EFC1_HUMAN
ID EFC1_HUMAN Reviewed; 584 AA.
AC P60507; Q5JTS0;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Endogenous retrovirus group FC1 Env polyprotein;
DE AltName: Full=Envelope polyprotein;
DE AltName: Full=Fc1env;
DE AltName: Full=HERV-F(c)1_Xq21.33 provirus ancestral Env polyprotein;
DE AltName: Full=HERV-Fc1env;
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=ERVFC1;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [2]
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 [3]
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 [4]
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 [5]
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 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: Specific enzymatic cleavages in vivo yield the mature SU and TM
CC proteins. {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 protein (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Orthologs in P.troglodytes and G.gorilla (truncated).
CC -!- SIMILARITY: Belongs to the gamma type-C retroviral envelope protein
CC family. HERV class-I F(c)1 env subfamily. {ECO:0000305}.
CC -!- CAUTION: CKS-17 sequence does not match the minimal active consensus.
CC {ECO:0000305}.
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DR EMBL; AL354685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_011507308.1; XM_011509006.2.
DR RefSeq; XP_011529387.1; XM_011531085.2.
DR AlphaFoldDB; P60507; -.
DR SMR; P60507; -.
DR GlyGen; P60507; 11 sites.
DR iPTMnet; P60507; -.
DR PhosphoSitePlus; P60507; -.
DR BioMuta; ERVFC1; -.
DR jPOST; P60507; -.
DR MassIVE; P60507; -.
DR PRIDE; P60507; -.
DR GeneID; 105373297; -.
DR KEGG; hsa:105373297; -.
DR CTD; 105373297; -.
DR GeneCards; ERVFC1; -.
DR neXtProt; NX_P60507; -.
DR OrthoDB; 653205at2759; -.
DR PhylomeDB; P60507; -.
DR Pharos; P60507; Tdark.
DR PRO; PR:P60507; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P60507; 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 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..584
FT /note="Endogenous retrovirus group FC1 Env polyprotein"
FT /id="PRO_0000008430"
FT CHAIN 23..383
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008431"
FT CHAIN 384..584
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008432"
FT TOPO_DOM 23..518
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..584
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 384..404
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT MOTIF 251..254
FT /note="CXXC"
FT /evidence="ECO:0000250"
FT MOTIF 449..465
FT /note="CKS-17"
FT /evidence="ECO:0000250"
FT MOTIF 466..474
FT /note="CX6CC"
FT /evidence="ECO:0000250"
FT SITE 383..384
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 466..473
FT /evidence="ECO:0000250"
SQ SEQUENCE 584 AA; 65248 MW; 8C7339ADF9136646 CRC64;
MARPSPLCLL LLLTLLTPIV PSNSLLTEPP FRWRFYLHET WTQGNRLSTV TLATVDCQPH
GCQAQVTFNF TSFKSVLRGW SNPTICFVYD QTHSNCRDYW VDTNGGCPYA YCRMHVTQLH
TAKKLQHTYR LTSDGRTTYF LTIPDPWDSR WVSGVTGRLY RWPTDSYPVG KLRIFLTYIR
VIPQVLSNLK DQADNIKHQE EVINTLVQSH PKADMVTYDD KAEAGPFSWI TLVRHGARLV
NMAGLVNLSH CFLCTALSQP PLVAVPLPQA FNTSGNHTAH PSGVFSEQVP LFRDPLQPQF
PFCYTTPNSS WCNQTYSGSL SNLSAPAGGY FWCNFTLTKH LNISSNNTLS RNLCLPISLV
PRLTLYSEAE LSSLVNPPMR QKRAVFPPLV IGVSLTSSLV ASGLGTGAIV HFISSSQDLS
IKLQMAIEAS AESLASLQRQ ITSVAKVAMQ NRRALDLLTA DKGGTCMFLG EECCYYINES
GLVETSLLTL DKIRDGLHRP SSTPNYGGGW WQSPLTTWII PFISPILIIC LLLLIAPCVL
KFIKNRISEV SRVTVNQMLL HPYSRLPTSE DHYDDALTQQ EAAR
