MCP_HHV6U
ID MCP_HHV6U Reviewed; 1345 AA.
AC P17887;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 02-DEC-2020, entry version 83.
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=4L, U57;
OS Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS lymphotropic virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=10370;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2153237; DOI=10.1128/jvi.64.2.714-722.1990;
RA Littler E., Lawrence G., Liu M.-Y., Barrell B.G., Arrand J.R.;
RT "Identification, cloning, and expression of the major capsid protein gene
RT of human herpesvirus 6.";
RL J. Virol. 64:714-722(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2152817; DOI=10.1128/jvi.64.1.287-299.1990;
RA Lawrence G.L., Chee M., Craxton M.A., Gompels U.A., Honess R.W.,
RA Barrell B.G.;
RT "Human herpesvirus 6 is closely related to human cytomegalovirus.";
RL J. Virol. 64:287-299(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT genome evolution.";
RL Virology 209:29-51(1995).
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}.
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; M33515; AAA51531.1; -; Genomic_DNA.
DR EMBL; M68963; AAA65567.1; -; Genomic_DNA.
DR EMBL; X83413; CAA58391.1; -; Genomic_DNA.
DR PIR; E33560; VCBEH6.
DR RefSeq; NP_042950.1; NC_001664.2.
DR SMR; P17887; -.
DR PRIDE; P17887; -.
DR GeneID; 1487939; -.
DR KEGG; vg:1487939; -.
DR Proteomes; UP000009295; 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 3: Inferred from homology;
KW Capsid protein; Host nucleus; Reference proteome;
KW T=16 icosahedral capsid protein; Virion.
FT CHAIN 1..1345
FT /note="Major capsid protein"
FT /id="PRO_0000115705"
FT CONFLICT 344
FT /note="E -> K (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 779
FT /note="K -> E (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1345 AA; 151951 MW; F1DE8D083A85A949 CRC64;
MENWQATEIL PKIEAPLNIF NDIKTYTAEQ LFDNLRIYFG DDPSRYNISF EALLGIYCNK
IEWINFFTTP IAVAANVIRF NDVSRMTLGK VLFFIQLPRV ATGNDVTASK ETTIMVAKHS
EKHPINISFD LSAACLEHLE NTFKNTVIDQ ILNINALHTV LRSLKNSADS LERGLIHAFM
QTLLRKSPPQ FIVLTMNENK VHNKQALSRV QRSNMFQSLK NRLLTSLFFL NRNNNISYIY
RILNDMMESV TESILNDTNN YTSKENVPLD GVLLGPIGSI QKLTSILSQY ISTQVVSAPI
SYGHFIMGKE NAVTAIAYRA IMADFTQFTV NAGTEQQDTN NKSEIFDKSR AYADLKLNTL
KLGDKLVAFD HLHKVYKNTD VNDPLEQSLQ LTFFFPLGIY IPSETGFSTM ETRVKLNDTM
ENNLPTSVFF HNKDQVVQRI DFADILPSVC HPIVHDSTIV ERLMKSEPLP TGHRFSQLCQ
LKITRENPAR ILQTLYNLYE SRQEVPKNTN VLKNELNIED FYKPDNPTLP TERHPFFDLT
YIQKNRATEV LCTPRIMIGN IPLPLAPVSF HEARTNQILE HAKTNCQKYD FTLKIVTESL
TSGSYPELAY VIETLVHGNK HAFMILKQVI SQCISYWFNM KHILLFCNSF EMIMLISNHM
GDELIPGAAF AHYRNLVSLI RLVKRTISIS NLNEQLCGEP LVNFANALFD GRLFCPFVHT
MPRNDTNAKI TADDTPLTQN TVRVRNYEIS DVQRMNLIDS SVVFTDNDRP SNETTILSKI
FYFCVLPALS NNKACGAGVN VKELVLDLFY TEPFISPDDY FQENPITSDV LMSLIREGMG
PGYTVANTSC IAKQLFKSLI YINENTKILE VEVSLDPAQR HGNSVHFQSL QHILYNGLCL
ISPITTLRRY YQPIPFHRFF SDPGICGTMN ADIQVFLNTF PHCQRNDGGF PLPPPLALEF
YNWQRTPFSV YSAFCPNSLL SIMTLAAMHS KLSPVAIAIQ SKNKIHPGFA ATLVRTDNFD
VECLLYSSRA ATSIILDDPT VTAEAKDIAT TYNFTQHLSF VDMGLGFSST TATANLKRIK
SDMGSKIQNL FSAFPIHAFT NADINTWIRH HVGIEKPNPS ESEALNIITF GGINKNPPSI
LLHGQQAICE VILTPVTTNI NFFKSPHNPR GRESCMMGTD PHNEEAARKA LYDHTQTDSD
TFAATTNPWA SLPGSLGDIL YNTAHREQLC YNPKTYSPNA QFFTESDILK TNKMMYKVIS
EYCMKSNSCL NSDSEIQYSC SEGTDSFVSR PCQFLQNALP LHCSSNQALL ESRSKTGNTQ
ISETHYCNYA IGETIPFQLI IESSI