SYCY1_HYLPI
ID SYCY1_HYLPI Reviewed; 538 AA.
AC P61562;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Syncytin-1;
DE AltName: Full=ERV-W1 provirus ancestral Env polyprotein;
DE AltName: Full=ERVWE1 envelope protein;
DE AltName: Full=Endogenous retrovirus group W member 1;
DE AltName: Full=Envelope polyprotein;
DE AltName: Full=Syncytin;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE Flags: Precursor;
GN Name=ERVW-1; Synonyms=ERVWE1;
OS Hylobates pileatus (Pileated gibbon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Hylobates.
OX NCBI_TaxID=9589;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14757826; DOI=10.1073/pnas.0305763101;
RA Mallet F., Bouton O., Prudhomme S., Cheynet V., Oriol G., Bonnaud B.,
RA Lucotte G., Duret L., Mandrand B.;
RT "The endogenous retroviral locus ERVWE1 is a bona fide gene involved in
RT hominoid placental physiology.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1731-1736(2004).
CC -!- FUNCTION: This endogenous retroviral envelope protein has retained its
CC original fusogenic properties and participates in trophoblast fusion
CC and the formation of a syncytium during placenta morphogenesis. May
CC recognize and induce fusion through binding of SLC1A4 and SLC1A5 (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: Endogenous envelope proteins may have kept, lost or modified
CC their original function during evolution. Retroviral envelope proteins
CC mediate receptor recognition and membrane fusion during early
CC infection. The surface protein (SU) mediates receptor recognition,
CC while the transmembrane protein (TM) acts as a class I viral fusion
CC protein. The protein may have at least 3 conformational states: pre-
CC fusion native state, pre-hairpin intermediate state, and post-fusion
CC hairpin state. During viral and target cell membrane fusion, the coiled
CC coil regions (heptad repeats) assume a trimer-of-hairpins structure,
CC positioning the fusion peptide in close proximity to the C-terminal
CC region of the ectodomain. The formation of this structure appears to
CC drive apposition and subsequent fusion of membranes (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of SU-
CC TM heterodimers attached probably by a labile interchain disulfide
CC bond. Interacts with the C-type lectin CD209/DC-SIGN (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Cell membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}. Note=The surface protein is
CC not anchored to the membrane, but localizes to the extracellular
CC surface through its binding to TM. {ECO:0000250|UniProtKB:Q9UQF0}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Syncytin-1]: Virion {ECO:0000250}.
CC -!- DOMAIN: The cytoplasmic region is essential for the fusiogenic
CC function. {ECO:0000250}.
CC -!- DOMAIN: The 17 amino acids long immunosuppressive region is present in
CC many retroviral envelope proteins. Synthetic peptides derived from this
CC relatively conserved sequence inhibit immune function in vitro and in
CC vivo (By similarity). {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC Envelope glycoproteins are synthesized as an inactive precursor that is
CC heavily N-glycosylated and processed likely by furin in the Golgi to
CC yield the mature SU and TM proteins. The cleavage site between SU and
CC TM requires the minimal sequence [KR]-X-[KR]-R (By similarity).
CC {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-W_7q21.2 envelope protein.
CC -!- MISCELLANEOUS: The genome contains a high percentage of proviral-like
CC elements, also called endogenous retroviruses (ERVs) that are the
CC genomic traces of ancient infections of the germline by exogenous
CC retroviruses. Although most of these elements are defective, some have
CC conserved a functional envelope (env) gene, most probably diverted by
CC the host for its benefit.
CC -!- SIMILARITY: Belongs to the gamma type-C retroviral envelope protein
CC family. HERV class-I W env subfamily. {ECO:0000305}.
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DR EMBL; AY101592; AAM68171.1; -; Genomic_DNA.
DR EMBL; AY101593; AAM68172.1; -; Genomic_DNA.
DR AlphaFoldDB; P61562; -.
DR SMR; P61562; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006949; P:syncytium formation; ISS:UniProtKB.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF00429; TLV_coat; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cleavage on pair of basic residues; Disulfide bond; ERV;
KW Glycoprotein; Membrane; Signal; Transmembrane; Transmembrane helix;
KW Transposable element; Viral envelope protein; Virion.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..538
FT /note="Syncytin-1"
FT /id="PRO_0000008488"
FT CHAIN 21..317
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008489"
FT CHAIN 318..538
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008490"
FT TOPO_DOM 31..443
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 320..340
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 380..396
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT REGION 465..484
FT /note="Essential for the fusiogenic function"
FT /evidence="ECO:0000250"
FT REGION 494..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 186..189
FT /note="CXXC"
FT /evidence="ECO:0000305"
FT MOTIF 397..405
FT /note="CX6CC"
FT /evidence="ECO:0000305"
FT SITE 317..318
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF0"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 186..405
FT /note="Interchain (between SU and TM chains, or C-189 with
FT C-405); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF0"
FT DISULFID 186..189
FT /evidence="ECO:0000250|UniProtKB:P23064"
FT DISULFID 397..404
FT /evidence="ECO:0000250|UniProtKB:P60508"
SQ SEQUENCE 538 AA; 60100 MW; E833A5AF7AF66BD7 CRC64;
MALPYHIFLF TVLLPSFTLT APPPCRCMTS SSPYQEFLWR TQRPGNIDAP LYRSFSKGSP
TFTAHTYMPR TCYNSATLCM HANTQYWTGK MINPSCPGGL GVTVCWTYFT HTGMSDGGGV
QDQAREKHVK EVISQLTQVH STSSPYKGLD LSKLHETLRT HTRLVSLFNT TLTGLHEVSA
QNPTNCWMCL PLDFRPYVSI PVPEQWNNFS TEINTTSVLV GPLVSNLEIT HTSNLTCVKF
SNTTDTTNSQ CIRWVTPPTR IFCLPSGIFF VCGTSAYRCL NGSSESMCFL SFLVPPMTIY
TEQDLYNYVV SKPRNKRVPI LPFVMGAGVL GALGTGIGSI TTSTQFYYKL SRELNGDMER
VADSLVTLQD QLNSLAAVVL QNRRALDLLT AERGGTCLFL GEECCYYVNQ SGIVTEKVKE
IRDRIQRRAE ELRNIGPWGL LSQWMPWILP FLGPLAAIIL LLLFGPCIFN LLVNFVSSRI
EAIKLQMEPK MESKTKNYRR SLDWPASPRS DVNDIKGIPP EEISTAQPLL RPNSAGSS
