1376 AA.
AC Q2HRA7;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 29-SEP-2021, entry version 55.
DE RecName: Full=Major capsid protein {ECO:0000255|HAMAP-Rule:MF_04016};
DE Short=MCP {ECO:0000255|HAMAP-Rule:MF_04016};
GN Name=MCP {ECO:0000255|HAMAP-Rule:MF_04016}; Synonyms=ORF25;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
RN [3]
RP FUNCTION.
RX PubMed=11000237; DOI=10.1128/jvi.74.20.9646-9654.2000;
RA Wu L., Lo P., Yu X., Stoops J.K., Forghani B., Zhou Z.H.;
RT "Three-dimensional structure of the human herpesvirus 8 capsid.";
RL J. Virol. 74:9646-9654(2000).
CC -!- FUNCTION: Self-assembles to form an icosahedral capsid with a T=16
CC symmetry, about 200 nm in diameter, and consisting of 150 hexons and 12
CC pentons (total of 162 capsomers). Hexons form the edges and faces of
CC the capsid and are each composed of six MCP molecules. In contrast, one
CC penton is found at each of the 12 vertices. Eleven of the pentons are
CC MCP pentamers, while the last vertex is occupied by the portal complex.
CC The capsid is surrounded by a layer of proteinaceous material
CC designated the tegument which, in turn, is enclosed in an envelope of
CC host cell-derived lipids containing virus-encoded glycoproteins.
CC {ECO:0000255|HAMAP-Rule:MF_04016, ECO:0000269|PubMed:11000237}.
CC -!- SUBUNIT: Homomultimer. Makes the hexons and eleven out of twelve
CC pentons. Interacts with triplex proteins 1/TRX1 and 2/TRX2; adjacent
CC capsomers are linked together in groups of three by triplexes,
CC heterotrimeric complexes composed of one molecule of TRX1 and two
CC molecules of TRX2. Interacts with scaffold protein; this interaction
CC allows efficient MCP transport to the host nucleus. Interacts with
CC capsid vertex component 2/CVC2. Interacts with the small capsomere-
CC interacting protein/SCP. {ECO:0000255|HAMAP-Rule:MF_04016}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04016}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04016}.
CC -!- SIMILARITY: Belongs to the herpesviridae major capsid protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04016}.
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DR EMBL; AF148805; ABD28876.1; -; Genomic_DNA.
DR RefSeq; YP_001129378.1; NC_009333.1.
DR PDB; 6PPB; EM; 4.30 A; S/T/W/X=1-1376.
DR PDB; 6PPD; EM; 3.70 A; 4/S/T/W/X=1-1376.
DR PDB; 6PPH; EM; 3.80 A; 4/S/T/W/X=1-1376.
DR PDBsum; 6PPB; -.
DR PDBsum; 6PPD; -.
DR PDBsum; 6PPH; -.
DR SMR; Q2HRA7; -.
DR BioGRID; 1776955; 1.
DR PRIDE; Q2HRA7; -.
DR DNASU; 4961452; -.
DR GeneID; 4961452; -.
DR KEGG; vg:4961452; -.
DR Proteomes; UP000000942; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0039622; C:T=16 icosahedral viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04016; HSV_MCP; 1.
DR InterPro; IPR000912; Herpes_MCP.
DR InterPro; IPR023233; Herpes_MCP_upper_sf.
DR Pfam; PF03122; Herpes_MCP; 1.
DR PRINTS; PR00235; HSVCAPSIDMCP.
DR SUPFAM; SSF103417; SSF103417; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Host nucleus; Reference proteome;
KW T=16 icosahedral capsid protein; Virion.
FT CHAIN 1..1376
FT /note="Major capsid protein"
FT /id="PRO_0000423760"
SQ SEQUENCE 1376 AA; 153420 MW; 413E0CD4A7BB98D2 CRC64;
MEATLEQRPF PYLATEANLL TQIKESAADG LFKSFQLLLG KDAREGSVRF EALLGVYTNV
VEFVKFLETA LAAACVNTEF KDLRRMIDGK IQFKISMPTI AHGDGRRPNK QRQYIVMKAC
NKHHIGAEIE LAAADIELLF AEKETPLDFT EYAGAIKTIT SALQFGMDAL ERGLVDTVLA
VKLRHAPPVF ILKTLGDPVY SERGLKKAVK SDMVSMFKAH LIEHSFFLDK AELMTRGKQY
VLTMLSDMLA AVCEDTVFKG VSTYTTASGQ QVAGVLETTD SVMRRLMNLL GQVESAMSGP
AAYASYVVRG ANLVTAVSYG RAMRNFEQFM ARIVDHPNAL PSVEGDKAAL ADGHDEIQRT
RIAASLVKIG DKFVAIESLQ RMYNETQFPC PLNRRIQYTY FFPVGLHLPV PRYSTSVSVR
GVESPAIQST ETWVVNKNNV PLCFGYQNAL KSICHPRMHN PTQSAQALNQ AFPDPDGGHG
YGLRYEQTPN MNLFRTFHQY YMGKNVAFVP DVAQKALVTT EDLLHPTSHR LLRLEVHPFF
DFFVHPCPGA RGSYRATHRT MVGNIPQPLA PREFQESRGA QFDAVTNMTH VIDQLTIDVI
QETAFDPAYP LFCYVIEAMI HGQEEKFVMN MPLIALVIQT YWVNSGKLAF VNSYHMVRFI
CTHMGNGSIP KEAHGHYRKI LGELIALEQA LLKLAGHETV GRTPITHLVS ALLDPHLLPP
FAYHDVFTDL MQKSSRQPII KIGDQNYDNP QNRATFINLR GRMEDLVNNL VNIYQTRVNE
DHDERHVLDV APLDENDYNP VLEKLFYYVL MPVCSNGHMC GMGVDYQNVA LTLTYNGPVF
ADVVNAQDDI LLHLENGTLK DILQAGDIRP TVDMIRVLCT SFLTCPFVTQ AARVITKRDP
AQSFATHEYG KDVAQTVLVN GFGAFAVADR SREAAETMFY PVPFNKLYAD PLVAATLHPL
LANYVTRLPN QRNAVVFNVP SNLMAEYEEW HKSPVAAYAA SCQATPGAIS AMVSMHQKLS
APSFICQAKH RMHPGFAMTV VRTDEVLAEH ILYCSRASTS MFVGLPSVVR REVRSDAVTF
EITHEIASLH TALGYSSVIA PAHVAAITTD MGVHCQDLFM IFPGDAYQDR QLHDYIKMKA
GVQTGSPGNR MDHVGYTAGV PRCENLPGLS HGQLATCEII PTPVTSDVAY FQTPSNPRGR
AACVVSCDAY SNESAERLLY DHSIPDPAYE CRSTNNPWAS QRGSLGDVLY NITFRQTALP
GMYSPCRQFF HKEDIMRYNR GLYTLVNEYS ARLAGAPATS TTDLQYVVVN GTDVFLDQPC
HMLQEAYPTL AASHRVMLDE YMSNKQTHAP VHMGQYLIEE VAPMKRLLKL GNKVVY
