EFC2_HUMAN
ID EFC2_HUMAN Reviewed; 527 AA.
AC P60608;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Endogenous retrovirus group FC1 member 1 Env polyprotein;
DE AltName: Full=Envelope polyprotein;
DE AltName: Full=Fc2deltaenv;
DE AltName: Full=HERV-F(c)2_7q36.2 provirus ancestral Env polyprotein;
DE Includes:
DE RecName: Full=Surface protein;
DE Short=SU;
DE Includes:
DE RecName: Full=Truncated transmembrane protein;
DE Short=TM;
GN Name=ERVFC1-1;
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 [GENOMIC DNA].
RA Birren B., Linton L., Nusbaum C., Lander E.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP CHARACTERIZATION.
RX PubMed=11689652; DOI=10.1128/jvi.75.23.11709-11719.2001;
RA Benit L., Dessen P., Heidmann T.;
RT "Identification, phylogeny, and evolution of retroviral elements based on
RT their envelope genes.";
RL J. Virol. 75:11709-11719(2001).
RN [4]
RP CHARACTERIZATION.
RX PubMed=12890629; DOI=10.1016/s0042-6822(03)00163-6;
RA Benit L., Calteau A., Heidmann T.;
RT "Characterization of the low-copy HERV-Fc family: evidence for recent
RT integrations in primates of elements with coding envelope genes.";
RL Virology 312:159-168(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 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: Virion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=1;
CC Comment=A ribosomal frameshift due to a slippery site present at the
CC end of the gene may lead to a longer protein.;
CC Name=1;
CC IsoId=P60608-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Low expression in skin and testis.
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 -!- MISCELLANEOUS: Orthologs in P.troglodytes (truncated), G.gorilla
CC (truncated).
CC -!- SIMILARITY: Belongs to the gamma type-C retroviral envelope protein
CC family. HERV class-I F(c)2 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}.
CC -!- CAUTION: No predictable signal peptide. {ECO:0000305}.
CC -!- CAUTION: Truncated; premature stop codon upstream of the potential
CC transmembrane domain. {ECO:0000305}.
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DR EMBL; AC016222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P60608; -.
DR SMR; P60608; -.
DR iPTMnet; P60608; -.
DR PhosphoSitePlus; P60608; -.
DR BioMuta; HGNC:38137; -.
DR DMDM; 45476806; -.
DR MassIVE; P60608; -.
DR PRIDE; P60608; -.
DR GeneCards; ERVFC1-1; -.
DR HGNC; HGNC:38137; ERVFC1-1.
DR neXtProt; NX_P60608; -.
DR PhylomeDB; P60608; -.
DR PathwayCommons; P60608; -.
DR Pharos; P60608; Tdark.
DR PRO; PR:P60608; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P60608; protein.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF00429; TLV_coat; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; ERV; Reference proteome; Ribosomal frameshifting;
KW Transposable element; Viral envelope protein; Virion.
FT CHAIN 1..527
FT /note="Endogenous retrovirus group FC1 member 1 Env
FT polyprotein"
FT /id="PRO_0000008437"
FT REGION 1..411
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT REGION 412..527
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT REGION 412..432
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT MOTIF 280..283
FT /note="CXXC"
FT /evidence="ECO:0000250"
FT MOTIF 477..493
FT /note="CKS-17"
FT /evidence="ECO:0000250"
FT MOTIF 494..502
FT /note="CX6CC"
FT /evidence="ECO:0000250"
FT SITE 411..412
FT /note="Ancestral cleavage site"
FT /evidence="ECO:0000255"
FT DISULFID 494..501
FT /evidence="ECO:0000250"
SQ SEQUENCE 527 AA; 58319 MW; A3E936C20EFFA02E CRC64;
MNSPCDRLQQ FIQVLLEESW SFPSFANTLH WPENLLSYID ELVWQGSLQN FHQHEVRFDK
PPLRLPLTGF SSLTENWSSR QAVSSRLVAT AASPPAGCQA PIAFLGLKFS SLGPARKNPA
LCFLYDQSNS KCNTSWVKEN VGCPWHWCNI HEALIRTEKG SDPMFYVNTS TGGRDGFNGF
NLQISDPWDP RWASGVDGGL YEHKTFMYPV AKIRIARTLK TTVTGLSDLA SSIQSAEKEL
TSQLQPAADQ AKSSRFSWLT LISEGAQLLQ STGVQNLSHC FLCAALRRPP LVAVPLPTPF
NYTINSSTPI PPVPKGQVPL FSDPIRHKFP FCYSTPNASW CNQTRMLTST PAPPRGYFWC
NSTLTKVLNS TGNHTLCLPI SLIPGLTLYS QDELSHLLAW TEPRPQNKSK WAIFLPLVLG
ISLASSLVAS GLGKGALTHS IQTSQDLSTH LQLAIEASAE SLDSLQRQIT TVAQVAAQNR
QALDLLMAEK GRTCLFLQEE CCYYLNESGV VENSLQTLKK KKSSKRS
