|ENK17_HUMAN » Endogenous retrovirus group K member 25 Env polyprotein » Envelope polyprotein;|
|Hydrophobic Thickness||28.8 ± 1.8 Å|
|Tilt Angle||0 ± 1°|
|Links||UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC|
|TM Segments||636-657 (635-658)|
AA: 114-283, Retro-transcribing viruses envelope glycoprotein
AA: 486-661, Retroviral envelope protein
|UniProt annotation for ENK17_HUMAN » Endogenous retrovirus group K member 25 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 (By similarity). FUNCTION: SU mediates receptor recognition. FUNCTION: TM 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 (By similarity). SUBUNIT: The surface (SU) and transmembrane (TM) proteins form a heterodimer. SU and TM are attached by noncovalent interactions or by a labile interchain disulfide bond (By similarity). MISCELLANEOUS: Has a type 2 genome. The HERV-K(HML-2) family contains type 1 and type 2 genomes depending on the absence or presence of 292 nucleotides at the 5"-end of the env gene resulting in Env proteins of distinct sizes. Despite their overall retroviral envelope structure HERV-K(HML-2) type 1 envelope proteins lack a predictable signal sequence. Subgenomic RNA transcripts coding for full-length envelope proteins have been detected for both type of genomes.|
|UniProt features for ENK17_HUMAN » Endogenous retrovirus group K member 25 Env polyprotein|
SIGNAL 1 89 Potential. |
CHAIN 90 661 HERV-K_11q22.1 provirus ancestral Env polyprotein.
CHAIN 90 465 Surface protein (By similarity).
CHAIN 466 661 Transmembrane protein (By similarity).
REGION 466 486 Fusion peptide (Potential).
SITE 465 466 Cleavage (By similarity).
|Amino Acid Sequence for ENK17_HUMAN » Endogenous retrovirus group K member 25 Env polyprotein|
|MNPSEMQRKA PPRRRRHRNR APLTHKMNKM VTSEEQMKLP STKKAEPPTW AQLKKLTQLA TKYLENTKVT QTPESMLLAA LMIVSMVVSL PMPAGAAAAN YTYWAYVPFP PLIRAVTWMD NPIEVYVNDS VWVPGPIDDR CPAKPEEEGM MINISIGYRY PPICLGTAPG CLMPAVQNWL VEVPIVSPIS RFTYHMVSGM SLRPRVNYLQ DFSYQRSLKF RPKGKPCPKE IPKESKNTEV LVWEECVANS AVILQNNEFG TIIDWAPRGQ FYHNCSGQTQ SCPSAQVSPA VDSDLTESLD KHKHKKLQSF YPWEWGEKGI STPRPKIVSP VSGPEHPELW RLTVASHHIR IWSGNQTLET RDRKPFYTVD LNSSLTVPLQ SCVKPPYMLV VGNIVIKPDS QTITCENCRL LTCIDSTFNW QHRILLVRAR EGVWIPVSMD RPWEASPSIH ILTEVLKGVL NRSKRFIFTL IAVIMGLIAV TATGAVAGVA LHSSVQSVNF VNDWQKNSTR LWNSQSSIDQ KLANQINDLR QTVIWMGDRL MSLEHRFQLQ CDWNTSDFCI TPQIYNESEH HWDMVRRHLQ GREDNLTLDI SKLKEQIFKA SKAHLNLVPG TEAIAGVADG LANLNPVTWV KTIGSTTIIN LILILVCLFC LLLVCRCTQQ L|