GAG_JSRV
ID GAG_JSRV Reviewed; 612 AA.
AC P31622; Q9WR75;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 23-FEB-2022, entry version 105.
DE RecName: Full=Gag polyprotein;
DE AltName: Full=Core polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p10;
DE Contains:
DE RecName: Full=Phosphorylated protein pp24;
DE Contains:
DE RecName: Full=p12;
DE Contains:
DE RecName: Full=Capsid protein p27;
DE Contains:
DE RecName: Full=Nucleocapsid protein p14;
DE Contains:
DE RecName: Full=p4;
GN Name=gag;
OS Sheep pulmonary adenomatosis virus (Jaagsiekte sheep retrovirus) (JSRV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11746;
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=JSRV-SA;
RX PubMed=1629959; DOI=10.1128/jvi.66.8.4930-4939.1992;
RA York D.F., Vigne R., Verwoerd D.W., Querat G.;
RT "Nucleotide sequence of the jaagsiekte retrovirus, an exogenous and
RT endogenous type D and B retrovirus of sheep and goats.";
RL J. Virol. 66:4930-4939(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=JSRV-21;
RX PubMed=10400795; DOI=10.1128/jvi.73.8.6964-6972.1999;
RA Palmarini M., Sharp J.M., de las Heras M., Fan H.;
RT "Jaagsiekte sheep retrovirus is necessary and sufficient to induce a
RT contagious lung cancer in sheep.";
RL J. Virol. 73:6964-6972(1999).
RN [3]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=24298557; DOI=10.1155/2013/984028;
RA Huang X., Cheng Q., Du Z.;
RT "A genome-wide analysis of RNA pseudoknots that stimulate efficient -1
RT ribosomal frameshifting or readthrough in animal viruses.";
RL Biomed. Res. Int. 2013:984028-984028(2013).
RN [4] {ECO:0007744|PDB:2V4X}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 257-388.
RC STRAIN=JSRV-21;
RX PubMed=19007792; DOI=10.1016/j.jmb.2008.10.066;
RA Mortuza G.B., Goldstone D.C., Pashley C., Haire L.F., Palmarini M.,
RA Taylor W.R., Stoye J.P., Taylor I.A.;
RT "Structure of the capsid amino-terminal domain from the betaretrovirus,
RT Jaagsiekte sheep retrovirus.";
RL J. Mol. Biol. 386:1179-1192(2009).
CC -!- FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.
CC -!- FUNCTION: [Nucleocapsid protein p14]: Nucleocapsid protein.
CC {ECO:0000305}.
CC -!- FUNCTION: [Capsid protein p27]: Capsid protein.
CC {ECO:0000250|UniProtKB:P07567}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag polyprotein;
CC IsoId=P31622-1; Sequence=Displayed;
CC Name=Gag-Pro polyprotein;
CC IsoId=P31625-1; Sequence=External;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P31623-1; Sequence=External;
CC -!- DOMAIN: [Gag polyprotein]: Late-budding domains (L domains) are short
CC sequence motifs essential for viral particle release. They can occur
CC individually or in close proximity within structural proteins. They
CC interacts with sorting cellular proteins of the multivesicular body
CC (MVB) pathway. Most of these proteins are class E vacuolar protein
CC sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes.
CC Gag-p12 contains two L domains: a PTAP/PSAP motif which interacts with
CC the UEV domain of TSG101, and a PPXY motif which binds to the WW
CC domains of the ubiquitin ligase NEDD4. Gag-p27 contains one L domain: a
CC PTAP/PSAP motif which interacts with the UEV domain of TSG101.
CC {ECO:0000250|UniProtKB:P07567}.
CC -!- PTM: [Gag polyprotein]: Myristoylated. Myristoylation of the matrix
CC (MA) domain mediates the transport and binding of Gag polyproteins to
CC the host plasma membrane and is required for the assembly of viral
CC particles. {ECO:0000250|UniProtKB:P10258}.
CC -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. {ECO:0000250|UniProtKB:P07567}.
CC -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC translation. {ECO:0000305|PubMed:24298557}.
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DR EMBL; M80216; AAA89180.1; -; Genomic_RNA.
DR EMBL; AF105220; AAD45224.1; -; Genomic_DNA.
DR PIR; A42740; FOMVJA.
DR RefSeq; NP_041184.1; NC_001494.1. [P31622-1]
DR PDB; 2V4X; X-ray; 1.50 A; A=257-388.
DR PDBsum; 2V4X; -.
DR SMR; P31622; -.
DR GeneID; 1490018; -.
DR KEGG; vg:1490018; -.
DR EvolutionaryTrace; P31622; -.
DR Proteomes; UP000007215; Genome.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.490; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR InterPro; IPR003322; B_retro_matrix.
DR InterPro; IPR038124; B_retro_matrix_sf.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_N.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF02337; Gag_p10; 1.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF57756; SSF57756; 2.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Coiled coil; Host-virus interaction;
KW Lipoprotein; Metal-binding; Myristate; Phosphoprotein; Repeat;
KW Ribosomal frameshifting; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral matrix protein;
KW Viral nucleoprotein; Viral release from host cell; Virion; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT CHAIN 2..612
FT /note="Gag polyprotein"
FT /id="PRO_0000443121"
FT CHAIN 2..99
FT /note="Matrix protein p10"
FT /id="PRO_0000040867"
FT CHAIN 100..?168
FT /note="Phosphorylated protein pp24"
FT /id="PRO_0000040868"
FT CHAIN ?169..256
FT /note="p12"
FT /id="PRO_0000040869"
FT CHAIN 257..477
FT /note="Capsid protein p27"
FT /id="PRO_0000040870"
FT CHAIN 478..579
FT /note="Nucleocapsid protein p14"
FT /id="PRO_0000040871"
FT CHAIN 580..612
FT /note="p4"
FT /id="PRO_0000040872"
FT ZN_FING 507..524
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 534..551
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 103..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 202..205
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000305"
FT MOTIF 208..211
FT /note="PPXY motif"
FT /evidence="ECO:0000305"
FT MOTIF 287..290
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000250|UniProtKB:P10258"
FT COMPBIAS 115..131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 99..100
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 129..130
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 168..169
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 256..257
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 477..478
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 579..580
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:P10258"
FT VARIANT 3
FT /note="H -> Q (in strain:JSRV-21)"
FT /evidence="ECO:0000269|PubMed:10400795"
FT VARIANT 28
FT /note="T -> P (in strain:JSRV-21)"
FT /evidence="ECO:0000269|PubMed:10400795"
FT VARIANT 116
FT /note="V -> G (in strain:JSRV-21)"
FT /evidence="ECO:0000269|PubMed:10400795"
FT VARIANT 139
FT /note="S -> L (in strain:JSRV-21)"
FT /evidence="ECO:0000269|PubMed:10400795"
FT VARIANT 193..197
FT /note="QLPSN -> SLPH (in strain:JSRV-21)"
FT /evidence="ECO:0000269|PubMed:10400795"
FT VARIANT 214
FT /note="T -> S (in strain:JSRV-21)"
FT /evidence="ECO:0000269|PubMed:10400795"
FT VARIANT 237
FT /note="K -> R (in strain:JSRV-21)"
FT /evidence="ECO:0000269|PubMed:10400795"
FT VARIANT 298
FT /note="S -> N (in strain:JSRV-21)"
FT /evidence="ECO:0000269|PubMed:10400795"
FT VARIANT 385
FT /note="K -> R (in strain:JSRV-21)"
FT /evidence="ECO:0000269|PubMed:10400795"
FT VARIANT 526..529
FT /note="HQTS -> QQGP (in strain:JSRV-21)"
FT /evidence="ECO:0000269|PubMed:10400795"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:2V4X"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:2V4X"
FT HELIX 272..284
FT /evidence="ECO:0007829|PDB:2V4X"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:2V4X"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:2V4X"
FT HELIX 319..343
FT /evidence="ECO:0007829|PDB:2V4X"
FT HELIX 349..353
FT /evidence="ECO:0007829|PDB:2V4X"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:2V4X"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:2V4X"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:2V4X"
FT HELIX 371..384
FT /evidence="ECO:0007829|PDB:2V4X"
SQ SEQUENCE 612 AA; 68089 MW; 4CC6803A033EEFCC CRC64;
MGHTHSRQLF VHMLSVMLKH RGITVSKTKL INFLSFIEEV CPWFPREGTV NLETWKKVGE
QIRTHYTLHG PEKVPVETLS FWTLIRDCLD FDNDELKRLG NLLKQEEDPL HTPDSVPSYD
PPPPPPPSLK MHPSDNDDSL SSTDEAELDE EAAKYHQEDW GFLAQEKGAL TSKDELVECF
KNLTIALQNA GIQLPSNNNT FPSAPPFPPA YTPTVMAGLD PPPGFPPPSK HMSPLQKALR
QAQRLGEVVS DFSLAFPVFE NNNQRYYESL PFKQLKELKI ACSQYGPTAP FTIAMIESLG
TQALPPNDWK QTARACLSGG DYLLWKSEFF EQCARIADVN RQQGIQTSYE MLIGEGPYQA
TDTQLNFLPG AYAQISNAAR QAWKKLPSSS TKTEDLSKVR QGPDEPYQDF VARLLDTIGK
IMSDEKAGMV LAKQLAFENA NSACQAALRP YRKKGDLSDF IRICADIGPS YMQGIAMAAA
LQGKSIKEVL FQQQARNKKG LQKSGNSGCF VCGQPGHRAA VCPQKHQTSV NTPNLCPRCK
KGKHWARDCR SKTDVQGNPL PPVSGNWVRG QPLAPKQCYG ATLQVPKEPL QTSVEPQEAA
RDWTSVPPPI QY
