ENV_WDSV
ID ENV_WDSV Reviewed; 1160 AA.
AC Q88938;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
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=env;
OS Walleye dermal sarcoma virus (WDSV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Epsilonretrovirus.
OX NCBI_TaxID=39720;
OH NCBI_TaxID=283036; Sander vitreus (Walleye) (Perca vitrea).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PROTEOLYTIC PROCESSING OF
RP POLYPROTEIN.
RX PubMed=7636975; DOI=10.1128/jvi.69.9.5320-5331.1995;
RA Holzschu D.L., Martineau D., Fodor S.K., Vogt V.M., Bowser P.R.,
RA Casey J.W.;
RT "Nucleotide sequence and protein analysis of a complex piscine retrovirus,
RT walleye dermal sarcoma virus.";
RL J. Virol. 69:5320-5331(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Chappey C.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE REVISION.
RX PubMed=17698670; DOI=10.1099/vir.0.82967-0;
RA Rovnak J., Casey R.N., Brewster C.D., Casey J.W., Quackenbush S.L.;
RT "Establishment of productively infected walleye dermal sarcoma explant
RT cells.";
RL J. Gen. Virol. 88:2583-2589(2007).
CC -!- FUNCTION: [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: [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 non-covalent interactions or by a labile
CC interchain disulfide bond. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host cell
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral
CC membrane protein. Host cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Note=The surface protein is not anchored to the
CC viral envelope, but associates with the extravirion surface through its
CC binding to TM. Both proteins are thought to be concentrated at the site
CC of budding and incorporated into the virions possibly by contacts
CC between the cytoplasmic tail of Env and the N-terminus of Gag (By
CC 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA99527.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors.; Evidence={ECO:0000305};
CC Sequence=AAC82608.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; L41838; AAA99527.1; ALT_SEQ; Genomic_RNA.
DR EMBL; AF033822; AAC82608.1; ALT_SEQ; Genomic_RNA.
DR PIR; T09395; T09395.
DR RefSeq; NP_045939.1; NC_001867.1.
DR GeneID; 1403498; -.
DR KEGG; vg:1403498; -.
DR Proteomes; UP000007081; Genome.
DR Proteomes; UP000008337; 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:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
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;
KW Fusion of virus membrane with host cell membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1160
FT /note="Envelope glycoprotein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000410600"
FT CHAIN 34..468
FT /note="Surface protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000410601"
FT CHAIN 469..1160
FT /note="Transmembrane protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000410602"
FT TOPO_DOM 23..853
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 854..874
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 875..1048
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1049..1069
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1070..1127
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1128..1148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1149..1160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 230..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
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 148
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 664
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1160 AA; 130922 MW; 7D6D50DC022AFD73 CRC64;
MDTPGSLQVI AIISLLLVGG ASQPATFLEK ALPTDGPSLE TIEHKTEMVN TTRSEEQSPV
RPSKTRQQLI DETPEICANA WVIRLITEFP TELGNMSQKQ KTIAIQVHNT TMTMEETVFS
LVSHVNKKNY EIHNVSGICT KYQLVPGNFT CSTRKCISQT KEKRIISTTV KDTYEVYLPF
AWSQKPTGGD KYPEPQIGYN TGTGRLNQWN KDEFVIKQCR KKRGKRQITV PNSTLSPTGT
TDFTKFTPNP ISPNSTALNE LEQKTTPIGT EQPFNNEKWQ NLIFGNIVTK MDPQCEAELF
QQFNISDKTV QVEFKVTSLP GQNISCQAIY NTEHGINIEN KNCVISLIKE NRKIKAHAYI
TRTGSYEWYA QQVTSKGIIQ EVRNLVTIVE CECPIVKPLP QGGIIPLTMP MRVLTNPSPI
LIHSALKFDL SKFGLSPCSF SPMEWQTYIT KPLKRAMHGF EVHQRKKRDL GIGLHSTLNS
WWNGANSLGL TVESADRQKY DQKILKVLQN LAVQQRTDVK NQQTLGKALE TPIYTITLQL
ADSLTAAILK HEQQQNVGIT CKDIAILTVT QIATYLRDIQ HEHLPVWFIE QITNQILLPV
GQVIMPEITA PPILNPLIGW NQSVLVIGLT HQLTITTVQQ PLYKAANMGN FQDWTPFPPF
ILANKTHGFS IDCPIMRNSF LCHTLPTPVK LSEWERSTST IYQTSPQVWI TPEGKACLNH
RNITVQDRTC LINKPGCFIP KHPWSAGKQT IVPTQYIQQN FVPDTIDTED NQTRVLQKEM
IEAISKAKRD YGVLKQGQIA LIRHHEAITT ILGQEATYSI KETQALISSI EQEAWYNNLF
SWYDGSVWSQ LQLIIVVITC TIPLLWVLNT CLFFKLRRAI RRERDNNIVV EYQAQTRGRR
THMTEPITKK QRAKLLRHAK TNRRLPRSLR ATPAVSAFEM VTFDPQEETV EINRIDPSHE
NNDHGGPMNM APIISADSYA LPTPYITIML DRELLNQGMR KVITLLNDPA REVFNKAYNL
VTTNHFTLAY GCDESAGWVN QHAEYMGKPV IVTLAGLVIT PVGLAWIPLP QQEPLEKLFM
VPNSMPHVTV AMADYHETKE MGKIVKDINN EELLLVKPQL FKWGPEGFFV ACPLVIRGVV
TGHSLLHIAC PATAVQAEGT
