ID   ENH1_PANTR              Reviewed;         457 AA.
AC   P61559;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=ERV-H1 provirus ancestral Env polyprotein;
DE   AltName: Full=ERV-H/env62;
DE   AltName: Full=Envelope polyprotein;
DE            Short=Env protein;
DE   Contains:
DE     RecName: Full=Surface protein;
DE              Short=SU;
DE   Contains:
DE     RecName: Full=Transmembrane protein;
DE              Short=TM;
DE   Flags: Precursor;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11162811; DOI=10.1006/viro.2000.0737;
RA   de Parseval N., Casella J.-F., Gressin L., Heidmann T.;
RT   "Characterization of the three HERV-H proviruses with an open envelope
RT   reading frame encompassing the immunosuppressive domain and evolutionary
RT   history in primates.";
RL   Virology 279:558-569(2001).
CC   -!- FUNCTION: Retroviral envelope proteins mediate receptor recognition and
CC       membrane fusion during early infection. Endogenous envelope proteins
CC       may have kept, lost or modified their original function during
CC       evolution.
CC   -!- FUNCTION: SU mediates receptor recognition. {ECO:0000250}.
CC   -!- FUNCTION: TM anchors the envelope heterodimer to the viral membrane
CC       through one transmembrane domain. The other hydrophobic domain, called
CC       fusion peptide, mediates fusion of the viral membrane with the target
CC       cell membrane (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The surface (SU) and transmembrane (TM) proteins form a
CC       heterodimer. SU and TM are attached by noncovalent interactions or by a
CC       labile interchain disulfide bond (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion.
CC   -!- DOMAIN: The CKS-17 immunosuppressive domain is present in many
CC       retroviral envelope proteins. As a synthetic peptide, it inhibits
CC       immune function in vitro and in vivo (By similarity). {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield the mature SU and TM
CC       proteins. {ECO:0000250}.
CC   -!- PTM: The CXXC motif is highly conserved across a broad range of
CC       retroviral envelope proteins. It is thought to participate in the
CC       formation of a labile disulfide bond possibly with the CX6CC motif
CC       present in the transmembrane protein (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: Ortholog of the human HERV-H_2q24.3 envelope protein.
CC   -!- SIMILARITY: Belongs to the gamma type-C retroviral envelope protein
CC       family. HERV class-I H env subfamily. {ECO:0000305}.
CC   -!- CAUTION: Truncated; premature stop codon upstream of the potential
CC       transmembrane domain. {ECO:0000305}.
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DR   AlphaFoldDB; P61559; -.
DR   SMR; P61559; -.
DR   Proteomes; UP000002277; Unplaced.
DR   InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR   PANTHER; PTHR10424; PTHR10424; 1.
DR   Pfam; PF00429; TLV_coat; 2.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond; ERV; Glycoprotein;
KW   Reference proteome; Signal; Transposable element; Viral envelope protein;
KW   Virion.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..457
FT                   /note="ERV-H1 provirus ancestral Env polyprotein"
FT                   /id="PRO_0000008463"
FT   CHAIN           36..387
FT                   /note="Surface protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000008464"
FT   CHAIN           388..457
FT                   /note="Transmembrane protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000008465"
FT   REGION          388..408
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000255"
FT   MOTIF           64..67
FT                   /note="CXXC"
FT                   /evidence="ECO:0000250"
FT   SITE            387..388
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   457 AA;  49843 MW;  D6CD416F7BC1F5C5 CRC64;
     MIFAGKAPSN TSTLMKFYSL ILYSLLFSFP FLCHPLPLPS YLHHTINLTH SLLAASNPSL
     ANNCWLCISL SSSAYTAVPA LQTDRATSPV SLHLQTSFNS PHLYPPEELI YFLDRSIKTS
     PDISHQQAAA LLHTYLKHLS PYINSTPPIF GPLTTQTTIP VAAPLCISRR RPTGIPLGNL
     SPSRCSFTLH LRSPTTNITE TIGAFQLHIT DKPSINTDKL KNISSHYCLG RHLPCISLHP
     WLPSPCSSDC PPRPSSCLLI PSPENNSESL LVDTRRFLIH HENRTSPSTQ LPHQSPLQPL
     TAAALAGSLG VWIQDTPFST PSHLFTLHLQ FCLAQGLFFL CGSSNYMCLP ANWTGTCTLV
     FLTPKIQFAN GTEELPVPLM TPTRQKRVIP LIPLMFGLGL SASTIALSTG IAGISTSVMT
     FRSLSNDFSA SITDISQTLS VLQAQVDSLA AVVLQNR