ENK25_HUMAN
ID ENK25_HUMAN Reviewed; 661 AA.
AC P61570;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Endogenous retrovirus group K member 25 Env polyprotein;
DE AltName: Full=Envelope polyprotein;
DE AltName: Full=HERV-K_11q22.1 provirus ancestral Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE Flags: Precursor;
GN Name=ERVK-25;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hattori M., Ishii K., Toyoda A., Taylor T.D., Hong-Seog P., Fujiyama A.,
RA Yada T., Totoki Y., Watanabe H., Sakaki Y.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Retroviral envelope proteins mediate receptor recognition and
CC membrane fusion during early infection. Endogenous envelope proteins
CC may have kept, lost or modified their original function during
CC evolution (By similarity). {ECO:0000250}.
CC -!- FUNCTION: SU mediates receptor recognition. {ECO:0000250}.
CC -!- FUNCTION: TM anchors the envelope heterodimer to the viral membrane
CC through one transmembrane domain. The other hydrophobic domain, called
CC fusion peptide, mediates fusion of the viral membrane with the target
CC cell membrane (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The surface (SU) and transmembrane (TM) proteins form a
CC heterodimer. SU and TM are attached by noncovalent interactions or by a
CC labile interchain disulfide bond (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield the mature SU and TM
CC proteins. {ECO:0000250}.
CC -!- MISCELLANEOUS: Has a type 2 genome. The HERV-K(HML-2) family contains
CC type 1 and type 2 genomes depending on the absence or presence of 292
CC nucleotides at the 5'-end of the env gene resulting in Env proteins of
CC distinct sizes. Despite their overall retroviral envelope structure
CC HERV-K(HML-2) type 1 envelope proteins lack a predictable signal
CC sequence. Subgenomic RNA transcripts coding for full-length envelope
CC proteins have been detected for both type of genomes.
CC -!- SIMILARITY: Belongs to the beta type-B retroviral envelope protein
CC family. HERV class-II K(HML-2) env subfamily. {ECO:0000305}.
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DR EMBL; AP000776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P61570; -.
DR IntAct; P61570; 1.
DR iPTMnet; P61570; -.
DR PhosphoSitePlus; P61570; -.
DR BioMuta; HGNC:39039; -.
DR jPOST; P61570; -.
DR MassIVE; P61570; -.
DR PeptideAtlas; P61570; -.
DR PRIDE; P61570; -.
DR GeneCards; ERVK-25; -.
DR HGNC; HGNC:39039; ERVK-25.
DR neXtProt; NX_P61570; -.
DR PhylomeDB; P61570; -.
DR Pharos; P61570; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR CDD; cd09909; HIV-1-like_HR1-HR2; 1.
DR InterPro; IPR000328; GP41-like.
DR InterPro; IPR029104; HERV-K_env.
DR Pfam; PF00517; GP41; 1.
DR Pfam; PF13804; HERV-K_env_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cleavage on pair of basic residues; Disulfide bond; ERV;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transposable element; Viral envelope protein; Virion.
FT SIGNAL 1..89
FT /evidence="ECO:0000255"
FT CHAIN 90..661
FT /note="Endogenous retrovirus group K member 25 Env
FT polyprotein"
FT /id="PRO_0000008535"
FT CHAIN 90..465
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008536"
FT CHAIN 466..661
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008537"
FT TRANSMEM 633..653
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..486
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT COMPBIAS 10..24
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 465..466
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 661 AA; 74892 MW; 0C43729EB7390229 CRC64;
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
