ENV_CAEVC
ID ENV_CAEVC Reviewed; 966 AA.
AC P31626;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE AltName: Full=Glycoprotein 135;
DE Short=gp135;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE AltName: Full=Glycoprotein 38;
DE Short=gp38;
DE Flags: Precursor;
GN Name=env;
OS Caprine arthritis encephalitis virus (strain Cork) (CAEV-Co).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11661;
OH NCBI_TaxID=9925; Capra hircus (Goat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1656067; DOI=10.1128/jvi.65.11.5744-5750.1991;
RA Knowles D.P. Jr., Cheevers W.P., McGuire T.C., Brassfield A.L.,
RA Harwood W.G., Stem T.A.;
RT "Structure and genetic variability of envelope glycoproteins of two
RT antigenic variants of caprine arthritis-encephalitis lentivirus.";
RL J. Virol. 65:5744-5750(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2171210; DOI=10.1016/0042-6822(90)90303-9;
RA Saltarelli M., Querat G., Konings D.A.M., Vigne R., Clements J.E.;
RT "Nucleotide sequence and transcriptional analysis of molecular clones of
RT CAEV which generate infectious virus.";
RL Virology 179:347-364(1990).
CC -!- FUNCTION: The surface protein (SU) attaches the virus to the host cell
CC by binding to its receptor. This interaction triggers the refolding of
CC the transmembrane protein (TM) and is thought to activate its fusogenic
CC potential by unmasking its fusion peptide. Fusion occurs at the host
CC cell plasma membrane (By similarity). {ECO:0000250}.
CC -!- FUNCTION: The transmembrane protein (TM) acts as a class I viral fusion
CC protein. Under the current model, the protein has at least 3
CC conformational states: pre-fusion native state, pre-hairpin
CC intermediate state, and post-fusion hairpin state. During viral and
CC target cell membrane fusion, the coiled coil regions (heptad repeats)
CC assume a trimer-of-hairpins structure, positioning the fusion peptide
CC in close proximity to the C-terminal region of the ectodomain. The
CC formation of this structure appears to drive apposition and subsequent
CC fusion of viral and target cell membranes. Membranes fusion leads to
CC delivery of the nucleocapsid into the cytoplasm (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of SU-
CC TM heterodimers attached by noncovalent interactions or by a labile
CC interchain disulfide bond. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host
CC cell membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}. Note=It is probably concentrated at the site of budding
CC and incorporated into the virions possibly by contacts between the
CC cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Virion membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Host cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The
CC surface protein is not anchored to the viral envelope, but associates
CC with the extravirion surface through its binding to TM. It is probably
CC concentrated at the site of budding and incorporated into the virions
CC possibly by contacts between the cytoplasmic tail of Env and the N-
CC terminus of Gag (By similarity). {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC Envelope glycoproteins are synthesized as an inactive precursor that is
CC N-glycosylated and processed likely by host cell furin or by a furin-
CC like protease in the Golgi to yield the mature SU and TM proteins. The
CC cleavage site between SU and TM requires the minimal sequence [KR]-X-
CC [KR]-R (By similarity). {ECO:0000250}.
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DR EMBL; M33677; AAA91829.1; -; Genomic_RNA.
DR PIR; B41307; VCLJCC.
DR RefSeq; NP_040942.1; NC_001463.1.
DR GeneID; 1489974; -.
DR KEGG; vg:1489974; -.
DR Proteomes; UP000203242; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
KW Glycoprotein; Host cell membrane; Host membrane; Host-virus interaction;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..83
FT /evidence="ECO:0000250"
FT CHAIN 84..966
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239522"
FT CHAIN 84..632
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038688"
FT CHAIN 633..966
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038689"
FT TOPO_DOM 84..801
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 802..822
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 823..966
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 633..653
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 699..715
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 665..715
FT /evidence="ECO:0000255"
FT COILED 756..791
FT /evidence="ECO:0000255"
FT SITE 632..633
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CONFLICT 41
FT /note="N -> Q (in Ref. 2; AAA91829)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="N -> Q (in Ref. 2; AAA91829)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="D -> P (in Ref. 2; AAA91829)"
FT /evidence="ECO:0000305"
FT CONFLICT 834
FT /note="E -> Q (in Ref. 2; AAA91829)"
FT /evidence="ECO:0000305"
FT CONFLICT 936..937
FT /note="GL -> DC (in Ref. 2; AAA91829)"
FT /evidence="ECO:0000305"
FT CONFLICT 941..966
FT /note="HKKGTDIGLGQIPVDHLWCYKKSKSL -> AKED (in Ref. 2;
FT AAA91829)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 966 AA; 110291 MW; 2ADEB6A92EC1D69B CRC64;
MDAGARYMRL TGKENWVEVT MDGEKERKRE GFTAGQQGKY NPQVSKNIGN RNTNDCFAYK
GIFLWRISLT MWILLGINMC VSAEDYITLI SDPYGFSPIK NVSGVPVTCV TKEFAKWGCQ
PLGAYPDPEI EYRNVSQEVV KEVYQENWPW NTYHWPLWQM ENVRYWLKEN MQENQQRKNN
TKEGIEELLA GTIRGRFCVP YPFALLKCTK WCWYTAAINN ESGKAGKIKI NCTEARAVSC
TEDMPLASIQ RAYWDEKDRE SMAFMNIKAC DSNLRCQKRP GGCMEGYPIP VGAEIIPESM
KYLRGAKSQY GGIKDKNGEL KLPLTLRVWV KLANVSEWVN GTPPDWQDRI NGSKGINGTL
WGELNSMHHL GFALSQNGKW CNYTGEIKLG QETFQYHYKP NWNCTGNWTQ YPVWQVIRNL
DMVEHMTGEC VQRPQRHNIT VGNGTITGNC STTNWDGCNC SRSGNYLYNS SEGGLLLILC
RQNSTLTRIL GTNTNWTTMW GIYKNCSGCE NATLDNTGEG TLGGVANKNC SLPHKNESNK
WTCAPRQRDG KTDSLYIAGG KKFWTRIKAQ FSCESNIGQL DGMLHQQILL QKYQVIKVRA
YTYGVIEMPE NYAKTRIINR KKRELSHKRK KRGVGLVIML VIMAIVAAAG ASLGVANAIQ
QSYTKAAVQT LANATAAQQD VLEATYAMVQ HVAKGVRILE ARVARVEAIT DRIMLYQELD
CWHYHQYCIT STKTEVAKYI NWTRFKDNCT WQQWERGLQG YDTNLTILLK ESAAMTQLAE
EQARRIPEVW ESLKDVFDWS GWFSWLKYIP IIVVGLLGCI LIRAVICVCQ PLVEIYRTLS
TPTYQRVTVI METRADVAGE NQDFGDGLEE SDNSETSERV TVQKAWSRAW ELWQNSPWKE
PWKRGLLRLL VLPLTMGIWI NGWLGEHHKN KKRKGGLETW HKKGTDIGLG QIPVDHLWCY
KKSKSL
