ID   UL144_HCMVO             Reviewed;         176 AA.
AC   Q68396;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 81.
DE   RecName: Full=Membrane glycoprotein UL144;
DE   AltName: Full=TNF alpha-like receptor UL144;
DE   AltName: Full=UL144 protein;
DE   Flags: Precursor;
GN   Name=UL144;
OS   Human cytomegalovirus (strain Toledo) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=311339;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8523595; DOI=10.1128/jvi.70.1.78-83.1996;
RA   Cha T.A., Tom E., Kemble G.W., Duke G.M., Mocarski E.S., Spaete R.R.;
RT   "Human cytomegalovirus clinical isolates carry at least 19 genes not found
RT   in laboratory strains.";
RL   J. Virol. 70:78-83(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Davison A.J.;
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=16932746; DOI=10.1038/sj.emboj.7601287;
RA   Poole E., King C.A., Sinclair J.H., Alcami A.;
RT   "The UL144 gene product of human cytomegalovirus activates NFkappaB via a
RT   TRAF6-dependent mechanism.";
RL   EMBO J. 25:4390-4399(2006).
RN   [4]
RP   INTERACTION WITH HUMAN TRIM23.
RX   PubMed=19176615; DOI=10.1128/jvi.02072-08;
RA   Poole E., Groves I., MacDonald A., Pang Y., Alcami A., Sinclair J.;
RT   "Identification of TRIM23 as a cofactor involved in the regulation of NF-
RT   kappaB by human cytomegalovirus.";
RL   J. Virol. 83:3581-3590(2009).
CC   -!- FUNCTION: Activates NF-kappaB in a tumor necrosis factor receptor
CC       (TNFR)-associated factor 6 (TRAF6)-dependent manner, causing the up-
CC       regulation of the chemokine CCL22. {ECO:0000269|PubMed:16932746}.
CC   -!- SUBUNIT: Interacts with host TRIM23; this interaction causes auto-
CC       ubiquitination of TRAF6, leading to NF-kappaB activation.
CC       {ECO:0000269|PubMed:19176615}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; U33331; AAA85883.1; -; Genomic_DNA.
DR   EMBL; GU937742; AAR31515.1; -; Genomic_DNA.
DR   SMR; Q68396; -.
DR   Proteomes; UP000008455; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039652; P:induction by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR   CDD; cd10582; TNFRSF14; 1.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   InterPro; IPR034031; TNFRSF14/UL144_N.
DR   Pfam; PF00020; TNFR_c6; 1.
DR   SMART; SM00208; TNFR; 2.
DR   PROSITE; PS00652; TNFR_NGFR_1; 1.
DR   PROSITE; PS50050; TNFR_NGFR_2; 1.
PE   1: Evidence at protein level;
KW   Activation of host NF-kappa-B by virus; Disulfide bond;
KW   Host-virus interaction; Membrane; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..176
FT                   /note="Membrane glycoprotein UL144"
FT                   /id="PRO_0000410894"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          22..56
FT                   /note="TNFR-Cys 1"
FT   REPEAT          58..95
FT                   /note="TNFR-Cys 2"
FT   DISULFID        23..34
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        35..48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        38..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        59..71
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        74..87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        77..95
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
SQ   SEQUENCE   176 AA;  19624 MW;  4874D6CC0B1646F5 CRC64;
     MKPLIMLICF AVILLQLGVT KVCQHNEVQL GNECCPPCGS GQRVTKVCTD YTSVTCTPCP
     NGTYVSGLYN CTDCTQCNVT QVMIRNCTST NNTVCAPKNH TYFSTPGVQH HKQRQQNHTA
     HITVKQGKSG RHTLAWLSLF IFLVGIILLI LYLIAAYRSE RCQQCCSIGK IFYRTL