ENH3_HUMAN
ID ENH3_HUMAN Reviewed; 555 AA.
AC Q9N2J8;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=HERV-H_2q24.1 provirus ancestral Env polyprotein;
DE AltName: Full=Env protein HERV-H/p59;
DE AltName: Full=Envelope polyprotein;
DE AltName: Full=HERV-H/env59;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE Flags: Precursor;
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=11162811; DOI=10.1006/viro.2000.0737;
RA de Parseval N., Casella J.-F., Gressin L., Heidmann T.;
RT "Characterization of the three HERV-H proviruses with an open envelope
RT reading frame encompassing the immunosuppressive domain and evolutionary
RT history in primates.";
RL Virology 279:558-569(2001).
RN [2]
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 [3]
RP TISSUE SPECIFICITY.
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).
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: Virion.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Low expression in testis.
CC {ECO:0000269|PubMed:12970426}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield the mature SU and TM
CC proteins. {ECO:0000250}.
CC -!- MISCELLANEOUS: Orthologs in P.troglodytes, G.gorilla (truncated) and
CC P.pygmaeus (truncated).
CC -!- MISCELLANEOUS: HERV-H family subgenomic RNAs have been observed.
CC -!- MISCELLANEOUS: This provirus is intergenic, the closest flanking genes
CC being KCNJ3 and NR4A2.
CC -!- SIMILARITY: Belongs to the gamma type-C retroviral envelope protein
CC family. HERV class-I H env subfamily. {ECO:0000305}.
CC -!- CAUTION: Lacks the CX6CC and the CKS-17 domains. {ECO:0000305}.
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DR EMBL; AJ289711; CAB94194.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9N2J8; -.
DR SMR; Q9N2J8; -.
DR GlyGen; Q9N2J8; 7 sites.
DR BioMuta; -; -.
DR PeptideAtlas; Q9N2J8; -.
DR PRIDE; Q9N2J8; -.
DR TopDownProteomics; Q9N2J8; -.
DR neXtProt; NX_Q9N2J8; -.
DR PhylomeDB; Q9N2J8; -.
DR Pharos; Q9N2J8; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9N2J8; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF00429; TLV_coat; 1.
PE 2: Evidence at transcript 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..35
FT /evidence="ECO:0000255"
FT CHAIN 36..555
FT /note="HERV-H_2q24.1 provirus ancestral Env polyprotein"
FT /id="PRO_0000008470"
FT CHAIN 36..387
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008471"
FT CHAIN 388..555
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008472"
FT TOPO_DOM 36..515
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..555
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 388..408
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT MOTIF 64..67
FT /note="CXXC"
FT /evidence="ECO:0000250"
FT SITE 387..388
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 555 AA; 60911 MW; E559604545407844 CRC64;
MILAGRAPSN TSTLMKFYSL LLYSLLFSFP FLYHPLPLPS YLHHTINLTH SLPAASNPSL
ANNCWLCISL SSSAYIAVPT LQTDRATSPV SLHLRTSFNS PHLYPPEELI YFLDRSSKTS
PDISHQPAAA LLHIYLKNLS PYINSTPPIF GPLTTQTTIP VAAPLCISRQ RPTGIPLGNI
SPSRCSFTLH LQSPTTHVTE TIGVFQLHII DKPSINTDKL KNVSSNYCLG RHLPYISLHP
WLPSPCSSDS PPRPSSCLLT PSPQNNSERL LVDTQRFLIH HENRTSSSMQ LAHQSPLQPL
TAAALAGSLG VWVQDTPFST PSHPFSLHLQ FCLTQGLFFL CGSSTYMCLP ANWTGTCTLV
FLTPKIQFAN GTKELPVPLM TLTPQKRVIP LIPLMVGLGL SASTIALSTG IAGISTSVTT
FRSPSNDFSA SITDISQTLS VLQAQVDSLA AVVLQNRRGL GLSILLNEEC CFYLNQSGLV
YENIKKLKDR AQKLANQASN YAESPWALSN WMSWVLPILS PLIPIFLLLL FGPCIFHLVS
QFIQNRIQAI TNHSI
