EFC2_HUMAN » HERV-F(c)2_7q36.2 provirus ancestral Env polyprotein

EFC2_HUMAN » HERV-F(c)2_7q36.2 provirus ancestral Env polyprotein
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
EFC2_HUMAN » HERV-F(c)2_7q36.2 provirus ancestral Env polyprotein » Envelope polyprotein;Fc2deltaenv;
Hydrophobic Thickness 29.8 ± 2.2 Å
Tilt Angle 3 ± 5°
ΔGtransfer -15.7 kcal/mol
ΔGfold -9.2 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC
Topology Out
TM Segments 409-429 (405-430)
Pathways none
PDB none
OPM none
Complexes none
Interactions none
Domains

AA: 186-527, PDBID: 1XNL, Subunit A, Seq Identity:63%, ENV polyprotein (coat polyprotein)

UniProt annotation for EFC2_HUMAN » HERV-F(c)2_7q36.2 provirus ancestral Env polyprotein
FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties.

TISSUE SPECIFICITY: Low expression in skin and testis.

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

MISCELLANEOUS: Orthologs in Pan troglodytes (truncated), Gorilla gorilla (truncated).

UniProt features for EFC2_HUMAN » HERV-F(c)2_7q36.2 provirus ancestral Env polyprotein
CHAIN 1 527 HERV-F(c)2_7q36.2 provirus ancestral Env polyprotein.
REGION 1 411 Surface protein (By similarity).
REGION 412 527 Transmembrane protein (By similarity).
REGION 412 432 Fusion peptide (Potential).
MOTIF 280 283 CXXC (By similarity).
MOTIF 477 493 CKS-17 (By similarity).
MOTIF 494 502 CX6CC (By similarity).
SITE 411 412 Ancestral cleavage site (Potential).
DISULFID 494 501 By similarity.
Amino Acid Sequence for EFC2_HUMAN » HERV-F(c)2_7q36.2 provirus ancestral Env polyprotein
MNSPCDRLQQ FIQVLLEESW SFPSFANTLH WPENLLSYID ELVWQGSLQN FHQHEVRFDK PPLRLPLTGF SSLTENWSSR QAVSSRLVAT AASPPAGCQA PIAFLGLKFS SLGPARKNPA LCFLYDQSNS KCNTSWVKEN VGCPWHWCNI HEALIRTEKG SDPMFYVNTS TGGRDGFNGF NLQISDPWDP RWASGVDGGL YEHKTFMYPV AKIRIARTLK TTVTGLSDLA SSIQSAEKEL TSQLQPAADQ AKSSRFSWLT LISEGAQLLQ STGVQNLSHC FLCAALRRPP LVAVPLPTPF NYTINSSTPI PPVPKGQVPL FSDPIRHKFP FCYSTPNASW CNQTRMLTST PAPPRGYFWC NSTLTKVLNS TGNHTLCLPI SLIPGLTLYS QDELSHLLAW TEPRPQNKSK WAIFLPLVLG ISLASSLVAS GLGKGALTHS IQTSQDLSTH LQLAIEASAE SLDSLQRQIT TVAQVAAQNR QALDLLMAEK GRTCLFLQEE CCYYLNESGV VENSLQTLKK KKSSKRS