SYCY2_CALJA
ID SYCY2_CALJA Reviewed; 538 AA.
AC P61553;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Syncytin-2;
DE AltName: Full=ERV-FRD provirus ancestral Env polyprotein;
DE AltName: Full=Envelope polyprotein;
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=ERVFRD-1; Synonyms=ERVFRDE1;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14557543; DOI=10.1073/pnas.2132646100;
RA Blaise S., de Parseval N., Benit L., Heidmann T.;
RT "Genomewide screening for fusogenic human endogenous retrovirus envelopes
RT identifies syncytin 2, a gene conserved on primate evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13013-13018(2003).
RN [2]
RP FUNCTION.
RX PubMed=14694139; DOI=10.1128/jvi.78.2.1050-1054.2004;
RA Blaise S., Ruggieri A., Dewannieux M., Cosset F.-L., Heidmann T.;
RT "Identification of an envelope protein from the FRD family of human
RT endogenous retroviruses (HERV-FRD) conferring infectivity and functional
RT conservation among simians.";
RL J. Virol. 78:1050-1054(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. The
CC interaction with MFSD2A is apparently important for this process (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: Endogenous envelope proteins may have kept, lost or modified
CC their original function during evolution but this one can still make
CC pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity.
CC Retroviral envelope proteins mediate receptor recognition and membrane
CC fusion during early infection. The surface protein mediates receptor
CC recognition, while the transmembrane protein anchors the envelope
CC heterodimer to the viral membrane through one transmembrane domain. The
CC other hydrophobic domain, called fusion peptide, mediates fusion of the
CC viral membrane with the target cell membrane (PubMed:14694139).
CC {ECO:0000269|PubMed:14694139}.
CC -!- SUBUNIT: The surface and transmembrane proteins form a heterodimer.
CC They are attached by non-covalent interactions or by a labile
CC interchain disulfide bond (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
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 membrane protein {ECO:0000255}.
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: This envelope is not fusogenic in a human cell system.
CC -!- MISCELLANEOUS: Ortholog of the human HERV-FRD_6p24.1 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 FRD env subfamily. {ECO:0000305}.
CC -!- CAUTION: CKS-17 sequence does not match the minimal active consensus.
CC {ECO:0000305}.
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DR EMBL; AJ577600; CAE12267.1; -; Genomic_DNA.
DR AlphaFoldDB; P61553; -.
DR SMR; P61553; -.
DR STRING; 9483.ENSCJAP00000040973; -.
DR eggNOG; ENOG502SD08; Eukaryota.
DR InParanoid; P61553; -.
DR Proteomes; UP000008225; Unplaced.
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 GO; GO:0000768; P:syncytium formation by plasma membrane fusion; IDA: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; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transposable element; Viral envelope protein; Virion.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..538
FT /note="Syncytin-2"
FT /id="PRO_0000008442"
FT CHAIN 16..350
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008443"
FT CHAIN 351..538
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008444"
FT TOPO_DOM 16..478
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 500..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 354..374
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT MOTIF 43..46
FT /note="CXXC"
FT /evidence="ECO:0000305"
FT MOTIF 414..430
FT /note="CKS-17"
FT /evidence="ECO:0000250"
FT MOTIF 431..439
FT /note="CX6CC"
FT /evidence="ECO:0000305"
FT SITE 350..351
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF0"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..439
FT /note="Interchain (between SU and TM chains, or C-46 with
FT C-439); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF0"
FT DISULFID 43..46
FT /evidence="ECO:0000250|UniProtKB:P23064"
FT DISULFID 431..438
FT /evidence="ECO:0000250|UniProtKB:P60508"
SQ SEQUENCE 538 AA; 59594 MW; 82B26430EB4E69C2 CRC64;
MGLLLLLLIL TPLLAAYCHP DFRLLEKAQQ LLQSTGSPYS TNCWLCTSSS SKTPGRAYPA
SSREWTTIEA ELHISYQWDP NLKGLIRLAN SLLSKVKQDF PDIRKEPPIF GPIFTNVNLI
GIAPICVTAK RKDGTNVGTL PSTVCNVTLT VDPNQQTYQK YAHNQFHHQP RFPKPPNITF
PQGTLLDKST RFCQGRPSSC STRNFWFQPA DYNQCLQIPN LSSTAEWVLL DQTRNSLFWE
NKTKGANQSQ TPCVQVLAGM TIATSYLSTS AVSEFSGTSV TSLFSFHIST CLKTQGAFYI
CGQSIHQCLP TNWTGTCTIG YVSPDIFIAP GNLSLPIPIY GNFHFPRVKR AIHLIPLLVG
LGIVGSAGTG IAGIAKASFT YSQLSKEIAN NIEAMAKTLT TVQEQIDSLA AVVLQNRRGL
DMLTAAQGGI CLALDEKCCF WVNQSGKVQD NIRQLLNRAS TLQEQATQGW LNWEGTWKWF
SWVLPFTGPL VSLLLLLLFG PCLLNLITQF VSSRLQATKL QMKLNKRVHP RNSQESPF
