EFRD1_HUMAN » Syncytin-2

EFRD1_HUMAN » Syncytin-2
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
EFRD1_HUMAN » Syncytin-2 » Endogenous retrovirus group FRD member 1;Envelope polyprotein;HERV-FRD;Syncytin-2;
Hydrophobic Thickness 34.8 ± 3.0 Å
Tilt Angle 38 ± 5°
ΔGtransfer -28.3 kcal/mol
ΔGfold -17.4 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC
Topology Out
TM Segments 479-509 (477-514)
Pathways none
PDB none
OPM none
Complexes

EFRD1:EFRD1_HUMAN

Interactions

A4, Complex: A4:EFRD1, PubMed

EFRD1, Complex: Homotrimer of syncytin-2, PDBID: 1Y4M

Domains

AA: 211-512, PDBID: 1y4m, Subunit C, Seq Identity:100%, ENV polyprotein (coat polyprotein)

UniProt annotation for EFRD1_HUMAN » Syncytin-2
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. The interaction with MFSD2A is apparently important for this process (PubMed).

FUNCTION: Endogenous envelope proteins may have kept, lost or modified their original function during evolution but this one can still make pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein mediates receptor recognition, while the transmembrane protein anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane (PubMed).

SUBUNIT: The surface and transmembrane proteins form a heterodimer. They are attached by non-covalent interactions or by a labile interchain disulfide bond (By similarity). Interacts with MFSD2A.

TISSUE SPECIFICITY: Expressed at higher level in placenta. Expressed at lower level in adrenal, bone marrow, brain, breast, colon, kidney, lung, ovary, peripheral blood lymphocytes, prostate, skin, spleen, testis, thymus, thyroid, trachea.

DOMAIN: Contains the CKS-17 immunosuppressive domain present in many retroviral envelope proteins. As a synthetic peptide, it inhibits immune function in vitro and in vivo (By similarity).

MISCELLANEOUS: HERV-FRD subgenomic RNA has been observed.

MISCELLANEOUS: Ortholog in old-world and new-world monkeys, but not in prosimians.

MISCELLANEOUS: The human genome contains a high percentage of proviral-like elements, also called endogenous retroviruses (ERVs) that are the genomic traces of ancient infections of the germline by exogenous retroviruses. Although most of these elements are defective, some have conserved a functional envelope (env) gene, most probably diverted by the host for its benefit.

UniProt features for EFRD1_HUMAN » Syncytin-2
SIGNAL 1 15 Potential.
CHAIN 16 538 HERV-FRD_6p24.1 provirus ancestral Env polyprotein.
CHAIN 16 350 Surface protein (By similarity).
CHAIN 351 538 Transmembrane protein (By similarity).
REGION 354 374 Fusion peptide (By similarity).
MOTIF 43 46 CXXC (By similarity).
MOTIF 414 430 CKS-17 (By similarity).
MOTIF 431 439 CX6CC (By similarity).
SITE 350 351 Cleavage (By similarity).
DISULFID 431 438
Amino Acid Sequence for EFRD1_HUMAN » Syncytin-2
MGLLLLVLIL TPSLAAYRHP DFPLLEKAQQ LLQSTGSPYS TNCWLCTSSS TETPGTAYPA SPREWTSIEA ELHISYRWDP NLKGLMRPAN SLLSTVKQDF PDIRQKPPIF GPIFTNINLM GIAPICVMAK RKNGTNVGTL PSTVCNVTFT VDSNQQTYQT YTHNQFRHQP RFPKPPNITF PQGTLLDKSS RFCQGRPSSC STRNFWFRPA DYNQCLQISN LSSTAEWVLL DQTRNSLFWE NKTKGANQSQ TPCVQVLAGM TIATSYLGIS AVSEFFGTSL TPLFHFHIST CLKTQGAFYI CGQSIHQCLP SNWTGTCTIG YVTPDIFIAP GNLSLPIPIY GNSPLPRVRR AIHFIPLLAG LGILAGTGTG IAGITKASLT YSQLSKEIAN NIDTMAKALT TMQEQIDSLA AVVLQNRRGL DMLTAAQGGI CLALDEKCCF WVNQSGKVQD NIRQLLNQAS SLRERATQGW LNWEGTWKWF SWVLPLTGPL VSLLLLLLFG PCLLNLITQF VSSRLQAIKL QTNLSAGRHP RNIQESPF