Detail Information for IndEnz0002008414
IED ID IndEnz0002008414
Enzyme Type ID protease008414
Protein Name Syncytin-1
Endogenous retrovirus group W member 1
Env-W
Envelope polyprotein gPr73
Enverin
HERV-7q Envelope protein
HERV-W envelope protein
HERV-W_7q21.2 provirus ancestral Env polyprotein
Syncytin

Cleaved into: Surface protein
SU
gp50
; Transmembrane protein
TM
gp24
Gene Name ERVW-1 ERVWE1
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MALPYHIFLFTVLLPSFTLTAPPPCRCMTSSSPYQEFLWRMQRPGNIDAPSYRSLSKGTPTFTAHTHMPRNCYHSATLCMHANTHYWTGKMINPSCPGGLGVTVCWTYFTQTGMSDGGGVQDQAREKHVKEVISQLTRVHGTSSPYKGLDLSKLHETLRTHTRLVSLFNTTLTGLHEVSAQNPTNCWICLPLNFRPYVSIPVPEQWNNFSTEINTTSVLVGPLVSNLEITHTSNLTCVKFSNTTYTTNSQCIRWVTPPTQIVCLPSGIFFVCGTSAYRCLNGSSESMCFLSFLVPPMTIYTEQDLYSYVISKPRNKRVPILPFVIGAGVLGALGTGIGGITTSTQFYYKLSQELNGDMERVADSLVTLQDQLNSLAAVVLQNRRALDLLTAERGGTCLFLGEECCYYVNQSGIVTEKVKEIRDRIQRRAEELRNTGPWGLLSQWMPWILPFLGPLAAIILLLLFGPCIFNLLVNFVSSRIEAVKLQMEPKMQSKTKIYRRPLDRPASPRSDVNDIKGTPPEEISAAQPLLRPNSAGSS
Enzyme Length 538
Uniprot Accession Number Q9UQF0
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. May induce fusion through binding of SLC1A4 and SLC1A5 (PubMed:10708449, PubMed:12050356, PubMed:23492904). {ECO:0000269|PubMed:10708449, ECO:0000269|PubMed:12050356, ECO:0000269|PubMed:23492904}.; FUNCTION: Endogenous envelope proteins may have kept, lost or modified their original function during evolution. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein (SU) mediates receptor recognition, while the transmembrane protein (TM) acts as a class I viral fusion protein. The protein may have at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of membranes.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (3); Compositional bias (1); Disulfide bond (3); Glycosylation (7); Helix (4); Motif (2); Mutagenesis (3); Natural variant (4); Region (4); Sequence conflict (6); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1)
Keywords 3D-structure;Cell membrane;Cleavage on pair of basic residues;Disulfide bond;ERV;Glycoprotein;Membrane;Reference proteome;Signal;Transmembrane;Transmembrane helix;Transposable element;Viral envelope protein;Virion
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Surface protein]: Cell membrane {ECO:0000305|PubMed:15827173}; Peripheral membrane protein {ECO:0000305|PubMed:15827173}. Note=The surface protein is not anchored to the membrane, but localizes to the extracellular surface through its binding to TM. {ECO:0000305|PubMed:15827173}.; SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Syncytin-1]: Virion {ECO:0000250}.
Modified Residue
Post Translational Modification PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. The intracytoplasmic tail cleavage by the viral protease that is required for the fusiogenic activity of some retroviruses envelope proteins seems to have been lost during evolution. {ECO:0000269|PubMed:15827173}.; PTM: The CXXC motif is highly conserved across a broad range of retroviral envelope proteins. It is thought to participate in the formation of a labile disulfide bond possibly with the CX6CC motif present in the transmembrane protein. Isomerization of the intersubunit disulfide bond to an SU intrachain disulfide bond is thought to occur upon receptor recognition in order to allow membrane fusion. {ECO:0000305|PubMed:15827173}.
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D X-ray crystallography (2)
Cross Reference PDB 5HA6; 6RX1;
Mapped Pubmed ID 11854637; 12175968; 12397062; 12724415; 12757936; 14520239; 14613893; 15109395; 15269105; 15507602; 15888734; 16004993; 16140326; 16176588; 16760410; 16820059; 16871371; 17209768; 17762178; 18077339; 18351375; 19321927; 19327884; 19407656; 19561344; 19692500; 19903052; 20100784; 20546612; 21493955; 21771862; 22109522; 22348442; 22573555; 22573740; 22971074; 22999499; 23212585; 23290063; 23457515; 23727510; 23888950; 24013223; 24204983; 24413738; 24478419; 24687878; 24812088; 24814867; 25340371; 25651508; 26230721; 26992684; 27456869; 27546366; 27714815; 28112190; 28302141; 28656540; 28928004; 30699112; 31397118; 31711961; 31883959; 32012247; 32145327; 32785870; 33317172; 33438105; 33867312; 34302264;
Motif MOTIF 186..189; /note=CXXC; /evidence=ECO:0000305; MOTIF 397..406; /note=CX6CC; /evidence=ECO:0000305
Gene Encoded By
Mass 59,866
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda