ENVT1_HUMAN
ID ENVT1_HUMAN Reviewed; 626 AA.
AC P61550; I7GPQ9;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Endogenous retrovirus group S71 member 1 Env polyprotein;
DE AltName: Full=Envelope polyprotein;
DE AltName: Full=HERV-T Env protein;
DE AltName: Full=HERV-T_19q13.11 provirus ancestral Env polyprotein;
DE Includes:
DE RecName: Full=Surface protein;
DE Short=SU;
DE Includes:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE Flags: Precursor;
GN Name=ERVS71-1;
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 [MRNA].
RC TISSUE=Thyroid;
RA Abe H., Lavanya M., Kajiwara E., Kitaguchi D., Manel N., Arita T.,
RA Tsuji-Kawahara S., Battini J.L., Takemura T., Sitbon M., Miyazawa M.;
RT "Functional receptor binding domain encoded by the human endogenous
RT retroviral envT gene and the presence of an envT-related env gene within
RT the context of formerly envelope-less HC2 provirus.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
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 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Note=At the origin, this retroviral envelope
CC protein was localized in the virion. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at higher level in thyroid. Expressed at
CC lower level in adrenal, bone marrow, brain, breast, kidney, ovary,
CC placenta, prostate, skin, testis and trachea.
CC {ECO:0000269|PubMed:12970426}.
CC -!- DOMAIN: The CKS-17 immunosuppressive domain is present in many
CC retroviral envelope proteins. As a synthetic peptide, it inhibits
CC immune function in vitro and in vivo (By similarity). {ECO:0000250}.
CC -!- PTM: The CXXC motif is highly conserved across a broad range of
CC retroviral envelope proteins. It is thought to participate in the
CC formation of a labile disulfide bond possibly with the CX6CC motif
CC present in the transmembrane domain (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the gamma type-C retroviral envelope protein
CC family. HERV class-I T env subfamily. {ECO:0000305}.
CC -!- CAUTION: The cleavage site does not match the consensus. {ECO:0000305}.
CC -!- CAUTION: CKS-17 sequence does not match the minimal active consensus.
CC {ECO:0000305}.
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DR EMBL; AB266802; BAG06168.1; -; mRNA.
DR EMBL; AC078899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_011526770.1; XM_011528468.2.
DR RefSeq; XP_011526771.1; XM_011528469.2.
DR AlphaFoldDB; P61550; -.
DR SMR; P61550; -.
DR BioMuta; HGNC:41525; -.
DR DMDM; 47716681; -.
DR MassIVE; P61550; -.
DR PeptideAtlas; P61550; -.
DR PRIDE; P61550; -.
DR GeneCards; ERVS71-1; -.
DR HGNC; HGNC:41525; ERVS71-1.
DR neXtProt; NX_P61550; -.
DR OrthoDB; 1281266at2759; -.
DR PhylomeDB; P61550; -.
DR Pharos; P61550; Tdark.
DR PRO; PR:P61550; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P61550; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 3.90.310.10; -; 1.
DR InterPro; IPR008981; FMuLV_rcpt-bd.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF00429; TLV_coat; 1.
DR SUPFAM; SSF49830; SSF49830; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; ERV; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transposable element.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..626
FT /note="Endogenous retrovirus group S71 member 1 Env
FT polyprotein"
FT /id="PRO_0000008481"
FT TOPO_DOM 39..575
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 597..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 39..438
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT REGION 439..626
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT REGION 439..459
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT MOTIF 302..305
FT /note="CXXC"
FT /evidence="ECO:0000250"
FT MOTIF 503..519
FT /note="CKS-17"
FT /evidence="ECO:0000250"
FT MOTIF 520..528
FT /note="CX6CC"
FT /evidence="ECO:0000250"
FT SITE 438..439
FT /note="Ancestral cleavage site"
FT /evidence="ECO:0000255"
FT DISULFID 520..527
FT /evidence="ECO:0000250"
SQ SEQUENCE 626 AA; 68171 MW; 44C010ABA3E26C2F CRC64;
MGPEAWVRPL KTAPKPGEAI RLILFIYLSC FFLPVMSSEP SYSFLLTSFT TGRVFANTTW
RAGTSKEVSF AVDLCVLFPE PARTHEEQHN LPVIGAGSVD LAAGFGHSGS QTGCGSSKGA
EKGLQNVDFY LCPGNHPDAS CRDTYQFFCP DWTCVTLATY SGGSTRSSTL SISRVPHPKL
CTRKNCNPLT ITVHDPNAAQ WYYGMSWGLR LYIPGFDVGT MFTIQKKILV SWSSPKPIGP
LTDLGDPIFQ KHPDKVDLTV PLPFLVPRPQ LQQQHLQPSL MSILGGVHHL LNLTQPKLAQ
DCWLCLKAKP PYYVGLGVEA TLKRGPLSCH TRPRALTIGD VSGNASCLIS TGYNLSASPF
QATCNQSLLT SISTSVSYQA PNNTWLACTS GLTRCINGTE PGPLLCVLVH VLPQVYVYSG
PEGRQLIAPP ELHPRLHQAV PLLVPLLAGL SIAGSAAIGT AALVQGETGL ISLSQQVDAD
FSNLQSAIDI LHSQVESLAE VVLQNCRCLD LLFLSQGGLC AALGESCCFY ANQSGVIKGT
VKKVRENLDR HQQERENNIP WYQSMFNWNP WLTTLITGLA GPLLILLLSL IFGPCILNSF
LNFIKQRIAS VKLTYLKTQY DTLVNN
