GAG_WDSV
ID GAG_WDSV Reviewed; 582 AA.
AC Q88937;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 75.
DE RecName: Full=Gag polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p10;
DE Short=MA;
DE Contains:
DE RecName: Full=RNA-binding phosphoprotein p20;
DE AltName: Full=pp12;
DE Contains:
DE RecName: Full=Capsid protein p25;
DE Short=CA;
DE Contains:
DE RecName: Full=Nucleocapsid protein p14;
DE Short=NC-gag;
GN Name=gag;
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], PROTEIN SEQUENCE OF 96-105; 252-266 AND
RP 458-467, AND PROTEOLYTIC PROCESSING OF 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.
CC -!- FUNCTION: [Matrix protein p10]: Targets Gag and gag-pol polyproteins to
CC the plasma membrane via a multipartite membrane binding signal, that
CC includes its myristoylated N-terminus. Also mediates nuclear
CC localization of the preintegration complex (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Capsid protein p25 forms the spherical core of the virion
CC that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
CC -!- FUNCTION: [Nucleocapsid protein p14]: Involved in the packaging and
CC encapsidation of two copies of the genome. Binds with high affinity to
CC conserved UCUG elements within the packaging signal, located near the
CC 5'-end of the genome. This binding is dependent on genome dimerization
CC (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Gag polyprotein]: Plays a role in budding and is processed
CC by the viral protease during virion maturation outside the cell.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Gag polyprotein]: Virion {ECO:0000250}. Host
CC cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p25]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000305}.
CC -!- PTM: Specific enzymatic cleavages by the viral protease yield mature
CC proteins. The protease is released by autocatalytic cleavage. The
CC polyprotein is cleaved during and after budding, this process is termed
CC maturation (By similarity). {ECO:0000250}.
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DR EMBL; L41838; AAA99526.1; -; Genomic_RNA.
DR EMBL; AF033822; AAC82607.1; -; Genomic_RNA.
DR RefSeq; NP_045938.1; NC_001867.1.
DR GeneID; 1403496; -.
DR KEGG; vg:1403496; -.
DR Proteomes; UP000007081; Genome.
DR Proteomes; UP000008337; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Capsid protein; Coiled coil; Direct protein sequencing; Host cell membrane;
KW Host membrane; Lipoprotein; Membrane; Metal-binding; Myristate;
KW Reference proteome; Viral nucleoprotein; Virion; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..582
FT /note="Gag polyprotein"
FT /id="PRO_0000410603"
FT CHAIN 2..95
FT /note="Matrix protein p10"
FT /id="PRO_0000410604"
FT CHAIN 96..251
FT /note="RNA-binding phosphoprotein p20"
FT /id="PRO_0000410605"
FT CHAIN 252..457
FT /note="Capsid protein p25"
FT /id="PRO_0000410606"
FT CHAIN 458..582
FT /note="Nucleocapsid protein p14"
FT /id="PRO_0000410607"
FT ZN_FING 501..518
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 168..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 154..185
FT /evidence="ECO:0000255"
FT COMPBIAS 168..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 95..96
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 251..252
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 457..458
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 582 AA; 65697 MW; CA5EF28EE38A3434 CRC64;
MGNSSSTPPP SALKNSDLFK TMLRTQYSGS VKTRRINQDI KKQYPLWPDQ GTCATKHWEQ
AVLIPLDSVS EETAKVLNFL RVKIQARKGE TARQMTAHTI KKLIVGTIDK NKQQTEILQK
TDESDEEMDT TNTMLFIARN KRERIAQQQQ ADLAAQQQVL LLQREQQREQ REKDIKKRDE
KKKKLLPDTT QKVEQTDIGE ASSSDASAQK PISTDNNPDL KVDGVLTRSQ HTTVPSNITI
KKDGTSVQYQ HPIRNYPTGE GNLTAQVRNP FRPLELQQLR KDCPALPEGI PQLAEWLTQT
MAIYNCDEAD VEQLARVIFP TPVRQIAGVI NGHAAANTAA KIQNYVTACR QHYPAVCDWG
TIQAFTYKPP QTAHEYVKHA EIIFKNNSGL EWQHATVPFI NMVVQGLPPK VTRSLMSGNP
DWSTKTIPQI IPLMQHYLNL QSRQDAKIKQ TPLVLQLAMP AQTMNGNKGY VGSYPTNEPY
YSFQQQQRPA PRAPPGNVPS NTCFFCKQPG HWKADCPNKT RNLRNMGNMG RGGRMGGPPY
RSQPYPAFIQ PPQNHQNQYN GRMDRSQLQA SAQEWLPGTY PA
