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Endogenous retrovirus group 3 member 1 Env polyprotein (ERV-3 envelope protein) (ERV3 envelope protein) (ERV3-1 envelope protein) (Envelope polyprotein) (HERV-R envelope protein) (ERV-R envelope protein) (HERV-R_7q21.2 provirus ancestral Env polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]

 ENR1_HUMAN              Reviewed;         604 AA.
Q14264;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
23-MAY-2018, entry version 132.
RecName: Full=Endogenous retrovirus group 3 member 1 Env polyprotein;
AltName: Full=ERV-3 envelope protein;
Short=ERV3 envelope protein;
AltName: Full=ERV3-1 envelope protein;
AltName: Full=Envelope polyprotein;
AltName: Full=HERV-R envelope protein;
Short=ERV-R envelope protein;
AltName: Full=HERV-R_7q21.2 provirus ancestral Env polyprotein;
Contains:
RecName: Full=Surface protein;
Short=SU;
Contains:
RecName: Full=Transmembrane protein;
Short=TM;
Flags: Precursor;
Name=ERV3-1; Synonyms=ERV3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-604, AND VARIANTS ILE-90;
SER-481 AND SER-569.
PubMed=3840930; DOI=10.1016/0042-6822(85)90147-3;
Cohen M., Powers M., O'Connell C., Kato N.;
"The nucleotide sequence of the env gene from the human provirus ERV3
and isolation and characterization of an ERV3-specific cDNA.";
Virology 147:449-458(1985).
[3]
FUNCTION.
PubMed=7645262; DOI=10.1006/viro.1995.1442;
Venables P.J.W., Brookes S.M., Griffiths D., Weiss R.A., Boyd M.T.;
"Abundance of an endogenous retroviral envelope protein in placental
trophoblasts suggests a biological function.";
Virology 211:589-592(1995).
[4]
FUNCTION.
PubMed=10692254; DOI=10.1053/plac.1999.0443;
Lin L., Xu B., Rote N.S.;
"The cellular mechanism by which the human endogenous retrovirus ERV-3
env gene affects proliferation and differentiation in a human
placental trophoblast model, BeWo.";
Placenta 21:73-78(2000).
[5]
FUNCTION.
PubMed=14557543; DOI=10.1073/pnas.2132646100;
Blaise S., de Parseval N., Benit L., Heidmann T.;
"Genomewide screening for fusogenic human endogenous retrovirus
envelopes identifies syncytin 2, a gene conserved on primate
evolution.";
Proc. Natl. Acad. Sci. U.S.A. 100:13013-13018(2003).
[6]
TISSUE SPECIFICITY.
PubMed=12970426; DOI=10.1128/JVI.77.19.10414-10422.2003;
de Parseval N., Lazar V., Casella J.-F., Benit L., Heidmann T.;
"Survey of human genes of retroviral origin: identification and
transcriptome of the genes with coding capacity for complete envelope
proteins.";
J. Virol. 77:10414-10422(2003).
[7]
DEVELOPMENTAL STAGE.
PubMed=12083821; DOI=10.1006/viro.2002.1428;
Andersson A.-C., Venables P.J.W., Toenjes R.R., Scherer J.,
Eriksson L., Larsson E.;
"Developmental expression of HERV-R (ERV3) and HERV-K in human
tissue.";
Virology 297:220-225(2002).
[8]
VARIANTS TYR-192; CYS-236; PRO-522 AND SER-569, AND POLYMORPHISM.
PubMed=9525678;
de Parseval N., Heidmann T.;
"Physiological knockout of the envelope gene of the single-copy ERV-3
human endogenous retrovirus in a fraction of the Caucasian
population.";
J. Virol. 72:3442-3445(1998).
[9]
VARIANTS ILE-90; TYR-192; CYS-236; SER-481 AND SER-569, AND
POLYMORPHISM.
PubMed=10427470; DOI=10.1155/1998/958379;
Rasmussen H.B., Clausen J.;
"Large number of polymorphic nucleotides and a termination codon in
the env gene of the endogenous human retrovirus ERV3.";
Dis. Markers 14:127-133(1998).
-!- FUNCTION: Retroviral envelope proteins mediate receptor
recognition and membrane fusion during early infection. Endogenous
envelope proteins may have kept, lost or modified their original
function during evolution. This endogenous envelope protein has
lost its fusogenic properties. It can inhibit cell growth through
decrease expression of cyclin B1 and increased expression of p21
in vitro. {ECO:0000269|PubMed:10692254,
ECO:0000269|PubMed:14557543, ECO:0000269|PubMed:7645262}.
-!- FUNCTION: SU mediates receptor recognition. {ECO:0000250}.
-!- FUNCTION: TM anchors the envelope heterodimer to the viral
membrane through one transmembrane domain. The other hydrophobic
domain, called fusion peptide, mediates fusion of the viral
membrane with the target cell membrane (By similarity).
{ECO:0000250}.
-!- SUBUNIT: The surface (SU) and transmembrane (TM) proteins form a
heterodimer. SU and TM are attached by non-covalent interactions
or by a labile interchain disulfide bond (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Virion.
-!- TISSUE SPECIFICITY: Expressed at higher level in adrenal,
sebaceous glands and placenta. Expressed at lower level in bone
marrow, brain, breast, colon, heart, kidney, liver, lung, ovary,
PBL, prostate, skin, spleen, testis, thymus, thyroid, trachea.
{ECO:0000269|PubMed:12970426}.
-!- DEVELOPMENTAL STAGE: Highly expressed in primitive adrenal cortex
and placenta. Expressed at lower level in developing nervous
tissues, tongue, heart, gut, kidney, columna vertebralis and
liver. {ECO:0000269|PubMed:12083821}.
-!- DOMAIN: Contains the CKS-17 immunosuppressive domain present in
many retroviral envelope proteins. As a synthetic peptide, it
inhibits immune function in vitro and in vivo (By similarity).
{ECO:0000250}.
-!- PTM: Specific enzymatic cleavages in vivo yield the mature SU and
TM proteins (By similarity). Has been mainly detected in vivo as
an 65 kDa unprocessed polyprotein precursor. {ECO:0000250}.
-!- PTM: The CXXC motif is highly conserved across a broad range of
retroviral envelope proteins. It is thought to participate in the
formation of a labile disulfide bond possibly with the CX6CC motif
present in the transmembrane protein. Isomerization of the
intersubunit disulfide bond to an SU intrachain disulfide bond is
thought to occur upon receptor recognition in order to allow
membrane fusion (By similarity). {ECO:0000250}.
-!- POLYMORPHISM: This envelope gene is polymorphic with at least five
different alleles. A mutation introducing a premature stop codon
instead of amino acid 223 is present in approximately 1% of the
Caucasian population (PubMed:9525678).
{ECO:0000269|PubMed:10427470, ECO:0000269|PubMed:3840930,
ECO:0000269|PubMed:9525678}.
-!- MISCELLANEOUS: HERV-R_7q21.2 genomic and subgenomic RNAs have been
observed.
-!- MISCELLANEOUS: This provirus is intergenic, the closest flanking
genes being ZNF117 and FLJ25037.
-!- SIMILARITY: Belongs to the gamma type-C retroviral envelope
protein family. HERV class-I R env subfamily. {ECO:0000305}.
-!- CAUTION: CKS-17 sequence does not match the minimal active
consensus. {ECO:0000305}.
-!- CAUTION: Truncated; premature stop codon upstream of the fusion
peptide on TM. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AC073210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M12140; AAA88027.1; -; Genomic_DNA.
CCDS; CCDS47595.1; -.
RefSeq; NP_001007254.2; NM_001007253.3.
UniGene; Hs.250693; -.
UniGene; Hs.596334; -.
ProteinModelPortal; Q14264; -.
SMR; Q14264; -.
BioGrid; 108395; 1.
STRING; 9606.ENSP00000391594; -.
iPTMnet; Q14264; -.
PhosphoSitePlus; Q14264; -.
BioMuta; ERV3-1; -.
DMDM; 44887883; -.
PaxDb; Q14264; -.
PeptideAtlas; Q14264; -.
PRIDE; Q14264; -.
TopDownProteomics; Q14264; -.
Ensembl; ENST00000394323; ENSP00000391594; ENSG00000213462.
GeneID; 2086; -.
KEGG; hsa:2086; -.
UCSC; uc011kdr.3; human.
CTD; 2086; -.
DisGeNET; 2086; -.
EuPathDB; HostDB:ENSG00000213462.4; -.
GeneCards; ERV3-1; -.
HGNC; HGNC:3454; ERV3-1.
HPA; HPA017209; -.
neXtProt; NX_Q14264; -.
OpenTargets; ENSG00000213462; -.
PharmGKB; PA27866; -.
eggNOG; ENOG410J56G; Eukaryota.
eggNOG; ENOG410ZFDP; LUCA.
GeneTree; ENSGT00910000146046; -.
HOGENOM; HOG000112377; -.
HOVERGEN; HBG048920; -.
InParanoid; Q14264; -.
OMA; WPWEARE; -.
OrthoDB; EOG091G08G1; -.
PhylomeDB; Q14264; -.
GeneWiki; ERV3; -.
GenomeRNAi; 2086; -.
PRO; PR:Q14264; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000213462; -.
CleanEx; HS_ERV3; -.
InterPro; IPR018154; TLV/ENV_coat_polyprotein.
PANTHER; PTHR10424; PTHR10424; 1.
2: Evidence at transcript level;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
ERV; Glycoprotein; Polymorphism; Reference proteome; Signal;
Transposable element; Viral envelope protein; Virion.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 604 Endogenous retrovirus group 3 member 1
Env polyprotein.
/FTId=PRO_0000008477.
CHAIN 23 471 Surface protein. {ECO:0000250}.
/FTId=PRO_0000008478.
CHAIN 472 604 Transmembrane protein. {ECO:0000250}.
/FTId=PRO_0000008479.
MOTIF 165 168 CXXC. {ECO:0000250}.
MOTIF 548 564 CKS-17. {ECO:0000250}.
MOTIF 565 574 CX6CC. {ECO:0000250}.
SITE 471 472 Cleavage. {ECO:0000250}.
CARBOHYD 64 64 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 105 105 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 201 201 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 316 316 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 369 369 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 382 382 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 399 399 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 527 527 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 569 569 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 90 90 T -> I (in dbSNP:rs6460219).
{ECO:0000269|PubMed:10427470,
ECO:0000269|PubMed:3840930}.
/FTId=VAR_017801.
VARIANT 192 192 C -> Y (in dbSNP:rs34639489).
{ECO:0000269|PubMed:10427470,
ECO:0000269|PubMed:9525678}.
/FTId=VAR_017802.
VARIANT 236 236 Y -> C (in dbSNP:rs71539632).
{ECO:0000269|PubMed:10427470,
ECO:0000269|PubMed:9525678}.
/FTId=VAR_017803.
VARIANT 481 481 N -> S (in dbSNP:rs4618579).
{ECO:0000269|PubMed:10427470,
ECO:0000269|PubMed:3840930}.
/FTId=VAR_017804.
VARIANT 522 522 L -> P. {ECO:0000269|PubMed:9525678}.
/FTId=VAR_017805.
VARIANT 569 569 N -> S (in dbSNP:rs4717229).
{ECO:0000269|PubMed:10427470,
ECO:0000269|PubMed:3840930,
ECO:0000269|PubMed:9525678}.
/FTId=VAR_017806.
CONFLICT 218 218 A -> T (in Ref. 2; AAA88027).
{ECO:0000305}.
CONFLICT 226 226 G -> D (in Ref. 2; AAA88027).
{ECO:0000305}.
CONFLICT 251 251 F -> L (in Ref. 2; AAA88027).
{ECO:0000305}.
SEQUENCE 604 AA; 67942 MW; C426D9193857D4BD CRC64;
MLGMNMLLIT LFLLLPLSML KGEPWEGCLH CTHTTWSGNI MTKTLLYHTY YECAGTCLGT
CTHNQTTYSV CDPGRGQPYV CYDPKSSPGT WFEIHVGSKE GDLLNQTKVF PSGKDVVSLY
FDVCQIVSMG SLFPVIFSSM EYYSSCHKNR YAHPACSTDS PVTTCWDCTT WSTNQQSLGP
IMLTKIPLEP DCKTSTCNSV NLTILEPDQP IWTTGLKAPL GARVSGEEIG PGAYVYLYII
KKTRTRSTQQ FRVFESFYEH VNQKLPEPPP LASNLFAQLA ENIASSLHVA SCYVCGGMNM
GDQWPWEARE LMPQDNFTLT ASSLEPAPSS QSIWFLKTSI IGKFCIARWG KAFTDPVGEL
TCLGQQYYNE TLGKTLWRGK SNNSESPHPS PFSRFPSLNH SWYQLEAPNT WQAPSGLYWI
CGPQAYRQLP AKWSGACVLG TIRPSFFLMP LKQGEALGYP IYDETKRKSK RGITIGDWKD
NEWPPERIIQ YYGPATWAED GMWGYRTPVY MLNRIIRLQA VLEIITNETA GALNLLAQQA
TKMRNVIYQN RLALDYLLAQ EEGVCGKFNL TNCCLELDDE GKVIKEITAK IQKLAHIPVQ
TWKG


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