ID   ITP_HHV2H               Reviewed;        1114 AA.
AC   P89460;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   23-FEB-2022, entry version 65.
DE   RecName: Full=Inner tegument protein {ECO:0000255|HAMAP-Rule:MF_04043};
GN   Name=UL37;
OS   Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10315;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1662697; DOI=10.1099/0022-1317-72-12-3057;
RA   McGeoch D.J., Cunningham C., McIntyre G., Dolan A.;
RT   "Comparative sequence analysis of the long repeat regions and adjoining
RT   parts of the long unique regions in the genomes of herpes simplex viruses
RT   types 1 and 2.";
RL   J. Gen. Virol. 72:3057-3075(1991).
RN   [2]
RP   SUBCELLULAR LOCATION, AND NUCLEAR EXPORT SIGNAL.
RX   PubMed=11027618; DOI=10.1006/bbrc.2000.3600;
RA   Watanabe D., Ushijima Y., Goshima F., Takakuwa H., Tomita Y., Nishiyama Y.;
RT   "Identification of nuclear export signal in UL37 protein of herpes simplex
RT   virus type 2.";
RL   Biochem. Biophys. Res. Commun. 276:1248-1254(2000).
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-
CC       Rule:MF_04043}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04043,
CC       ECO:0000269|PubMed:11027618}. Host nucleus {ECO:0000255|HAMAP-
CC       Rule:MF_04043, ECO:0000269|PubMed:11027618}. Host Golgi apparatus, host
CC       trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04043}.
CC   -!- SIMILARITY: Belongs to the herpesviridae inner tegument protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04043}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z86099; CAB06723.1; -; Genomic_DNA.
DR   SMR; P89460; -.
DR   PRIDE; P89460; -.
DR   Proteomes; UP000001874; 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; IPR005655; Herpes_UL37.
DR   InterPro; IPR034738; HSV_ITP.
DR   Pfam; PF03970; Herpes_UL37_1; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Host Golgi apparatus; Host nucleus; Reference proteome;
KW   Virion; Virion tegument.
FT   CHAIN           1..1114
FT                   /note="Inner tegument protein"
FT                   /id="PRO_0000406183"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          568..1114
FT                   /note="Interaction with large tegument protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04043"
FT   REGION          1046..1114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           263..272
FT                   /note="Nuclear export signal"
FT   COMPBIAS        28..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1064..1084
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1114 AA;  118846 MW;  1406DBD2064DDEEC CRC64;
     MSDSALQVPA PAGMTPPSAP PPNGPLQVLL GSLTNLRRPP SPSSEPAGSA DEPAFLSAAK
     LHAATAAFLL SGAAVGPAEA RACWHPLLEQ LCALHRAHGL PETALLAENL PGLLVHRMAV
     ALPETPEAAF REMDVIKDTV LAITGSDTTH ALEAAGLRTT AALGPVRVRQ CAVEWIDRWR
     TVTQSCLAMN PRTSLEALGE MSLKMSPVPL GQPGANLTTP AYSLLFPSPI VQEGLRFLAL
     VSNWVTLFSA HLQRIDDAAL TPLTRALFTL ALVDDYLTTP DRGAVVPPPL LAQFQHTVRE
     IDPAIMIPPL EATKMVRSRE EVRVSTALSR VSPRSACAPP GTLMARVRTD AAVFDPDVPF
     LSASALAIFR PAVTGLLQLG EPPSAGAQQR LLALLQQTWA LVQNSNSPSV VINTLTDAGF
     TPAHCTQYIS ALEGFLVAGV PARTPPGHGL SEIQQLFGCI ALAGANVFGL AREYGHYAGY
     VKTFRRIQGA SEHTHGRLCE AVGLSGGVLS QTLARIMGPA VPTEHLASLR RTLVGEFETA
     ERRFSAGQPS LLRETALIWL DVYGQTHWDL TPTTPATPLS ALLPVGPPSH APSVHLAAAT
     KIRFPALEGI HPNVLADPGF VPYVLALVVG DALRATCNAA YLPRPIEFAL RVLAWARDFG
     LGYLPTVEGH RTKLGALITL LEPATRAGVG PTMQMADNIE QLLRELYVIA RGAVEQLRPA
     VQLPPPQPPE VGSSLLLISM YALAARGVLQ ELAERADPLV RQLEDAIVLL RLHMRTLAAF
     FECRFESDGH RLYAVVADAH ERLGPWRPEA MGDAVSQYCG MYHDAKRALV ASLAGLRSVV
     TETTAHLGVC DELAAQVSHE GNVLAVVRRE IHGFLAIVSG IHARASKLMS GDQVPGFCYM
     SQFLARWRRL SAGYQAARAA TGPERVAEFV QELHDTWKGL QTERALVVAR FASSADQRTA
     AIQEVMAHAT EDAPPSPAAD LVVLTNRHDL GAWGDYSLGP LGQPTVVPDS VDLSPQGLAA
     TLSMDWLLIN ELLQVTDGVF RASAFRPSAG PGAPGDLEAQ DAGGSTPEPT TPGPQDTQAR
     APSTRPAGRE TVPWPNTPVE DDEMTPQETP PVHP