ID   ITP_EBVB9               Reviewed;        1239 AA.
AC   P03189; Q777G3;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   23-FEB-2022, entry version 77.
DE   RecName: Full=Inner tegument protein {ECO:0000255|HAMAP-Rule:MF_04043};
GN   ORFNames=BOLF1;
OS   Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=10377;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6087149; DOI=10.1038/310207a0;
RA   Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA   Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA   Tuffnell P.S., Barrell B.G.;
RT   "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL   Nature 310:207-211(1984).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15534216; DOI=10.1073/pnas.0407320101;
RA   Johannsen E., Luftig M., Chase M.R., Weicksel S., Cahir-McFarland E.,
RA   Illanes D., Sarracino D., Kieff E.;
RT   "Proteins of purified Epstein-Barr virus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:16286-16291(2004).
CC   -!- FUNCTION: Plays an essential role in cytoplasmic secondary envelopment
CC       during viral egress. Interacts with the capsid via the large tegument
CC       protein/LTP and participates in its transport to the host trans-Golgi
CC       network (TGN) where secondary envelopment occurs. Modulates
CC       tegumentation and capsid accumulation at the viral assembly complex.
CC       {ECO:0000255|HAMAP-Rule:MF_04043}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with the large tegument protein/LTP
CC       (via N-terminus). {ECO:0000255|HAMAP-Rule:MF_04043}.
CC   -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000255|HAMAP-Rule:MF_04043,
CC       ECO:0000269|PubMed:15534216}. Host cytoplasm {ECO:0000255|HAMAP-
CC       Rule:MF_04043}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04043}. Host
CC       Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-
CC       Rule:MF_04043}.
CC   -!- SIMILARITY: Belongs to the herpesviridae inner tegument protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04043}.
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DR   EMBL; V01555; CAA24841.1; -; Genomic_DNA.
DR   EMBL; AJ507799; CAD53403.1; -; Genomic_DNA.
DR   PIR; A43041; QQBE10.
DR   RefSeq; YP_401653.1; NC_007605.1.
DR   PRIDE; P03189; -.
DR   DNASU; 3783723; -.
DR   GeneID; 3783723; -.
DR   KEGG; vg:3783723; -.
DR   Proteomes; UP000153037; Genome.
DR   GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0039701; P:microtubule-dependent intracellular transport of viral material towards cell periphery; IEA:UniProtKB-UniRule.
DR   GO; GO:0019068; P:virion assembly; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04043; HSV_ITP; 1.
DR   InterPro; IPR007611; Herpes_U30.
DR   InterPro; IPR034738; HSV_ITP.
DR   Pfam; PF04523; Herpes_U30; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Host Golgi apparatus; Host nucleus; Reference proteome;
KW   Virion; Virion tegument.
FT   CHAIN           1..1239
FT                   /note="Inner tegument protein"
FT                   /id="PRO_0000116051"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          618..1239
FT                   /note="Interaction with large tegument protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04043"
FT   REGION          672..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1090..1239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1149..1164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1239 AA;  132749 MW;  6C5DBFC55F2FF729 CRC64;
     MASAMESDSS GGSGGADAQP PLAEVDGGLA RVTRQLLLSG DDPAARLRAL MPLELGIFGL
     GDLAQPVLVR DFLNTLTLMS GHAYPAAVLR HHAYYLLRAA SFSRRSFGLG HLEAALDVLA
     SSLPPTTASP ATDDPLDGSR LIAETRALAA AYRRIIEEGS GEVLAVSGPT ATFAFVEELV
     ADTYLARWDA FPREGLSFYA FNAAKTTLGR WLVTVYAETN RYPWAAAGQG QPTAADIKAM
     AVELVEHSGG GAGGGEGEES GGGLFHRPES LSSVVASLPL ARRRAVEILG VYAEASGGQT
     PPVAAVPVLA FDAARLRLLE PSGALFYDYV YEALLWDQTY GVPDSVIEAF LAGMAAEMEA
     LAARVQEAAG SRASFSPAAI EQVATVLLSA GLNETVAGDY AMMLASVPRV SRSRWRWLEA
     TAALLESLSG FALHFFRLLP TASPTSRFAR VARAAYLRAE AEAVDRRARR TSGPSTPAAA
     PAATAVGVGA AADPWDAVTP LRIFIVPPPA AEYEQVAGDL SSELLRSLLW VRYSRLWQAP
     APAPALPCKP PLLPGEQGRR QWTAAVAAAP RTDVEAYCRS LRAGQTARAD PAYVHSPFFP
     AAFIEFQIWP ALRRVLSNEL PKTRSLAALR WLVSFGSDLA LPSPELTRAR RPLELIYATV
     WEIYDGAPPM PGESPQAVGL RPLNLEGEGK AGDAGAEGAE DEEGGGPWGL SSHDAVLRIM
     DAVREVSGII SETISASERA AEAPPLAWPT SLFSLLFTLR YSTTAESLGL ATRRFLVSGE
     TLSEDISRLT GAAWRLCSRP LLYDAETGRV QIPLATEEEE EAVVAVKEKS VSSSPRHYST
     DLQTLKSVVE GIQDVCRDAA ARWALATADT ATLRRRLLVP ALRESRGIAD HPLWAHTSEP
     LRPDLEELNE RVEHALELGY SLTGALRRSV AYRFRDYTFA RLFQPPAIDA ERAEAIVRRD
     ARPPPVFIPA PRRLPQGGAD TPPPLSMDDI LYLGKSICKA LVDVLDHHPA APETTPIKTY
     TPAMDLNPEQ ITVTPRSPSV LAAFARTARV QTHHLVPALT DDSPSPVGQT PPPFRILPAK
     KLAAILLGNG RNASKRRASR DLSPPPHGRW RAVLDSSPFS FSSSDFSDQD EGEGGEADLR
     GVPGGGGEGA YEEDRERPSD IDTAARAQKV ETSCPRRRSP RTTPSPSRRA SGGGGPDRGE
     AEAHTYPPYL SAAAAASRVR PRTRRGATRR PPRPTAEDE