ID   ENK19_HUMAN             Reviewed;         699 AA.
AC   O71037; Q69386; Q9YNA7;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   13-FEB-2019, entry version 87.
DE   RecName: Full=Endogenous retrovirus group K member 19 Env polyprotein;
DE   AltName: Full=EnvK3 protein;
DE   AltName: Full=Envelope polyprotein;
DE   AltName: Full=HERV-K(C19) envelope protein;
DE   AltName: Full=HERV-K_19q11 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-19;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10516026;
RA   Toenjes R.R., Czauderna F., Kurth R.;
RT   "Genome wide screening, cloning, chromosomal assignment and expression
RT   of full-length human endogenous retrovirus type K (HERV-K).";
RL   J. Virol. 73:9187-9195(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-514.
RX   PubMed=9060628;
RA   Toenjes R.R., Limbach C., Loewer R., Kurth R.;
RT   "Expression of human endogenous retrovirus type K envelope
RT   glycoprotein in insect and mammalian cells.";
RL   J. Virol. 71:2747-2756(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-206.
RX   PubMed=9533039;
RA   Mayer J., Meese E.U., Mueller-Lantzsch N.;
RT   "Chromosomal assignment of human endogenous retrovirus K (HERV-K) env
RT   open reading frames.";
RL   Cytogenet. Cell Genet. 79:157-161(1997).
RN   [4]
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   [5]
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
RT   envelopes identifies syncytin 2, a gene conserved on primate
RT   evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13013-13018(2003).
RN   [6]
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.,
RA   Johanning G.L.;
RT   "Quantitation of HERV-K env gene expression and splicing in human
RT   breast cancer.";
RL   Oncogene 22:1528-1535(2003).
CC   -!- FUNCTION: Retroviral envelope proteins mediate receptor
CC       recognition and membrane fusion during early infection. Endogenous
CC       envelope proteins may have kept, lost or modified their original
CC       function during evolution. This endogenous envelope protein has
CC       lost its original fusogenic properties.
CC       {ECO:0000269|PubMed:14557543}.
CC   -!- FUNCTION: SU mediates receptor recognition. {ECO:0000250}.
CC   -!- FUNCTION: TM anchors the envelope heterodimer to the viral
CC       membrane through one transmembrane domain. The other hydrophobic
CC       domain, called fusion peptide, mediates fusion of the viral
CC       membrane with the target cell membrane (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: The surface (SU) and transmembrane (TM) proteins form a
CC       heterodimer. SU and TM are attached by noncovalent interactions or
CC       by a labile interchain disulfide bond (By similarity).
CC       {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
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The
CC       surface protein is not anchored to the membrane, but localizes to
CC       the extracellular surface through its binding to TM.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endogenous retrovirus group K member 19 Env
CC       polyprotein: Virion {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield the mature SU and
CC       TM proteins. {ECO:0000250}.
CC   -!- MISCELLANEOUS: ERVK-19 has a type 2 genome. The HERV-K(HML-2)
CC       family contains type 1 and type 2 genomes depending on the absence
CC       or presence of 292 nucleotides at the 5'-end of the env gene
CC       resulting in Env proteins of distinct sizes. Despite their overall
CC       retroviral envelope structure HERV-K(HML-2) type 1 envelope
CC       proteins lack a predictable signal sequence. Subgenomic RNA
CC       transcripts coding for full-length envelope proteins have been
CC       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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA76883.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Y17833; CAA76883.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X92887; CAA63481.1; -; Genomic_DNA.
DR   EMBL; AF023261; AAC16971.1; -; Genomic_DNA.
DR   iPTMnet; O71037; -.
DR   PhosphoSitePlus; O71037; -.
DR   BioMuta; HGNC:39026; -.
DR   PRIDE; O71037; -.
DR   ProteomicsDB; 49692; -.
DR   DisGeNET; 100862685; -.
DR   GeneCards; ERVK-19; -.
DR   HGNC; HGNC:39026; ERVK-19.
DR   neXtProt; NX_O71037; -.
DR   HOVERGEN; HBG051479; -.
DR   PhylomeDB; O71037; -.
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:0019031; C:viral envelope; IEA:UniProtKB-KW.
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; Complete proteome;
KW   Disulfide bond; ERV; Glycoprotein; Membrane; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix; Transposable element;
KW   Viral envelope protein; Virion.
FT   SIGNAL        1     89       {ECO:0000255}.
FT   CHAIN        90    699       Endogenous retrovirus group K member 19
FT                                Env polyprotein.
FT                                /FTId=PRO_0000008503.
FT   CHAIN        90    465       Surface protein. {ECO:0000250}.
FT                                /FTId=PRO_0000008504.
FT   CHAIN       466    699       Transmembrane protein. {ECO:0000250}.
FT                                /FTId=PRO_0000008505.
FT   TOPO_DOM     90    632       Extracellular. {ECO:0000255}.
FT   TRANSMEM    633    653       Helical. {ECO:0000255}.
FT   TOPO_DOM    654    699       Cytoplasmic. {ECO:0000255}.
FT   REGION      466    486       Fusion peptide. {ECO:0000255}.
FT   COMPBIAS     13     20       Poly-Arg.
FT   COMPBIAS     94     99       Poly-Ala.
FT   SITE        465    466       Cleavage. {ECO:0000250}.
FT   CARBOHYD    100    100       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    128    128       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    153    153       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    274    274       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    355    355       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    372    372       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    461    461       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    507    507       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    554    554       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    566    566       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    585    585       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   699 AA;  79252 MW;  79672A0E9BE58E02 CRC64;
     MNPSEMQRKA PPRRRRHRNR APLTHKMNKM VTSEEQMKLP STKKAEPPTW AQLKKLTQLA
     TKYLENTKVT QTPESMLLAA LMIVSMVVSL PMPAGAAAAN YTYWAYVPFP PLIRAVTWMD
     NPIEVYVNDS VWVPGPTDDH CPAKPEEEGM MINISIGYRY PPICLGRAPG CLMPAVQNWL
     VEVPTVSPIS RFTYHMVSGM SLRPRVNYLQ DFSYQRSFKF RPKGKPCPKE IPKESKNTEV
     LVWEECVANS AVILQNNEFG TIIDWAPRGQ FYHNCSGQTQ SCPSAQVSPA VDSDLTESLD
     KHKHKKLQSF YPWEWGEKGI STPRPKIISP VSGPEHPELW RLTVASHHIR IWSGNQTLET
     RDRKPFYTVD LNSSVTVPLQ SCIKPPYMLV VGNIVIKPDS QTITCENCRL LTCIDSTFNW
     QHRILLVRAR EGVWIPVSMD RPWETSPSIH TLTEVLKGVL NRSKRFIFTL IAVIMGLIAV
     TATAAVAGVA LHSSVQSVNF VNDWQKNSTR LWNSQSSIDQ KLANQINDLR QTVIWMGDRL
     MSLEHRFQLQ CDWNTSDFSI TPQIYNESEH HWDMVRRHLQ GREDNLTLDI SKLKEQIFEA
     SKAHLNLVPG TEAIAGVADG LANLNPVTWV KTIGSTTIIN LILILVCLFC LLLVCRCTQQ
     LRRDSDHRER AMMTMAVLSK RKGGNVGKSK RDQIVTVSV
//