EFCB_PAPAN
ID EFCB_PAPAN Reviewed; 579 AA.
AC P61552;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=ERV-BabFcenv provirus ancestral Env polyprotein;
DE AltName: Full=BabFcenv;
DE AltName: Full=Envelope polyprotein;
DE Includes:
DE RecName: Full=Surface protein;
DE Short=SU;
DE Includes:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE Flags: Precursor;
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
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.
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.
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 domain (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: This envelope protein is encoded by a baboon specific
CC provirus. It has no ortholog in human.
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: The cleavage site does not match the consensus. {ECO:0000305}.
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DR EMBL; AC091754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P61552; -.
DR SMR; P61552; -.
DR Proteomes; UP000028761; Unplaced.
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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; ERV; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Transposable element.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..579
FT /note="ERV-BabFcenv provirus ancestral Env polyprotein"
FT /id="PRO_0000008438"
FT TOPO_DOM 23..523
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..579
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 23..387
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT REGION 388..579
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT REGION 388..408
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT MOTIF 255..258
FT /note="CXXC"
FT /evidence="ECO:0000250"
FT MOTIF 453..469
FT /note="CKS-17"
FT /evidence="ECO:0000250"
FT MOTIF 470..478
FT /note="CX6CC"
FT /evidence="ECO:0000250"
FT SITE 387..388
FT /note="Ancestral cleavage site"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
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 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 470..477
FT /evidence="ECO:0000250"
SQ SEQUENCE 579 AA; 63475 MW; 608C15CBE4C90947 CRC64;
MISAVLNLPS TPLLPLLWFT LIIPASLTNP KFVWRFSITE TWSTGNQAHS QTQGTADCSP
QGCQDALLLN FHLSSVGNYD HPVICFLYDQ TEYNCKNYWQ ETNLGCPYNY CNMHEIGLMC
ANGICTPNDR PFVRNRTSGG YILTIKDPWD PRWAQGVKGG LYATSWSSYP TATLQIKRVY
VQQVPAPKSK QVDPPKSVQA LQNLTSVVKS HEQKIQKLLS PPNSPNNEDP FSWLTLIRQG
LNLTQAAGVR NLSHCFLCAA LGKAPLVAVP LPTAFNITTD STSSSQATSL PQVPLYRNPQ
SQTLPFCYST PNSSWCDRTQ APSRTQTAPV GGYFWCNQTL SKTLNHASIT QSLCVPVSLV
PSLTLYSEGE LAELASQLSS SNNIQKQAVF LPLIIGVSLA SSLVASGLGT GALTHSIQST
QTLSTQVQAA IEASAESLAS LQRQITSVAQ VAAQNRRALD LLTAEKGGTC LFLGEECCYY
VNESGLVDTN VKTLNKIKKE LQQFNAPLTP GPPVWLLPVV QQMLPFLIPI LILCLMLCLA
PILIKFLRAR VQEITRVTFN QMLLHPYTQL PTSDPNYAP
