ENK19_HUMAN
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 25-MAY-2022, entry version 97.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10516026; DOI=10.1128/jvi.73.11.9187-9195.1999;
RA Toenjes R.R., Czauderna F., Kurth R.;
RT "Genome wide screening, cloning, chromosomal assignment and expression of
RT 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; DOI=10.1128/jvi.71.4.2747-2756.1997;
RA Toenjes R.R., Limbach C., Loewer R., Kurth R.;
RT "Expression of human endogenous retrovirus type K envelope glycoprotein in
RT insect and mammalian cells.";
RL J. Virol. 71:2747-2756(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-206.
RX PubMed=9533039; DOI=10.1159/000134709;
RA Mayer J., Meese E.U., Mueller-Lantzsch N.;
RT "Chromosomal assignment of human endogenous retrovirus K (HERV-K) env open
RT 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 envelopes
RT identifies syncytin 2, a gene conserved on primate 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., 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 19 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: ERVK-19 has a type 2 genome. The HERV-K(HML-2) family
CC contains type 1 and type 2 genomes depending on the absence or presence
CC of 292 nucleotides at the 5'-end of the env gene resulting in Env
CC proteins of distinct sizes. Despite their overall retroviral envelope
CC structure HERV-K(HML-2) type 1 envelope proteins lack a predictable
CC signal sequence. Subgenomic RNA transcripts coding for full-length
CC envelope 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA76883.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y17833; CAA76883.1; ALT_INIT; Genomic_DNA.
DR EMBL; X92887; CAA63481.1; -; Genomic_DNA.
DR EMBL; AF023261; AAC16971.1; -; Genomic_DNA.
DR AlphaFoldDB; O71037; -.
DR IntAct; O71037; 1.
DR iPTMnet; O71037; -.
DR PhosphoSitePlus; O71037; -.
DR BioMuta; HGNC:39026; -.
DR jPOST; O71037; -.
DR MassIVE; O71037; -.
DR PRIDE; O71037; -.
DR GeneCards; ERVK-19; -.
DR HGNC; HGNC:39026; ERVK-19.
DR neXtProt; NX_O71037; -.
DR PhylomeDB; O71037; -.
DR Pharos; O71037; 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 19 Env
FT polyprotein"
FT /id="PRO_0000008503"
FT CHAIN 90..465
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008504"
FT CHAIN 466..699
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008505"
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; 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
