ENV_CAEVG
ID ENV_CAEVG Reviewed; 942 AA.
AC P31627;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 23-FEB-2022, entry version 107.
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 63) (CAEV-63).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11662;
OH NCBI_TaxID=9925; Capra hircus (Goat).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 81-95.
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 SEQUENCE REVISION.
RA Knowles D.P.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
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; M60855; AAB88709.2; -; mRNA.
DR PIR; A41307; VCLJC6.
DR PRIDE; P31627; -.
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 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Coiled coil; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Host cell membrane; Host membrane;
KW Host-virus interaction; Membrane; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Virion; Virus entry into host cell.
FT SIGNAL 1..80
FT /evidence="ECO:0000269|PubMed:1656067"
FT CHAIN 81..942
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239523"
FT CHAIN 81..630
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038691"
FT CHAIN 631..942
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038692"
FT TOPO_DOM 81..799
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 800..820
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 821..942
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 631..651
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 697..713
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 663..713
FT /evidence="ECO:0000255"
FT COILED 754..789
FT /evidence="ECO:0000255"
FT SITE 630..631
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 942 AA; 108437 MW; 5B0E1F0F3D355F4A CRC64;
MDAGASYMRL TGEENWVEVT MDEEKERKGK DVQQGKYRPQ VSKPIINRDT NTSFAYKGIF
LWGIQITMWI LLWTNMCVRA EDYITLISDP YGFSPIKNVS GVPVTCVTKE FARWGCQPLG
AYPDPEIEYR NVSQEIVKEV YQENWPWNTY HWPLWQMENV RYWLKENIAE NKKRKNSTKK
GIEELLAGTI RGRFCVPYPF ALLKCTKWCW YPAEIDQETG RARKIKINCT EARAVSCTEE
MPLASIHRAY WDEKDRESMA FMNIRACDSN LRCQKRPGGC VEGYPIPVGA NIIPENMKYL
RGQKSQYGGI KDKNGELKLP LTVRVWVKLA NVSTWVNGTP PYWQNRINGS KGINGTLWGQ
LSGMHHLGFN LSQTGKWCNY TGKIKIGQET FSYHYKPNWN CTGNWTQHPV WQVMRDLDMV
EHMTGECVQR PQRHNITVDR NQTITGNCSV TNWDGCNCSR SGNYLYNSTT GGLLVIICRN
NNTITGIMGT NTNWTTMWRI YRNCSGCENA TLDRKETGTL GGVANKNCSL PHKNESNKWT
CAPRQREGKT DSLYIAGGKK FWTREKAQYS CENNIGELDG MLHQQILLQK YQVIKVRAYT
YGVIEMPENY AKTRIINRRK RELSHTRKKR GVGLVIMLVI MAIVAAAGAS LGVANAIQQS
YTKAAVQTLA NATAAQQDAL EATYAMVQHV AKGVRILEAR VARVEAITDR IMLYQELDCW
HYHQYCVTST RADVAKYINW TRFKDNCTWQ QWERELQGYD GNLTMLLRES ARQTQLAEEQ
VRRIPDVWES LKEVFDWSGW FSWLKYIPII VVGLVGCILI RAVICVCQPL VQIYRTLSTP
TYQRVTVIME KRADVAGENQ DFGDGLEESD DSKTDQKVTV QKAWSRAWEL WQNSPWKEPW
KRSLLKLLIL PLTMGIWING RLGEHLKNKK ERVDCETWGK GD
