ENK8_HUMAN
ID ENK8_HUMAN Reviewed; 699 AA.
AC Q902F8;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Endogenous retrovirus group K member 8 Env polyprotein;
DE AltName: Full=EnvK6 protein;
DE AltName: Full=Envelope polyprotein;
DE AltName: Full=HERV-K115 envelope protein;
DE AltName: Full=HERV-K_8p23.1 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-8;
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].
RX PubMed=11591322; DOI=10.1016/s0960-9822(01)00455-9;
RA Turner G., Barbulescu M., Su M., Jensen-Seaman M.I., Kidd K.K., Lenz J.;
RT "Insertional polymorphisms of full-length endogenous retroviruses in
RT humans.";
RL Curr. Biol. 11:1531-1535(2001).
RN [2]
RP CHARACTERIZATION.
RX PubMed=12970426; DOI=10.1128/jvi.77.19.10414-10422.2003;
RA de Parseval N., Lazar V., Casella J.-F., Benit L., Heidmann T.;
RT "Survey of human genes of retroviral origin: identification and
RT transcriptome of the genes with coding capacity for complete envelope
RT proteins.";
RL J. Virol. 77:10414-10422(2003).
RN [3]
RP FUNCTION.
RX PubMed=14557543; DOI=10.1073/pnas.2132646100;
RA Blaise S., de Parseval N., Benit L., Heidmann T.;
RT "Genomewide screening for fusogenic human endogenous retrovirus envelopes
RT identifies syncytin 2, a gene conserved on primate evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13013-13018(2003).
RN [4]
RP SUBGENOMIC RNA.
RX PubMed=12629516; DOI=10.1038/sj.onc.1206241;
RA Wang-Johanning F., Frost A.R., Jian B., Epp L., Lu D.W., Johanning G.L.;
RT "Quantitation of HERV-K env gene expression and splicing in human breast
RT cancer.";
RL Oncogene 22:1528-1535(2003).
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. This endogenous envelope protein has lost its original
CC fusogenic properties. {ECO:0000269|PubMed:14557543}.
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: [Transmembrane protein]: Cell membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=The surface protein is
CC not anchored to the membrane, but localizes to the extracellular
CC surface through its binding to TM. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Endogenous retrovirus group K member 8 Env
CC polyprotein]: Virion {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield the mature SU and TM
CC proteins. {ECO:0000250}.
CC -!- MISCELLANEOUS: Insertional polymorphism. Provirus present in 16% of
CC tested individuals.
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 -!- MISCELLANEOUS: Intragenic, in first intron of DEFB107 gene.
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; AY037929; AAL18259.1; -; Genomic_DNA.
DR AlphaFoldDB; Q902F8; -.
DR IntAct; Q902F8; 1.
DR iPTMnet; Q902F8; -.
DR PhosphoSitePlus; Q902F8; -.
DR BioMuta; HGNC:32302; -.
DR jPOST; Q902F8; -.
DR MassIVE; Q902F8; -.
DR PRIDE; Q902F8; -.
DR GeneCards; ERVK-8; -.
DR HGNC; HGNC:32302; ERVK-8.
DR neXtProt; NX_Q902F8; -.
DR PhylomeDB; Q902F8; -.
DR Pharos; Q902F8; 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 1: Evidence at protein level;
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..699
FT /note="Endogenous retrovirus group K member 8 Env
FT polyprotein"
FT /id="PRO_0000008512"
FT CHAIN 90..465
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008513"
FT CHAIN 466..699
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008514"
FT TOPO_DOM 90..632
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 633..653
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 654..699
FT /note="Cytoplasmic"
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 699 AA; 79168 MW; 8B62B4C46B43C334 CRC64;
MNPSEMQRKA PPRRRRHRNR APLTHKMNKM VTSEEQMKLP STKKAEPPTW AQLKKLTQLA
TKYLENTKVT QTPESMLLAA LMIVSMVVSL PMPAGAAVAN YTNWAYVPFP PLIRAVTWMD
NPIEVYVNDS VWVPGPIDDR CPAKPEEEGM MINISIGYRY PPICLGRAPG CLMPAVQNWL
VEVPTVSPIS RFTYHMVSGM SLRPRVNYLQ DFSYQRSLKF RPKGKPCPKE IPKESKNTEV
LVWEECVANS AVILQNNEFG TIIDWAPRGQ FYHNCSGQTQ SCPSAQVSPA VDSDLTESLD
KHKHKKLQSF YPWEWGEKRI STPRPKIVSP VSGPEHPELW RLTVASHHIR IWSGNQTLET
RDRKPFYTVD LNSSLTLPLQ SCVKPPYMLV VGNIVIKPDS QTITCENCRL LTCIDSTFNW
QHRILLVRAR EGVWIPVSMD RPWEASPSVH ILTEVLKGVL NRSKRFIFTL IAVIMGLIAV
TATAAVAGVA LHSSVQSVNF VNDGQKNSTR LWNSQSSIDQ KLANQINDLR QTVIWMGDRL
MSLEHRFQLQ CDWNTSDFCI TPQIYNDSEH HWDMVRRHLQ GREDNLTLDI SKLKEQIFEA
SKAHLNLVPG TEAIAGVADG LANLNPVTWV KTIGSTTIIN LILILVCLFC LLLVCRCTQQ
LRRDSDHRER AMMTMAVLSK RKGGNVGKSK RDQIVTVSV
