Syna
entrez
214292
canonical
uniprot
Q5G5D5
canonical
ensembl
ENSMUSG00000085957
resolver
ensp
ENSMUSP00000116437
resolver
enst
ENSMUST00000149604
resolver
genesymbol
Syna
resolver
uniprot_entry
SYNA_MOUSE
resolver
amino_acid_sequence
MVRPWVFCLLLFPCSSAYSDSWMPLVNLTQHLLQEANSSFSSNCWVCLSIQTQRSLAMPAPLRTWTETPMKLRIMYSARTLSGPYPITDLERRLQNFQPLTPHSSFVNPDQRAIAFLQITSVTGILPILSRITSVRYPDDHVYESAQRPIWGSLSTQTILTSQAPLCISRFFKNSNHATFVGKLPASLCNHTFQLSPSANHQSIDLSSSYAFAPLMAMPGSKWRNPLRFSGPPSLNSGMPHYSCPIDDIHCHTYPTTPWRSCPSFPASTCYNLTLFEPDNSSHPITLSVDTTYFKIKLQGHKDPYPLFQYQPLMGAALSGQYSIWEYEPTVKKNGGITPNIFSHLVSLTYSFCLNSSGVFFLCGNSTYVCLPANWSGVCTLVFQYPDIELLPNNQTISVPLFATVPSSVPASRRKRALPLLPLLAGLGIASALGLGIAGITTSTVYFQQLSKALSDSLDEIATSIISLQDQIDSLAGVVLQNRRALDLIVAERGGTCLFLQEECCFYINQSGVVRHAARKLRERASELGTSSSSWIQWLGLGPWLPSWLTSLMAPILFILVLLVFRPCLLNCLTHSVSRRMSSFIHTTTEGHVDKILLLRESQYKRLPQEPPEEDAV
uniprot
proteins
function
FUNCTION: This endogenous retroviral envelope protein has retained its original fusogenic properties (PubMed:15644441, PubMed:17762178, PubMed:18077339, PubMed:19564597, PubMed:27589388). Together with Synb, participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis (PubMed:19564597). Syna is essential for placental development and is specifically required for formation of syncytiotrophoblast layer I (SynT-I) (PubMed:19564597). Promotes muscle myoblast fusion (PubMed:27589388). Does not have immunosuppressive activity (PubMed:18077339). {ECO:0000269|PubMed:15644441, ECO:0000269|PubMed:17762178, ECO:0000269|PubMed:18077339, ECO:0000269|PubMed:19564597, ECO:0000269|PubMed:27589388}.
uniprot
proteins
mass_dalton
68657
uniprot
proteins
mutagenesis
MUTAGEN 493; /note="R->K: No effect on fusogenic activity. Confers immunosuppressive activity not found in the wild type protein."; /evidence="ECO:0000269|PubMed:18077339
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000250|UniProtKB:Q9UQF0}.; 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:0000250|UniProtKB:Q9UQF0}.
uniprot
proteins
protein_family
Gamma type-C retroviral envelope protein family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15644441
uniprot
proteins
pubmed
17105734
uniprot
proteins
pubmed
17762178
uniprot
proteins
pubmed
18077339
uniprot
proteins
pubmed
18448564
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19564597
uniprot
proteins
pubmed
22032925
uniprot
proteins
pubmed
27589388
uniprot
proteins
sequence_length
617
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane {ECO:0000305|PubMed:17762178}; Single-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Surface protein]: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=The surface protein is not anchored to the membrane, but localizes to the extracellular surface through its binding to TM. {ECO:0000250|UniProtKB:Q9UQF0}.
uniprot
proteins
transmembrane_region
TRANSMEM 545..565; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins