ID   MCP_ELHVK               Reviewed;        1349 AA.
AC   Q18LE0;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 35.
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};
OS   Elephantid herpesvirus 1 (isolate Asian elephant/Berlin/Kiba/1998) (EIHV-1)
OS   (Elephant endotheliotropic herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Proboscivirus.
OX   NCBI_TaxID=654902;
OH   NCBI_TaxID=9783; Elephas maximus (Indian elephant).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=99490; Loxodonta cyclotis (African forest elephant).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17507487; DOI=10.1128/jvi.00255-07;
RA   Ehlers B., Kuchler J., Yasmum N., Dural G., Voigt S., Schmidt-Chanasit J.,
RA   Jakel T., Matuschka F.R., Richter D., Essbauer S., Hughes D.J., Summers C.,
RA   Bennett M., Stewart J.P., Ulrich R.G.;
RT   "Identification of novel rodent herpesviruses, including the first
RT   gammaherpesvirus of Mus musculus.";
RL   J. Virol. 81:8091-8100(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11172087; DOI=10.1099/0022-1317-82-3-475;
RA   Ehlers B., Burkhardt S., Goltz M., Bergmann V., Ochs A., Weiler H.,
RA   Hentschke J.;
RT   "Genetic and ultrastructural characterization of a European isolate of the
RT   fatal endotheliotropic elephant herpesvirus.";
RL   J. Gen. Virol. 82:475-482(2001).
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; AF322977; ABG36579.1; -; Genomic_DNA.
DR   SMR; Q18LE0; -.
DR   PRIDE; Q18LE0; -.
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; T=16 icosahedral capsid protein; Virion.
FT   CHAIN           1..1349
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000408157"
SQ   SEQUENCE   1349 AA;  152431 MW;  ED0DE38750299E25 CRC64;
     MERDVDADIR LGSELLSKYP LDINVAALIR NYTAGELFDN LRLFFGASPE DYNLQFEAIF
     GIYCNKLEWI HFLGTALGIT SHVVRFPDAE KLSVGKIVFN VTIPRVAVPS GVPNTKNATA
     VVVKYTERMP IGISFELSFA ALEKLRLSFQ DATLLDKLIN IQAINNTLQC INNSANALQR
     GLINVVLTKL LHKAPPFFIL KYLEEPTGGI SSNNSVNRSN AVFSIKSLLP QCLFILNRVE
     NKTSILNILT EMTALVKHSI MVDSSLYTTS GGDEVSGVLV TTSNVLNVIT NMFSKLIHKA
     SVVAPVAYGE FIMSKENAVT ALAHHAIIAD FDQYVQNAQN LTAGPLKKSN FLEMGQDRST
     ISVQLMQIGD TLVALEQLDK VYRNTMTHNP LDNRLELTFH TVIGLHLPKS ISYSTMDAKV
     SLNSTIRNNV PTSIYFYDKD FTLQKVEFTD CLRTLCHPIF NDGQVCARIF TREIKDGERL
     CDGHQYVLDN DPPYPNEQHM RNFYGDAPPP MTTNQLKNEY QDLEFFKPSN KCLYTELHPM
     YDFSDVMIDE AVGQICTPRI MIGNMPQALA PSEFQEIRSM QILEISKNVY PQLYETTVGL
     ATQTLNNPEY PEICYVISVL VHGNRDAFAA AHTLIVACIN NAYTTKNMLP FIHDFDMVRL
     IANNMTDSRI LSDAHMHYKR LWSLIGFLKK LVETGGLHGH LVDDPMLCYL NALFDKRLLP
     PIIHHFPAMK QDMNVKANNR PLNIRGAELR DYDVSNLERM INVGGHVVYR DDIIEAEDLT
     VSSKIYYYCM LPALTNNHMC GASLLLNQFI PDGFFNSDFI KPEALYAAEQ TFEASVMLRR
     LLEQAGVSTA RRPELHEIMT SFFRLLLRMP ENARVLEITG PLDHAQRHCM PAFQAVHHSL
     YDGFLLVAPP LILAEYIQAI PFHKFYSDPV IAQACAPYIR EFLTRYPQCN RTDGGFPTPP
     YFSREYFNWH RTPFFKYSDT CLNTVKSMMT LACMHTKFSP VSTYLQSRAR IHPGFAVTLV
     RTDLFDVERI LYSSKSSMSV IIGDPYVYKE KTDIHTTYHI TQDISTVDMG MGYSAVTCPA
     YLRRIVSDMG ATLQDLFKVF PVASFGNDEL DEWIRTHTGG THASLFDPNT IDILTFGQVN
     VNEQPGILIG QKAVVECVVT PVTAPLHYFK IPNNPRGRAS CTLAIDPERK QDLFRVIYDH
     SIPDAQSFLS TANPWGSIWG SIGDVMYNEF HREQIGYNSR IYSPCKQFFS LDDITISNRT
     LFKITGEYNS RSKSCIDGDN ETQYVCVEGT SDMVEKPCII FQESYPLLSA SSEGLLESHI
     KPPAVRMSET HFQNYLIEEV IPITQILKK